{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T10:56:16Z","timestamp":1790765776839,"version":"4.1.0"},"reference-count":412,"publisher":"MDPI AG","issue":"5","license":[{"start":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T00:00:00Z","timestamp":1684368000000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"German Research Foundation","award":["DFG TRR296"],"award-info":[{"award-number":["DFG TRR296"]}]},{"name":"German Research Foundation","award":["TRR152"],"award-info":[{"award-number":["TRR152"]}]},{"name":"German Research Foundation","award":["SFB1123"],"award-info":[{"award-number":["SFB1123"]}]},{"name":"German Research Foundation","award":["GRK 2816\/1"],"award-info":[{"award-number":["GRK 2816\/1"]}]},{"name":"German Research Foundation","award":["101044445"],"award-info":[{"award-number":["101044445"]}]},{"name":"German Center for Diabetes Research (DZD e.V.)","award":["DFG TRR296"],"award-info":[{"award-number":["DFG TRR296"]}]},{"name":"German Center for Diabetes Research (DZD e.V.)","award":["TRR152"],"award-info":[{"award-number":["TRR152"]}]},{"name":"German Center for Diabetes Research (DZD e.V.)","award":["SFB1123"],"award-info":[{"award-number":["SFB1123"]}]},{"name":"German Center for Diabetes Research (DZD e.V.)","award":["GRK 2816\/1"],"award-info":[{"award-number":["GRK 2816\/1"]}]},{"name":"German Center for Diabetes Research (DZD e.V.)","award":["101044445"],"award-info":[{"award-number":["101044445"]}]},{"name":"European Research Council ERC-CoG Trusted","award":["DFG TRR296"],"award-info":[{"award-number":["DFG TRR296"]}]},{"name":"European Research Council ERC-CoG Trusted","award":["TRR152"],"award-info":[{"award-number":["TRR152"]}]},{"name":"European Research Council ERC-CoG Trusted","award":["SFB1123"],"award-info":[{"award-number":["SFB1123"]}]},{"name":"European Research Council ERC-CoG Trusted","award":["GRK 2816\/1"],"award-info":[{"award-number":["GRK 2816\/1"]}]},{"name":"European Research Council ERC-CoG Trusted","award":["101044445"],"award-info":[{"award-number":["101044445"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Biomolecules"],"abstract":"<jats:p>Glycosylphosphatidylinositol (GPI)-anchored proteins (APs) are anchored at the outer leaflet of plasma membranes (PMs) of all eukaryotic organisms studied so far by covalent linkage to a highly conserved glycolipid rather than a transmembrane domain. Since their first description, experimental data have been accumulating for the capability of GPI-APs to be released from PMs into the surrounding milieu. It became evident that this release results in distinct arrangements of GPI-APs which are compatible with the aqueous milieu upon loss of their GPI anchor by (proteolytic or lipolytic) cleavage or in the course of shielding of the full-length GPI anchor by incorporation into extracellular vesicles, lipoprotein-like particles and (lyso)phospholipid- and cholesterol-harboring micelle-like complexes or by association with GPI-binding proteins or\/and other full-length GPI-APs. In mammalian organisms, the (patho)physiological roles of the released GPI-APs in the extracellular environment, such as blood and tissue cells, depend on the molecular mechanisms of their release as well as the cell types and tissues involved, and are controlled by their removal from circulation. This is accomplished by endocytic uptake by liver cells and\/or degradation by GPI-specific phospholipase D in order to bypass potential unwanted effects of the released GPI-APs or their transfer from the releasing donor to acceptor cells (which will be reviewed in a forthcoming manuscript).<\/jats:p>","DOI":"10.3390\/biom13050855","type":"journal-article","created":{"date-parts":[[2023,5,18]],"date-time":"2023-05-18T08:09:44Z","timestamp":1684397384000},"page":"855","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":35,"title":["(Patho)Physiology of Glycosylphosphatidylinositol-Anchored Proteins I: Localization at Plasma Membranes and Extracellular Compartments"],"prefix":"10.3390","volume":"13","author":[{"given":"G\u00fcnter A.","family":"M\u00fcller","sequence":"first","affiliation":[{"name":"Institute for Diabetes and Obesity (IDO), Helmholtz Diabetes Center (HDC) at Helmholtz Zentrum M\u00fcnchen, German Research Center for Environmental Health (GmbH), Ingolst\u00e4dter Landstra\u00dfe 1, 85764 Oberschleissheim, Germany"},{"name":"German Center for Diabetes Research (DZD), 85764 Oberschleissheim, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-0624-9339","authenticated-orcid":false,"given":"Timo D.","family":"M\u00fcller","sequence":"additional","affiliation":[{"name":"Institute for Diabetes and Obesity (IDO), Helmholtz Diabetes Center (HDC) at Helmholtz Zentrum M\u00fcnchen, German Research Center for Environmental Health (GmbH), Ingolst\u00e4dter Landstra\u00dfe 1, 85764 Oberschleissheim, Germany"},{"name":"German Center for Diabetes Research (DZD), 85764 Oberschleissheim, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2023,5,18]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"741","DOI":"10.1006\/jmbi.1999.3069","article-title":"Prediction of potential GPI-modification sites in proprotein sequences","volume":"292","author":"Eisenhaber","year":"1999","journal-title":"J. Mol. Biol."},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1093\/protein\/14.1.17","article-title":"Post-translational GPI lipid anchor modification of proteins in kingdoms of life: Analysis of protein sequence data from complete genomes","volume":"14","author":"Eisenhaber","year":"2001","journal-title":"Protein Eng."},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S1672-0229(07)60022-9","article-title":"FragAnchor: A large-scale predictor of glycosylphosphatidylinositol anchors in eukaryote protein sequences by qualitative scoring","volume":"5","author":"Poisson","year":"2007","journal-title":"Genom. Proteom. Bioinform."},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"4963","DOI":"10.1016\/S0021-9258(18)89166-9","article-title":"Trypanosoma brucei variant surface glycoprotein has a sn-1,2-dimyristyl glycerol membrane anchor at its COOH terminus","volume":"260","author":"Ferguson","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"4969","DOI":"10.1016\/S0021-9258(18)89167-0","article-title":"Acylation of a Plasmodium falciparum merozoite surface antigen via sn-1,2-diacyl glycerol","volume":"260","author":"Haldar","year":"1985","journal-title":"J. Biol. Chem."},{"key":"ref_6","doi-asserted-by":"crossref","first-page":"16955","DOI":"10.1016\/S0021-9258(17)44853-8","article-title":"Structure of the glycosyl-phosphatidylinositol membrane anchor of the Leishmania major Promastigote surface protease","volume":"265","author":"Schneider","year":"1990","journal-title":"J. Biol. Chem."},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1126\/science.3340856","article-title":"Glycosyl-phosphatidylinositol moiety that anchors Trypanosoma brucei variant surface glycoprotein to the membrane","volume":"239","author":"Ferguson","year":"1988","journal-title":"Science"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"e54352","DOI":"10.15252\/embr.202154352","article-title":"Ethanolamine-phosphate on the second mannose is a preferential bridge for some GPI-anchored proteins","volume":"23","author":"Ishida","year":"2022","journal-title":"EMBO Rep."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"285","DOI":"10.1146\/annurev.bi.57.070188.001441","article-title":"Cell-surface anchoring of proteins via glycosylphosphatidylinositol structure","volume":"57","author":"Ferguson","year":"1988","journal-title":"Ann. Rev. Biochem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1146\/annurev.bi.62.070193.001005","article-title":"The structure and biosynthesis of glycosyl phosphatidylinositol protein anchors","volume":"62","author":"Englund","year":"1993","journal-title":"Ann. Rev. Biochem."},{"key":"ref_11","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1194\/jlr.R700002-JLR200","article-title":"Thematic review series: Lipid posttranslational modifications. GPI anchoring of protein in yeast and mammalian cells, or: How we learned to stop worrying and love glycophospholipids","volume":"48","author":"Orlean","year":"2007","journal-title":"J. Lipid Res."},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"1050","DOI":"10.1016\/j.bbalip.2012.01.004","article-title":"GPI-anchor remodeling: Potential functions of GPI-anchors in intracellular trafficking and membrane dynamics","volume":"1821","author":"Fujita","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_13","doi-asserted-by":"crossref","unstructured":"Nakano, M., Sabido-Bozo, S., Okazaki, K., Aguilera-Romero, A., Rodriguez-Gallardo, S., Cortes-Gomez, A., Lopez, S., Ikeda, A., Funato, K., and Muniz, M. (2021). Structural analysis of the GPI glycan. PLoS ONE, 16.","DOI":"10.1371\/journal.pone.0257435"},{"key":"ref_14","doi-asserted-by":"crossref","unstructured":"Aguilera-Romero, A., Sabido-Bozo, S., Lopez, S., Cortes-Gomez, A., Rodriguez-Gallardo, S., Perez-Linero, A.M., Riezman, I., Riezman, H., Funato, K., and Goder, V. (2021). Determination of the lipid composition of the GPI anchor. PLoS ONE, 16.","DOI":"10.1371\/journal.pone.0256184"},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/j.molcel.2016.06.012","article-title":"Automated structure- and sequence-based design of proteins for high bacterial expression and stability","volume":"63","author":"Goldenzweig","year":"2016","journal-title":"Mol. Cell"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"19","DOI":"10.1111\/jnc.13992","article-title":"Recent developments in structural studies on acetylcholinesterase","volume":"142","author":"Silman","year":"2017","journal-title":"J. Neurochem."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"18573","DOI":"10.1016\/S0021-9258(19)37000-0","article-title":"Glycan components in the glycoinositol phospholipid anchor of human erythrocyte acetylcholinesterase. Novel fragments produced by trifluoroacetic acid","volume":"267","author":"Deeg","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_18","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1016\/j.cub.2014.11.039","article-title":"COPII coat composition is actively regulated by luminal cargo maturation","volume":"25","author":"Martin","year":"2015","journal-title":"Curr. Biol."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"3375","DOI":"10.1091\/mbc.e14-06-1033","article-title":"Cdc1 removes the ethanolamine phosphate of the first mannose of GPI anchors and thereby facilitates the integration of GPI proteins into yeast cell wall","volume":"25","author":"Vazquez","year":"2014","journal-title":"Mol. Biol. Cell"},{"key":"ref_20","unstructured":"Taylor, D.R., and Hooper, N.M. (2011). Post-Translational Modifications in Health and Disease, Springer."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"32744","DOI":"10.1074\/jbc.M110.137588","article-title":"Binding of Toxoplasma gondii glycosylphosphatidylinositols to galectin-3 is required for their recognition by macrophages","volume":"285","author":"Niehus","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"999","DOI":"10.1016\/S1286-4579(02)01617-9","article-title":"VSG-GPI anchors of African trypanosomes: Their role in macrophage activation and induction of infection-associated immunopathology","volume":"4","author":"Magez","year":"2002","journal-title":"Microb. Infect."},{"key":"ref_23","first-page":"933","article-title":"The importance of side branches of glycosylphosphatidylinositol anchors: A molecular dynamics perspective","volume":"32","author":"Banerjee","year":"2022","journal-title":"Glycobiology"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"101153","DOI":"10.1016\/j.jbc.2021.101153","article-title":"A Trypanosoma brucei \u00df3 glycosyltransferase superfamily gene encodes a \u00df1-6 GlcNAc-transferase mediating N-glycan and GPI anchor modification","volume":"297","author":"Duncan","year":"2021","journal-title":"J. Biol. Chem."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"190290","DOI":"10.1098\/rsob.190290","article-title":"Biosynthesis and biology of mammalian GPI-anchored proteins","volume":"10","author":"Kinoshita","year":"2020","journal-title":"Open Biol."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"1129","DOI":"10.1042\/BST20191142","article-title":"Mammalian GPI-anchor modifications and the enzymes involved","volume":"48","author":"Liu","year":"2020","journal-title":"Biochem. Soc. Trans."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"777","DOI":"10.1038\/s42003-021-02337-1","article-title":"A knockout cell library of GPI biosynthetic genes for functional studies of GPI-anchored proteins","volume":"4","author":"Liu","year":"2021","journal-title":"Commun. Biol."},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1038\/s41594-022-00726-6","article-title":"Structure of human glycosylphosphatidylinositol transamidase","volume":"29","author":"Zhang","year":"2022","journal-title":"Nat. Struct. Mol. Biol."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"960","DOI":"10.1002\/1873-3468.14048","article-title":"Subunits of the GPI transamidase complex localize to the endoplasmic reticulum and nuclear envelope in Drosophila","volume":"595","author":"Kawaguchi","year":"2021","journal-title":"FEBS Lett."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1038\/s41467-022-30250-6","article-title":"Molecular insights into biogenesis of glycosylphosphatidylinositol anchor proteins","volume":"13","author":"Xu","year":"2022","journal-title":"Nat. Commun."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1194\/jlr.R063313","article-title":"Biosynthesis of GPI-anchored proteins: Special emphasis on GPI lipid remodeling","volume":"57","author":"Kinoshita","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Liu, S.-S., Jin, F., Liu, Y.-S., Murakami, Y., Sugita, Y., Kato, T., Gao, X.-D., Kinoshita, T., Hattori, M., and Fujita, M. (2021). Functional analysis of the GPI transamidase complex by screening for amino acid mutations in each subunit. Molecules, 26.","DOI":"10.3390\/molecules26185462"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1021\/acs.biochem.2c00196","article-title":"A soluble, minimalistic glycosylphosphatidylinositol transamidase (GPI-T) retains transamidation activity","volume":"61","author":"Ness","year":"2022","journal-title":"Biochemistry"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"102444","DOI":"10.1016\/j.jbc.2022.102444","article-title":"ER entry pathway and glycosylation of GPI-anchored proteins are determined by N-terminal signal sequence and C-terminal GPI-attachment sequence","volume":"298","author":"Hirata","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"16399","DOI":"10.1074\/jbc.M112.350009","article-title":"Efficient glycosylphosphatidylinositol (GPI) modification of membrane proteins requires a C-terminal anchoring signal of marginal hydrophobicity","volume":"287","author":"Galian","year":"2012","journal-title":"J. Biol. Chem."},{"key":"ref_36","doi-asserted-by":"crossref","first-page":"1846","DOI":"10.1093\/bioinformatics\/bti299","article-title":"Identification of GPI anchor attachment signals by a Kohonen self-organizing map","volume":"21","author":"Fankhauser","year":"2005","journal-title":"Bioinformatics"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"4025","DOI":"10.1016\/j.cub.2021.06.078","article-title":"Post-ER degradation of misfolded GPI-anchored proteins is linked with microautophagy","volume":"31","author":"Lemus","year":"2021","journal-title":"Curr. Biol."},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1083\/jcb.201602010","article-title":"Limited ER quality control for GPI-anchored proteins","volume":"213","author":"Sikorska","year":"2016","journal-title":"J. Cell Biol."},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"e202208159","DOI":"10.1083\/jcb.202208159","article-title":"Accumulated precursors of specific GPI-anchored proteins upregulate GPI biosynthesis with ARV1","volume":"222","author":"Liu","year":"2023","journal-title":"J. Cell Biol."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"522","DOI":"10.1016\/j.cell.2014.06.026","article-title":"ER stress-induced clearance of misfolded GPI-anchored proteins via the secretory pathway","volume":"158","author":"Ajinkya","year":"2014","journal-title":"Cell"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"675","DOI":"10.1111\/tra.12761","article-title":"Tracking exocytosis of a GPI-anchored protein in Aspergillus nidulans","volume":"21","author":"Penalva","year":"2020","journal-title":"Traffic"},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"1134","DOI":"10.1016\/j.cell.2013.02.003","article-title":"A network of cytosolic factors targets SRP-independent proteins to the endoplasmic reticulum","volume":"152","author":"Ast","year":"2013","journal-title":"Cell"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"15860","DOI":"10.1074\/jbc.M314051200","article-title":"The surface coat of the mammal-dwelling infective trypomastigote stage of Trypanosoma cruzi is formed by highly diverse immunogenic mucins","volume":"279","author":"Buscaglia","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"12201","DOI":"10.1074\/jbc.M412939200","article-title":"Structural characterization of NETNES, a novel glycoconjugate in Trypanosoma cruzi epimastigotes","volume":"280","author":"Macrae","year":"2005","journal-title":"J. Biol. Chem."},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3335","DOI":"10.1021\/ac0517949","article-title":"Isolation and characterization of glycosylphosphatidylinositol-anchored peptides by hydrophilic interaction chromatography and MALDI tandem mass spectrometry","volume":"78","author":"Omaetxebarria","year":"2006","journal-title":"Anal. Chem."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1038\/msb.2009.13","article-title":"GPIomics: Global analysis of glycosylphosphatidylinositol-anchored molecules of Trypanosoma cruzi","volume":"5","author":"Nakayasu","year":"2009","journal-title":"Mol. Syst. Biol."},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"4204","DOI":"10.1074\/jbc.M311995200","article-title":"Apolipoprotein B production reduces lipotoxic cardiomyopathy: Studies in heart-specific lipoprotein lipase transgenic mouse","volume":"279","author":"Yokoyama","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"446","DOI":"10.3109\/10409238.2013.831024","article-title":"GPI transamidase and GPI anchored proteins: Oncogenes and biomarkers for cancer","volume":"48","author":"Gamage","year":"2013","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"834","DOI":"10.1091\/mbc.e05-05-0443","article-title":"Inositol deacylation by Bst1p is required for the quality control of glycosylphosphatidylinositol-anchored proteins","volume":"17","author":"Fujita","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2636","DOI":"10.1091\/mbc.e06-02-0104","article-title":"GUP1 of Saccharomyces cerevisiae encodes an O-acetyltransferase involved in remodeling of the GPI anchor","volume":"17","author":"Bosson","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"1493","DOI":"10.1111\/j.1365-2958.2007.05883.x","article-title":"CWH43 is required for the introduction of ceramides into GPI anchors in Saccharomyces cerevisiae","volume":"65","author":"Ghugtyal","year":"2007","journal-title":"Mol. Microbiol."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"4304","DOI":"10.1091\/mbc.e07-05-0482","article-title":"Saccharomyces cerevisiae CWH43 is involved in the remodeling of the lipid moiety of GPI anchors to ceramides","volume":"18","author":"Umemura","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"eaba8237","DOI":"10.1126\/sciadv.aba8237","article-title":"Ceramide chain length-dependent protein sorting into selective endoplasmic reticulum exit sites","volume":"6","author":"Kurokawa","year":"2020","journal-title":"Sci. Adv."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"110768","DOI":"10.1016\/j.celrep.2022.110768","article-title":"Quality-controlled ceramide-based GPI-anchored protein sorting into selective ER exit sites","volume":"39","author":"Ikeda","year":"2022","journal-title":"Cell Rep."},{"key":"ref_55","doi-asserted-by":"crossref","unstructured":"Lopez, S., Perez-Linero, A.M., Manzano-Lopez, J., Sabido-Bozo, S., Cortes-Gomez, A., Rodriguez-Gallardo, S., Aguilera-Romero, A., Goder, V., and Muniz, M. (2020). Dual independent roles of the p24 complex in selectivity of secretory cargo export from the endoplasmic reticulum. Cells, 9.","DOI":"10.3390\/cells9051295"},{"key":"ref_56","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1083\/jcb.201012074","article-title":"Sorting of GPI-anchored proteins into ER exit sites by p24 proteins dependent on remodeled GPI","volume":"194","author":"Fujita","year":"2011","journal-title":"J. Cell Biol."},{"key":"ref_57","doi-asserted-by":"crossref","unstructured":"Lopez, S., Rodriguez-Gallardo, S., Sabido-Bozo, S., and Muniz, M. (2019). Endoplasmic reticulum export of GPI-anchored proteins. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20143506"},{"key":"ref_58","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1016\/j.cell.2009.08.040","article-title":"GPI glycan remodeling by PGAP5 regulates transport of GPI-anchored proteins from the ER to the Golgi","volume":"139","author":"Fujita","year":"2009","journal-title":"Cell"},{"key":"ref_59","doi-asserted-by":"crossref","first-page":"5253","DOI":"10.1091\/mbc.e06-08-0715","article-title":"PER1 is required for GPI-phospholipase A2 activity and involved in lipid remodeling of GPI-anchored proteins","volume":"17","author":"Fujita","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_60","doi-asserted-by":"crossref","first-page":"1410","DOI":"10.1091\/mbc.e05-11-1005","article-title":"PGAP2 is essential for correct processing and stable expression of GPI-anchored proteins","volume":"17","author":"Tashima","year":"2006","journal-title":"Mol. Biol. Cell"},{"key":"ref_61","doi-asserted-by":"crossref","first-page":"352","DOI":"10.1194\/jlr.R062760","article-title":"Trafficking of glycosylphosphatidylinositol anchored proteins from the endoplasmic reticulum to the cell surface","volume":"57","author":"Muniz","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_62","doi-asserted-by":"crossref","first-page":"2145","DOI":"10.1083\/jcb.109.5.2145","article-title":"A glycophospholipid membrane anchor acts as an apical targeting signal in polarized epithelial cells","volume":"109","author":"Lisanti","year":"1989","journal-title":"J. Cell Biol."},{"key":"ref_63","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1016\/0092-8674(92)90189-J","article-title":"Sorting of GPI-anchored proteins to glycolipid-enriched membrane subdomains during transport to the apical surface","volume":"68","author":"Brown","year":"1992","journal-title":"Cell"},{"key":"ref_64","first-page":"85","article-title":"Membrane traffic in polarized neurons in culture","volume":"17","author":"Dotti","year":"1993","journal-title":"J. Cell Sci. Suppl."},{"key":"ref_65","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1083\/jcb.200507116","article-title":"GPI-anchored proteins are directly targeted to the apical surface in fully polarized MDCK cells","volume":"172","author":"Paladino","year":"2006","journal-title":"J. Cell Biol."},{"key":"ref_66","doi-asserted-by":"crossref","first-page":"269","DOI":"10.1016\/bs.ctm.2015.03.006","article-title":"Trafficking and membrane organization of GPI-anchored proteins in health and diseases","volume":"75","author":"Paladino","year":"2015","journal-title":"Curr. Top. Membr."},{"key":"ref_67","doi-asserted-by":"crossref","first-page":"1497","DOI":"10.1091\/mbc.e06-10-0885","article-title":"Fatty acid remodeling of GPI-anchored proteins is required for their raft association","volume":"18","author":"Maeda","year":"2007","journal-title":"Mol. Biol. Cell"},{"key":"ref_68","doi-asserted-by":"crossref","first-page":"313","DOI":"10.1083\/jcb.146.2.313","article-title":"N-glycans mediate the apical sorting of a GPI-anchored, rat-associated protein in Madin-Darby canine kidney cells","volume":"146","author":"Benting","year":"1999","journal-title":"J. Cell Biol."},{"key":"ref_69","doi-asserted-by":"crossref","first-page":"31632","DOI":"10.1074\/jbc.274.44.31632","article-title":"Carboxypeptidase M, a glycosylphosphatidylinositol-anchored protein, is localized on both the apical and basolateral domains of polarized Madin-Darby canine kidney cells","volume":"274","author":"McGwire","year":"1999","journal-title":"J. Biol. Chem."},{"key":"ref_70","doi-asserted-by":"crossref","first-page":"810","DOI":"10.1034\/j.1600-0854.2002.31106.x","article-title":"PrPC is sorted to the basolateral membrane of epithelial cells independently of its association with rafts","volume":"3","author":"Sarnataro","year":"2002","journal-title":"Traffic"},{"key":"ref_71","doi-asserted-by":"crossref","first-page":"2351","DOI":"10.1002\/1873-3468.13573","article-title":"Clustering in the Golgi apparatus governs sorting and function of GPI-APs in polarized epithelial cells","volume":"593","author":"Lebreton","year":"2019","journal-title":"FEBS Lett."},{"key":"ref_72","doi-asserted-by":"crossref","first-page":"632","DOI":"10.1016\/j.bbamem.2015.12.018","article-title":"Glycosylphosphatidylinositol-anchored proteins: Membrane organization anf transport","volume":"1858","author":"Zurzolo","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_73","first-page":"G54","article-title":"Mechanism of folate transport across the human colonic basolateral membrane","volume":"281","author":"Dudeja","year":"2001","journal-title":"Am. J. Physiol. Liver Physiol."},{"key":"ref_74","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1076\/ceyr.24.2.129.8167","article-title":"Transcellular transfer of folate across the retinal pigment epithelium","volume":"24","author":"Bridges","year":"2002","journal-title":"Curr. Eye Res."},{"key":"ref_75","doi-asserted-by":"crossref","first-page":"912","DOI":"10.1016\/j.ymthe.2019.02.013","article-title":"The GPI-linked protein LY6A drives AAV-PHP.B transport across the blood-brain barrier","volume":"27","author":"Hordeaux","year":"2019","journal-title":"Mol. Ther."},{"key":"ref_76","doi-asserted-by":"crossref","first-page":"92","DOI":"10.1159\/000316642","article-title":"Oral protein therapy for the future? Transport of glycolipid-modified therapeutic proteins","volume":"86","year":"2010","journal-title":"Pharmacology"},{"key":"ref_77","doi-asserted-by":"crossref","first-page":"10193","DOI":"10.1016\/S0021-9258(17)34042-5","article-title":"A conditionally lethal yeast mutant blocked at the first step in glycosyl phosphatidylinositol anchor synthesis","volume":"269","author":"Leidlich","year":"1994","journal-title":"J. Biol. Chem."},{"key":"ref_78","doi-asserted-by":"crossref","first-page":"10336","DOI":"10.1073\/pnas.180230697","article-title":"Critical roles of glycosylphosphatidylinositol for Trypanosoma brucei","volume":"97","author":"Nagamune","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_79","doi-asserted-by":"crossref","first-page":"229","DOI":"10.1105\/tpc.014407","article-title":"SETH1 and SETH2, two components of the glycosylphosphatidylinositol anchor biosynthetic pathway, are required for pollen germination and tube growth in Arabidopsis","volume":"16","author":"Lallanne","year":"2004","journal-title":"Plant Cell"},{"key":"ref_80","doi-asserted-by":"crossref","first-page":"1128","DOI":"10.1105\/tpc.105.031815","article-title":"Glycosylphosphatidylinositol-anchored proteins are required for cell wall synthesis and morphogenesis in Arabidopsis","volume":"17","author":"Gillmor","year":"2005","journal-title":"Plant Cell"},{"key":"ref_81","first-page":"293","article-title":"Developmental abnormalities of glycosylphosphatidylinositol-anchor-deficient embryos revealed by Cre\/loxP system","volume":"79","author":"Nozaki","year":"1999","journal-title":"Lab. Investig."},{"key":"ref_82","doi-asserted-by":"crossref","first-page":"2825","DOI":"10.1182\/blood-2004-02-0671","article-title":"GPI-anchor deficiency in myeloid cells causes impaired Fc\u03b3R effector functions","volume":"104","author":"Hazenbos","year":"2004","journal-title":"Blood"},{"key":"ref_83","doi-asserted-by":"crossref","first-page":"4377","DOI":"10.1182\/blood-2011-02-338053","article-title":"Impaired Fc\u03b5R1 stability, signaling and effector functions in murine mast cells lacking glycosylphosphatidylinositol-anchored proteins","volume":"118","author":"Hazenbos","year":"2011","journal-title":"Blood"},{"key":"ref_84","doi-asserted-by":"crossref","first-page":"30373","DOI":"10.1074\/jbc.M705601200","article-title":"PGAP1 knock-out mice show otocephaly and male infertility","volume":"282","author":"Ueda","year":"2007","journal-title":"J. Biol. Chem."},{"key":"ref_85","doi-asserted-by":"crossref","first-page":"7400","DOI":"10.1073\/pnas.94.14.7400","article-title":"Tissue specific knock-out of the mouse Pig-a gene reveals important roles for GPI-anchored proteins in skin development","volume":"94","author":"Tarutani","year":"1997","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_86","doi-asserted-by":"crossref","first-page":"101720","DOI":"10.1016\/j.jbc.2022.101720","article-title":"Loss of the N-acetylgalactosamine side chain of the GPI-anchor impairs bone formation and brain functions and accelerates the prion disease pathology","volume":"298","author":"Hirata","year":"2022","journal-title":"J. Biol. Chem."},{"key":"ref_87","doi-asserted-by":"crossref","first-page":"3600","DOI":"10.1182\/blood.V87.9.3600.bloodjournal8793600","article-title":"Glycosylphosphatidylinositol-anchor-deficient mice: Implications for clonal dominance of mutant cells in paroxysmal nocturnal hemoglobinuria","volume":"87","author":"Kawagoe","year":"1996","journal-title":"Blood"},{"key":"ref_88","first-page":"255","article-title":"Paroxysmal nocturnal hemoglobinuria: Insights from recent advances in molecular biology","volume":"15","author":"Bessler","year":"2001","journal-title":"Transfus. Med. Rev."},{"key":"ref_89","doi-asserted-by":"crossref","first-page":"2607","DOI":"10.1002\/1521-4141(200209)32:9<2607::AID-IMMU2607>3.0.CO;2-H","article-title":"Glycosylphosphatidylinositol-linked proteins are required for maintenance of a normal peripheral lymphoid compartment but not for lymphocyte development","volume":"32","author":"Bessler","year":"2002","journal-title":"Eur. J. Immunol."},{"key":"ref_90","doi-asserted-by":"crossref","first-page":"846","DOI":"10.1038\/nm1410","article-title":"Hypomorphic promoter mutation in PIGM causes inherited glycosylphosphatidylinositol deficiency","volume":"12","author":"Almeida","year":"2006","journal-title":"Nat. Med."},{"key":"ref_91","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1038\/ng.653","article-title":"Identity-by-descent filtering of exome sequence data identifies PIGV mutations in hyperphosphatasia mental retardation syndrome","volume":"42","author":"Krawitz","year":"2010","journal-title":"Nat. Genet."},{"key":"ref_92","doi-asserted-by":"crossref","first-page":"383","DOI":"10.1136\/jmg.2010.087114","article-title":"Multiple congenital anomalies-hypotonia-seizures syndrome is caused by a mutation in PIGN","volume":"48","author":"Maydan","year":"2011","journal-title":"J. Med. Genet."},{"key":"ref_93","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1038\/s41398-018-0359-4","article-title":"Abnormal ER quality control of neural GPI-anchored proteins via dysfunction in ER export processing in the frontal cortex of elderly subjects with schizophrenia","volume":"9","author":"Kim","year":"2019","journal-title":"Transl. Psychiatry"},{"key":"ref_94","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1002\/humu.23426","article-title":"A PIGH mutation leading to GPI deficiency is associated with developmental delay and autism","volume":"39","author":"Nguyen","year":"2018","journal-title":"Hum. Mutat."},{"key":"ref_95","doi-asserted-by":"crossref","first-page":"602","DOI":"10.1016\/j.ajhg.2018.08.014","article-title":"Mutations in PIGS, encoding a GPI transamidase, cause a neurological syndrome ranging from fetal akinesia to epileptic encephalopathy","volume":"103","author":"Nguyen","year":"2018","journal-title":"Am. J. Hum. Genet."},{"key":"ref_96","doi-asserted-by":"crossref","first-page":"259","DOI":"10.1007\/s10048-020-00615-4","article-title":"A defect in GPI synthesis as a suggested mechanism for the role of ARV1 in intellectual disability and seizures","volume":"21","author":"Segel","year":"2020","journal-title":"Case Rep. Neurogenet."},{"key":"ref_97","doi-asserted-by":"crossref","first-page":"40","DOI":"10.1186\/s13023-020-1313-0","article-title":"Significantly different clinical phenotypes associated with mutations in synthesis and transamidase + remodeling glycosylphosphatidylinositol (GPI)-anchor biosynthesis genes","volume":"15","author":"Carmody","year":"2020","journal-title":"Orphanet J. Rare Dis."},{"key":"ref_98","doi-asserted-by":"crossref","first-page":"3660","DOI":"10.1182\/blood.2020009810","article-title":"Inherited glycosylphosphatidylinositol defects cause the rare EMM-negative blood phenotype and developmental disorders","volume":"137","author":"Duval","year":"2021","journal-title":"Blood"},{"key":"ref_99","doi-asserted-by":"crossref","first-page":"e01686-16","DOI":"10.1128\/JVI.01686-16","article-title":"PrP knockout cells expressing transmembrane PrP resist prion infection","volume":"91","author":"Marshall","year":"2017","journal-title":"J. Virol."},{"key":"ref_100","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bbrc.2016.11.036","article-title":"Anchorless forms of prion protein\u2014Impact of truncation on structure destabilization and prion protein conversion","volume":"481","author":"Kovac","year":"2016","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_101","doi-asserted-by":"crossref","first-page":"2473","DOI":"10.1016\/j.bbamcr.2013.01.027","article-title":"Transport of glycosylphosphatidylinositol-anchored proteins from the endoplasmic reticulum","volume":"1833","author":"Kinoshita","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_102","doi-asserted-by":"crossref","first-page":"403","DOI":"10.1080\/10409238.2018.1485627","article-title":"Organization of GPI-anchored proteins at the cell surface and its physiopathological relevance","volume":"53","author":"Lebreton","year":"2018","journal-title":"Crit. Rev. Biochem. Mol. Biol."},{"key":"ref_103","doi-asserted-by":"crossref","first-page":"112","DOI":"10.1111\/cge.13425","article-title":"Clinical variability in inherited glycosylphosphatidylinositol deficiency disorders","volume":"95","author":"Nguyen","year":"2019","journal-title":"Clin. Genet."},{"key":"ref_104","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1242\/dev.000166","article-title":"Nodal signaling: Developmental roles and regulation","volume":"134","author":"Shen","year":"2007","journal-title":"Development"},{"key":"ref_105","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.bbrc.2010.10.128","article-title":"Intercellular transfer regulation of the paracrine activity of GPI-anchored Cripto-1 as a Nodal co-receptor","volume":"403","author":"Watanabe","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_106","doi-asserted-by":"crossref","first-page":"51","DOI":"10.1016\/j.semcancer.2014.08.003","article-title":"The multifaceted role of the embryonic gene Cripto-1 in cancer, stem cells and epithelial-mesenchymal transition","volume":"29","author":"Klauzinska","year":"2014","journal-title":"Semin. Cancer Biol."},{"key":"ref_107","doi-asserted-by":"crossref","first-page":"1231","DOI":"10.1089\/hum.1994.5.10-1231","article-title":"Purified GPI-anchored CD4DAF as a receptor for HIV-mediated gene transfer","volume":"5","author":"Brodsky","year":"1994","journal-title":"Hum. Gene Ther."},{"key":"ref_108","doi-asserted-by":"crossref","first-page":"1144","DOI":"10.1160\/TH15-01-0079","article-title":"Cell painting with an engineered EPCR to augment the protein C system","volume":"114","author":"Bouwens","year":"2015","journal-title":"Thromb. Haemost."},{"key":"ref_109","doi-asserted-by":"crossref","first-page":"173","DOI":"10.3389\/fcell.2018.00173","article-title":"Thy-1, a pathfinder protein for the post-genomic era","volume":"6","author":"Morris","year":"2018","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_110","doi-asserted-by":"crossref","first-page":"2763","DOI":"10.1021\/bi00553a035","article-title":"Lipid dynamics and lipid-protein interactions in rat enterocyte basolateral and microvillus membranes","volume":"19","author":"Brasitus","year":"1980","journal-title":"Biochemistry"},{"key":"ref_111","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1139\/o85-130","article-title":"Reconstitution of lymphocyte 5\u2032-nucleotidase in lipid bilayers: Behaviour and interaction with concanavalin A","volume":"63","author":"Sharom","year":"1985","journal-title":"Can. J. Biochem. Cell Biol."},{"key":"ref_112","doi-asserted-by":"crossref","first-page":"1398","DOI":"10.1021\/bi011579w","article-title":"PI-specific phospholipase C cleavage of a reconstituted GPI-anchored protein: Modulation by the lipid bilayer","volume":"41","author":"Lehto","year":"2002","journal-title":"Biochemistry"},{"key":"ref_113","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1242\/jcs.108.2.487","article-title":"The glycophosphatidylinositol anchor affects the conformation of Thy-1 protein","volume":"108","author":"Barboni","year":"1995","journal-title":"J. Cell Sci."},{"key":"ref_114","doi-asserted-by":"crossref","first-page":"41","DOI":"10.1016\/0960-9822(91)90123-E","article-title":"Dropping anchor with the lipophosphoglycans","volume":"1","author":"Rademacher","year":"1991","journal-title":"Curr. Biol."},{"key":"ref_115","doi-asserted-by":"crossref","first-page":"798","DOI":"10.1038\/29563","article-title":"GPI-anchored proteins are organized in submicron domains at the cell surface","volume":"394","author":"Varma","year":"1998","journal-title":"Nature"},{"key":"ref_116","doi-asserted-by":"crossref","first-page":"1085","DOI":"10.1016\/j.cell.2008.11.032","article-title":"Nanoclusters of GPI-anchored proteins are formed by cortical actin-driven activity","volume":"135","author":"Goswami","year":"2008","journal-title":"Cell"},{"key":"ref_117","doi-asserted-by":"crossref","first-page":"111","DOI":"10.1146\/annurev.cellbio.14.1.111","article-title":"Functions of lipid rafts in biological membranes","volume":"14","author":"Brown","year":"1998","journal-title":"Annu. Rev. Cell. Dev. Biol."},{"key":"ref_118","doi-asserted-by":"crossref","first-page":"969","DOI":"10.1038\/nmeth.1704","article-title":"Probing protein heterogeneity in the plasma membrane using PALM and pair correlation analysis","volume":"8","author":"Sengupta","year":"2011","journal-title":"Nat. Methods"},{"key":"ref_119","doi-asserted-by":"crossref","first-page":"1814","DOI":"10.1016\/j.febslet.2010.02.047","article-title":"Hierarchical organization of the plasma membrane: Investigations by single-molecule tracking vs. fluorescence correlation spectroscopy","volume":"584","author":"Kusumi","year":"2010","journal-title":"FEBS Lett."},{"key":"ref_120","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1007\/s00424-007-0409-x","article-title":"Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM","volume":"456","author":"Giocondi","year":"2008","journal-title":"Pfl\u00fcgers Arch. Eur. J. Physiol."},{"key":"ref_121","doi-asserted-by":"crossref","first-page":"C459","DOI":"10.1152\/ajpcell.00355.2016","article-title":"Caveolins and cavins in the trafficking, maturation, and degradation of caveolae: Implications for cell physiology","volume":"312","author":"Busija","year":"2017","journal-title":"Am. J. Physiol. Cell Physiol."},{"key":"ref_122","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.ceb.2017.02.014","article-title":"The caveolae dress code: Structure and signaling","volume":"47","author":"Lamaze","year":"2017","journal-title":"Curr. Opin. Cell Biol."},{"key":"ref_123","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1126\/science.1174621","article-title":"Lipid rafts as a membrane-organizing principle","volume":"327","author":"Lingwood","year":"2010","journal-title":"Science"},{"key":"ref_124","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1016\/j.cell.2015.03.048","article-title":"Transbilayer lipid interactions mediate nanoclustering of lipid-anchored proteins","volume":"161","author":"Raghupathy","year":"2015","journal-title":"Cell"},{"key":"ref_125","doi-asserted-by":"crossref","first-page":"6969","DOI":"10.1038\/ncomms7969","article-title":"GPI-anchored proteins do not reside in ordered domains in the live cell plasma membrane","volume":"6","author":"Seycsik","year":"2015","journal-title":"Nat. Commun."},{"key":"ref_126","doi-asserted-by":"crossref","first-page":"159","DOI":"10.1194\/jlr.R062885","article-title":"GPI-anchored protein organization and dynamics at the cell surface","volume":"57","author":"Saha","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_127","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1016\/j.cell.2015.04.008","article-title":"Membrane Nanoclusters\u2014Tails of the unexpected","volume":"161","author":"Sezgin","year":"2015","journal-title":"Cell"},{"key":"ref_128","doi-asserted-by":"crossref","first-page":"1042","DOI":"10.1038\/nprot.2012.059","article-title":"Elucidating membrane structure and protein behavior using giant plasma membrane vesicles","volume":"7","author":"Sezgin","year":"2012","journal-title":"Nat. Protoc."},{"key":"ref_129","first-page":"636","article-title":"Glycosylphosphatidylinositol-anchored proteins as regulators of cortical cytoskeleton","volume":"81","author":"Sharonov","year":"2016","journal-title":"Biochemistry"},{"key":"ref_130","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1002\/pro.3874","article-title":"Toward a new picture of the living plasma membrane","volume":"29","author":"Kalappurakkal","year":"2020","journal-title":"Protein Sci."},{"key":"ref_131","doi-asserted-by":"crossref","first-page":"e112030","DOI":"10.15252\/embj.2022112030","article-title":"Plasma membrane topography governs the 3D dynamic localization of IgM B cell antigen receptor clusters","volume":"42","author":"Saltukoglu","year":"2023","journal-title":"EMBO J."},{"key":"ref_132","doi-asserted-by":"crossref","first-page":"720536","DOI":"10.3389\/fcell.2021.720536","article-title":"The glycosylphosphatidyl anchor: A linchpin for cell surface versatility of Trypanosomatids","volume":"9","author":"Borges","year":"2021","journal-title":"Front. Cell Dev. Biol."},{"key":"ref_133","doi-asserted-by":"crossref","first-page":"93","DOI":"10.1186\/1423-0127-16-93","article-title":"Endocytosis of glycosylphosphatidylinositol-anchored proteins","volume":"16","author":"Lakhan","year":"2009","journal-title":"J. Biomed. Sci."},{"key":"ref_134","doi-asserted-by":"crossref","unstructured":"Chaudhary, N., Gomez, G.A., Howes, M.T., Lo, H.P., McMahon, K.-A., Rae, J.A., Schieber, N.L., Hill, M.M., Gaus, K., and Yap, A.S. (2014). Endocytic crosstalk: Cavins, caveolins, and caveolae regulate clathrin-independent endocytosis. PLoS Biol., 12.","DOI":"10.1371\/journal.pbio.1001832"},{"key":"ref_135","doi-asserted-by":"crossref","first-page":"704","DOI":"10.1111\/febs.13625","article-title":"Dynamics of internalization and recycling of the prometastatic membrane type 4 matrix metalloproteinase (MT4-MMP) in breast cancer cells","volume":"283","author":"Truong","year":"2016","journal-title":"FEBS J."},{"key":"ref_136","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1016\/j.tcb.2017.11.004","article-title":"Mechanisms of carrier formation during clathrin-independent endocytosis","volume":"28","author":"Ferreira","year":"2018","journal-title":"Trends Cell Biol."},{"key":"ref_137","doi-asserted-by":"crossref","first-page":"3542","DOI":"10.1091\/mbc.e04-02-0151","article-title":"Characterization of a nonclathrin endocytic pathway: Membrane cargo and lipid requirements","volume":"15","author":"Naslavsky","year":"2004","journal-title":"Mol. Biol. Cell"},{"key":"ref_138","doi-asserted-by":"crossref","first-page":"4391","DOI":"10.2147\/IJN.S164866","article-title":"Rho GTPases in A549 and Caco-2 cells dominating the endocytic pathways of nanocarbons with different morphologies","volume":"13","author":"Song","year":"2018","journal-title":"Int. J. Nanomed."},{"key":"ref_139","doi-asserted-by":"crossref","first-page":"702","DOI":"10.1111\/j.1600-0854.2007.00565.x","article-title":"Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway","volume":"8","author":"Chadda","year":"2007","journal-title":"Traffic"},{"key":"ref_140","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1083\/jcb.200609061","article-title":"Early endosomes associated with dynamic F-actin structures are required for late trafficking of H. pylori VacA toxin","volume":"177","author":"Gauthier","year":"2007","journal-title":"J. Cell Biol."},{"key":"ref_141","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/j.yexcr.2016.04.009","article-title":"GRP75 upregulates clathrin-independent endocytosis through actin cytoskeleton reorganization mediated by the concurrent activation of Cdc42 and RhoA","volume":"343","author":"Chen","year":"2016","journal-title":"Exp. Cell Res."},{"key":"ref_142","doi-asserted-by":"crossref","first-page":"3373","DOI":"10.1242\/jcs.00637","article-title":"shibire mutations reveal distinct dynamin-independent and -dependent endocytic pathways in primary cultures of Drosophila hemocytes","volume":"116","author":"Guha","year":"2003","journal-title":"J. Cell Sci."},{"key":"ref_143","doi-asserted-by":"crossref","unstructured":"M\u00fcller, G.A., and M\u00fcller, T.D. (2023). Transfer of proteins from cultured human adipose to blood cells and induction of anabolic phenotype are controlled by serum, insulin and sulfonylurea drugs. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24054825"},{"key":"ref_144","doi-asserted-by":"crossref","first-page":"427","DOI":"10.1016\/0304-4157(89)90014-2","article-title":"The glycosyl-phosphatidylinositol anchor of membrane proteins","volume":"988","author":"Low","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_145","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1006\/smim.1994.1012","article-title":"How GPI-anchored proteins turnover: Or where do they go after arrival at the plasma membrane","volume":"6","author":"Censullo","year":"1994","journal-title":"Semin. Immunol."},{"key":"ref_146","doi-asserted-by":"crossref","first-page":"268","DOI":"10.1126\/science.3276003","article-title":"Structural and functional roles of glycosylphosphatidylinositol in membranes","volume":"239","author":"Low","year":"1988","journal-title":"Science"},{"key":"ref_147","doi-asserted-by":"crossref","first-page":"6991","DOI":"10.1021\/bi8006324","article-title":"The glycosylphosphatidylinositol anchor: A complex membrane-anchoring structure for proteins","volume":"47","author":"Paulik","year":"2008","journal-title":"Biochemistry"},{"key":"ref_148","doi-asserted-by":"crossref","first-page":"457","DOI":"10.1038\/332457a0","article-title":"Induction of the proteolytic activity of a membrane protein in Plasmodium falciparum by phosphatidyl inositol-specific phospholipase C","volume":"332","author":"Rosenberry","year":"1988","journal-title":"Nature"},{"key":"ref_149","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1016\/0014-5793(93)80873-S","article-title":"The human sperm protein PH-20 has hyaluronidase activity","volume":"336","author":"Gmachl","year":"1993","journal-title":"FEBS Lett."},{"key":"ref_150","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1042\/bj3030633","article-title":"Activation of the glycosyl-phosphatidylinositol-anchored membrane dipeptidase upon release from pig kidney membranes by phospholipase C","volume":"303","author":"Brewis","year":"1994","journal-title":"Biochem. J."},{"key":"ref_151","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1042\/bj3320101","article-title":"Release of the glycosylphosphatidylinositol-anchored enzyme ecto-5\u2032-nucleotidase by phospholipase C: Catalytic activation and modulation by the lipid bilayer","volume":"332","author":"Lehto","year":"1998","journal-title":"Biochem. J."},{"key":"ref_152","doi-asserted-by":"crossref","first-page":"1245","DOI":"10.1016\/S0021-9258(18)48421-9","article-title":"Effect of glycoinositolphospholipid anchor lipid groups on functional properties of decay-accelerating factor protein in cells","volume":"267","author":"Walter","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_153","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1083\/jcb.116.4.997","article-title":"Micromanipulation of adhesion of a Jurkat cell to a planar bilayer membrane containing lymphocyte function-associated antigen 3 molecules","volume":"116","author":"Tozeren","year":"1992","journal-title":"J. Cell Biol."},{"key":"ref_154","doi-asserted-by":"crossref","first-page":"504","DOI":"10.1006\/abbi.1994.1071","article-title":"Lipolytic membrane release of two phosphatidylinositol-anchored cAMP receptor proteins in yeast alters their ligand-binding parameters","volume":"308","author":"Bandlow","year":"1994","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_155","doi-asserted-by":"crossref","first-page":"16305","DOI":"10.1021\/bi961098q","article-title":"Variant GPI structure in relation to membrane-associated functions of a murine folate receptor","volume":"35","author":"Wang","year":"1996","journal-title":"Biochemistry"},{"key":"ref_156","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1042\/BJ20141488","article-title":"Soluble CD109 binds TGF-\u00df and antagonizes TGF-\u00df signalling and responses","volume":"473","author":"Li","year":"2016","journal-title":"Biochem. J."},{"key":"ref_157","doi-asserted-by":"crossref","first-page":"1477","DOI":"10.1002\/(SICI)1097-0061(199712)13:15<1477::AID-YEA184>3.0.CO;2-L","article-title":"In silico identification of glycosyl-phosphatidylinositol-anchored plasma-membrane and cell wall proteins of Saccharomyces cerevisiae","volume":"13","author":"Caro","year":"1997","journal-title":"Yeast"},{"key":"ref_158","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1016\/S0304-4165(98)00137-8","article-title":"The contribution of cell wall proteins to the organisation of the yeast cell wall","volume":"1426","author":"Kapteyn","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_159","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1002\/yea.1349","article-title":"Cell wall construction in Saccharomyces cerevisiae","volume":"23","author":"Klis","year":"2006","journal-title":"Yeast"},{"key":"ref_160","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0304-4165(99)00012-4","article-title":"Structure of the glucan-binding sugar chain of Tip1p, a cell wall protein of Saccharomyces cerevisiae","volume":"1427","author":"Fujii","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_161","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1016\/S0304-4165(98)00138-X","article-title":"The Gas1 glycoprotein, a putative wall polymer cross-linker","volume":"1426","author":"Popolo","year":"1999","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_162","doi-asserted-by":"crossref","first-page":"442","DOI":"10.1128\/MCB.16.1.442","article-title":"Glucose-induced sequential processing of a glycosyl-phosphatidylinositol-anchored ectoprotein in Saccharomyces cerevisiae","volume":"16","author":"Wied","year":"1996","journal-title":"Mol. Cell. Biol."},{"key":"ref_163","doi-asserted-by":"crossref","first-page":"3104","DOI":"10.1128\/jb.177.11.3104-3110.1995","article-title":"Identification of three mannoproteins in the cell wall of Saccharomyces cerevisiae","volume":"177","author":"Caro","year":"1995","journal-title":"J. Bacteriol."},{"key":"ref_164","doi-asserted-by":"crossref","first-page":"2202","DOI":"10.1128\/jb.179.7.2202-2209.1997","article-title":"Restrictive glycosylphosphatidylinositol anchor synthesis in cwh6\/gpi3 yeast cells causes aberrant biogenesis of cell wall proteins","volume":"179","author":"Vossen","year":"1997","journal-title":"J. Bacteriol."},{"key":"ref_165","doi-asserted-by":"crossref","first-page":"3886","DOI":"10.1128\/JB.181.13.3886-3889.1999","article-title":"Amino acid residues in the omega-minus region participate in cellular localization of yeast glycosylphosphatidylinositol-attached proteins","volume":"181","author":"Hamada","year":"1999","journal-title":"J. Bacteriol."},{"key":"ref_166","doi-asserted-by":"crossref","first-page":"880","DOI":"10.1111\/gtc.12636","article-title":"Lipid moiety of glycosylphosphatidylinositol-anchored proteins contributes to the determination of their final destination in yeast","volume":"23","author":"Umemura","year":"2018","journal-title":"Genes Cells"},{"key":"ref_167","doi-asserted-by":"crossref","first-page":"1011","DOI":"10.1046\/j.1365-2958.2002.03244.x","article-title":"Two homologous genes, DCW1 (YKL046c) and DFG5, are essential for cell growth and encode glycosylphosphatidylinositol (GPI)-anchored membrane proteins required for cell wall biogenesis in Saccharomyces cerevisiae","volume":"46","author":"Kitagaki","year":"2002","journal-title":"Mol. Microbiol."},{"key":"ref_168","doi-asserted-by":"crossref","first-page":"247","DOI":"10.1046\/j.1365-2958.1999.01585.x","article-title":"A constitutive role for GPI anchors in Saccharomyces cerevisiae: Cell wall targeting","volume":"34","author":"Bourdineaud","year":"1999","journal-title":"Mol. Microbiol."},{"key":"ref_169","doi-asserted-by":"crossref","first-page":"140","DOI":"10.1111\/mmi.12175","article-title":"Determination and physiological roles of the glycosylphosphatidylinositol lipid remodelling pathway in yeast","volume":"88","author":"Ichikawa","year":"2013","journal-title":"Mol. Microbiol."},{"key":"ref_170","doi-asserted-by":"crossref","first-page":"2396","DOI":"10.1016\/j.bbapap.2013.05.006","article-title":"Colon tumour secretopeptidome: Insights into endogenous proteolytic cleavage events in the colon tumour microenvironment","volume":"1834","author":"Greening","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_171","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1111\/febs.12654","article-title":"Endoproteolytic processing of the mammalian prion glycoprotein family","volume":"281","author":"Mays","year":"2014","journal-title":"FEBS Lett."},{"key":"ref_172","doi-asserted-by":"crossref","first-page":"2494","DOI":"10.2741\/3392","article-title":"Multiple activities of a multifaceted receptor: Roles of cleaved and soluble uPAR","volume":"14","author":"Montuori","year":"2009","journal-title":"Front. Biosci."},{"key":"ref_173","doi-asserted-by":"crossref","first-page":"6368","DOI":"10.1158\/0008-5472.CAN-07-6768","article-title":"Tumor-associated MICA is shed by ADAM proteases","volume":"68","author":"Waldhauer","year":"2008","journal-title":"Cancer Res."},{"key":"ref_174","doi-asserted-by":"crossref","first-page":"8543","DOI":"10.1074\/jbc.M109.045906","article-title":"Differential mechanisms of shedding of the glycosylphosphatidylinositol (GPI)-anchored NKG2D ligands","volume":"285","author":"Ashiru","year":"2010","journal-title":"J. Biol. Chem."},{"key":"ref_175","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1006\/bbrc.2000.4090","article-title":"Mechanism of release of urinary Tamm-Horsfall glycoprotein from the kidney GPI-anchored counterpart","volume":"280","author":"Cavallone","year":"2001","journal-title":"Biochim. Biophys. Res. Commun."},{"key":"ref_176","doi-asserted-by":"crossref","first-page":"85","DOI":"10.1016\/0166-6851(89)90132-1","article-title":"Release of the variant surface glycoprotein during differentiation of bloodstream to procyclic forms of Trypanosoma brucei","volume":"32","author":"Overath","year":"1989","journal-title":"Mol. Biochem. Parasitol."},{"key":"ref_177","doi-asserted-by":"crossref","first-page":"113","DOI":"10.1023\/A:1014806916844","article-title":"Regulation of ecto-5\u2032-nucleotidase by TNF-alpha in human endothelial cells","volume":"232","author":"Kalsi","year":"2002","journal-title":"Mol. Cell. Biochem."},{"key":"ref_178","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1083\/jcb.136.2.421","article-title":"Differential regulation and function of CD73, a glycosyl-phosphatidylinositol-linked 70-kD adhesion molecule, on lymphocytes and endothelial cells","volume":"136","author":"Airas","year":"1997","journal-title":"J. Cell. Biol."},{"key":"ref_179","doi-asserted-by":"crossref","first-page":"27315","DOI":"10.1074\/jbc.M113.484212","article-title":"Soluble ecto-5\u2032-nucleotidase (5\u2032-NT), alkaline phosphatase, and adenosine deaminase (ADA1) activities in neonatal blood favor elevated extracellular adenosine","volume":"288","author":"Pettengill","year":"2013","journal-title":"J. Biol. Chem."},{"key":"ref_180","first-page":"e23649","article-title":"Negative regulation of urokinase receptor activity by a GPI-specific phospholipase C in breast cancer cells","volume":"6pii","author":"Kedziora","year":"2017","journal-title":"eLife"},{"key":"ref_181","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1172\/JCI113636","article-title":"Release of carcinoembryonic antigen from human colon cancer cells by phosphatidylinositol-specific phospholipase C","volume":"82","author":"Sack","year":"1988","journal-title":"J. Clin. Investig."},{"key":"ref_182","doi-asserted-by":"crossref","first-page":"339","DOI":"10.1042\/bj3530339","article-title":"Endogenous glycosylphosphatidylinositol-specific phospholipase C releases renal dipeptidase from kidney proximal tubules in vitro","volume":"353","author":"Park","year":"2001","journal-title":"Biochem. J."},{"key":"ref_183","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1159\/000049429","article-title":"Glycosyl-phosphatidylinositol (GPI)-anchored renal dipeptidase is released by a phospholipase C in vivo","volume":"25","author":"Park","year":"2002","journal-title":"Kidney Blood Press. Res."},{"key":"ref_184","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1007\/978-94-017-7197-9_9","article-title":"TNAP, an essential player in membrane lipid rafts of neuronal cells","volume":"Volume 76","author":"Ermonval","year":"2015","journal-title":"Neuronal Tissue-Nonspecific Alkaline Phosphatase (TNAP); Subcellular Biochemistry"},{"key":"ref_185","doi-asserted-by":"crossref","first-page":"325","DOI":"10.1007\/s00418-016-1449-0","article-title":"GAS1 is present in the cerebrospinal fluid and is expressed in the choroid plexus of the adult rat","volume":"146","author":"Estudillo","year":"2016","journal-title":"Histochem. Cell Biol."},{"key":"ref_186","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1186\/1742-2094-11-115","article-title":"Glimepiride reduces CD14 expression and cytokine secretion from macrophages","volume":"11","author":"Ingham","year":"2014","journal-title":"J. Neuroinflamm."},{"key":"ref_187","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0304-4157(97)00005-1","article-title":"Mammalian GPI proteins: Sorting, membrane residence and functions","volume":"1331","author":"Nosjean","year":"1997","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_188","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1016\/0014-5793(86)80476-8","article-title":"The membrane-anchoring systems of vertebrate acetylcholinesterase and variant surface glycoproteins of African trypanosomes share a common antigenic determinant","volume":"199","author":"Stieger","year":"1986","journal-title":"FEBS Lett."},{"key":"ref_189","doi-asserted-by":"crossref","first-page":"18766","DOI":"10.1016\/S0021-9258(18)37349-6","article-title":"Lipid analysis of the glycoinositol phospholipid membrane anchor of human erythrocyte acetylcholinesterase. Palmitoylation of inositol results in resistance to phosphatidylinositol-specific phospholipase C","volume":"263","author":"Roberts","year":"1988","journal-title":"J. Biol. Chem."},{"key":"ref_190","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1006\/abio.1994.1264","article-title":"The detection of phospholipase-resistant and -sensitive glycosyl-phosphatidylinositol membrane anchors by western blotting","volume":"219","author":"Guther","year":"1994","journal-title":"Anal. Biochem."},{"key":"ref_191","doi-asserted-by":"crossref","first-page":"13820","DOI":"10.1016\/S0021-9258(19)85176-1","article-title":"Sphingolipid deficiency induces hypersensitivity of CD14, a glycosyl phosphatidylinositol-anchored protein, to phosphatidylinositol-specific phospholipase C","volume":"268","author":"Hanada","year":"1993","journal-title":"J. Biol. Chem."},{"key":"ref_192","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1007\/BF02976358","article-title":"Conversion of glycosylphosphatidylinositol (GPI)-anchored alkaline phosphatase by GPI-PLD","volume":"22","author":"Moon","year":"1999","journal-title":"Arch. Pharm. Res."},{"key":"ref_193","doi-asserted-by":"crossref","first-page":"1275","DOI":"10.1083\/jcb.114.6.1275","article-title":"Phospholipase C release of basic fibroblast growth factor from human bone marrow cultures as a biologically active complex with a phosphatidylinositol-anchored heparan sulfate proteoglycan","volume":"114","author":"Brunner","year":"1991","journal-title":"J. Cell Biol."},{"key":"ref_194","doi-asserted-by":"crossref","first-page":"2115","DOI":"10.1182\/blood.V83.8.2115.2115","article-title":"An endogenous glycosylphosphatidylinositol-specific phospholipase D releases basic fibroblast growth factor-heparan sulfate proteoglycan complexes from human bone marrow cultures","volume":"83","author":"Brunner","year":"1994","journal-title":"Blood"},{"key":"ref_195","doi-asserted-by":"crossref","first-page":"12149","DOI":"10.1021\/bi00206a018","article-title":"Membrane association of lipoprotein lipase and a cAMP-binding ectoprotein in rat adipocytes","volume":"33","author":"Wetekam","year":"1994","journal-title":"Biochemistry"},{"key":"ref_196","doi-asserted-by":"crossref","first-page":"3157","DOI":"10.1016\/j.bbamem.2016.09.022","article-title":"Differential subcellular distribution of four phospholipase C isoforms and secretion of GPI-PLC activity","volume":"1858","author":"Staudt","year":"2016","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_197","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1016\/j.bbamem.2011.10.009","article-title":"Selective and programmed cleavage of GPI-anchored proteins from the surface membrane by phospholipase C","volume":"1818","author":"Simon","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_198","doi-asserted-by":"crossref","first-page":"548","DOI":"10.1016\/j.ccell.2016.08.016","article-title":"Glycerophosphodiesterase GDE2 promotes neuroblastome differentiation through glypican release and is a marker of clinical outcome","volume":"30","author":"Koster","year":"2016","journal-title":"Cancer Cell"},{"key":"ref_199","first-page":"388","article-title":"Neuronal differentiation through GPI-anchor cleavage","volume":"16","author":"Moolenaar","year":"2016","journal-title":"Cell Cycle"},{"key":"ref_200","doi-asserted-by":"crossref","first-page":"1670","DOI":"10.1126\/science.241.4873.1670","article-title":"Insulin-stimulated release of lipoprotein lipase by metabolism of its phosphatidylinositol anchor","volume":"241","author":"Chan","year":"1988","journal-title":"Science"},{"key":"ref_201","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1126\/science.3282305","article-title":"Phosphatidylinositol-glycan anchors of membrane proteins: Potential precursors of insulin mediators","volume":"240","author":"Romero","year":"1988","journal-title":"Science"},{"key":"ref_202","doi-asserted-by":"crossref","first-page":"531","DOI":"10.1042\/bj3260531","article-title":"Insulin stimulates the release of the glycosylphosphatidylinositol-anchored membrane dipeptidase from 3T3-L1 adipocytes through the action of a phospholipase C","volume":"326","author":"Movahedi","year":"1997","journal-title":"Biochem. J."},{"key":"ref_203","doi-asserted-by":"crossref","first-page":"509","DOI":"10.1042\/bj2890509","article-title":"The sulphonylurea drug, glimepiride, stimulates release of glycosylphosphatidylinositol-anchored plasma-membrane proteins from 3T3 adipocytes","volume":"289","author":"Dearey","year":"1993","journal-title":"Biochem. J."},{"key":"ref_204","doi-asserted-by":"crossref","first-page":"1267","DOI":"10.1083\/jcb.126.5.1267","article-title":"Stimulation of a glycosylphosphatidylinositol-specific phospholipase by insulin and the sulfonylurea, glimepiride, in rat adipocytes depends on increased glucose transport","volume":"126","author":"Dearey","year":"1994","journal-title":"J. Cell Biol."},{"key":"ref_205","doi-asserted-by":"crossref","first-page":"761","DOI":"10.1016\/j.bcp.2004.11.014","article-title":"Regulation of lipid raft proteins by glimepiride- and insulin-induced glycosylphosphatidylinositol-specific phospholipase C in rat adipocytes","volume":"69","author":"Schulz","year":"2005","journal-title":"Biochem. Pharmacol."},{"key":"ref_206","doi-asserted-by":"crossref","first-page":"945","DOI":"10.1007\/s000180050485","article-title":"Signalling via caveolin: Involvement in the cross-talk between phosphoinositolglycans and insulin","volume":"56","author":"Frick","year":"1999","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_207","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1016\/S0014-5793(02)03402-6","article-title":"Dynamics of plasma membrane microdomains and cross-talk to the insulin signalling cascade","volume":"531","year":"2002","journal-title":"FEBS Lett."},{"key":"ref_208","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/j.devcel.2004.08.005","article-title":"Opposing activities of Dally-like glypican at high and low levels of Wingless morphogen activity","volume":"7","author":"Kreuger","year":"2004","journal-title":"Dev. Cell"},{"key":"ref_209","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1042\/BJ20070511","article-title":"Mammalian Notum induces the release of glypicans and other GPI-anchored proteins from the cell surface","volume":"410","author":"Traister","year":"2007","journal-title":"Biochem. J."},{"key":"ref_210","doi-asserted-by":"crossref","first-page":"81","DOI":"10.1126\/science.2443973","article-title":"A glycan-phosphatidylinositol-specific phospholipase D in human serum","volume":"238","author":"Davitz","year":"1987","journal-title":"Science"},{"key":"ref_211","doi-asserted-by":"crossref","first-page":"980","DOI":"10.1073\/pnas.85.4.980","article-title":"A phospholipase D specific for the phosphatidylinositol anchor of cell-surface proteins is abundant in plasma","volume":"85","author":"Low","year":"1988","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_212","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1111\/j.1432-1033.1991.tb15883.x","article-title":"Enzymatic properties of phosphatidylinositol-glycan-specific phospholipase C from rat liver and phosphatidylinositol-glycan-specific phospholipase D from rat serum","volume":"197","author":"Stieger","year":"1991","journal-title":"Eur. J. Biochem."},{"key":"ref_213","doi-asserted-by":"crossref","first-page":"275","DOI":"10.1016\/j.biochi.2004.04.003","article-title":"Genetic regulation of mouse glycosylphosphatidylinositol-phospholipase D","volume":"86","author":"Kieszkievicz","year":"2004","journal-title":"Biochimie"},{"key":"ref_214","doi-asserted-by":"crossref","first-page":"747","DOI":"10.1111\/j.1432-1033.1992.tb16981.x","article-title":"Phosphatidylinositol-glycan-specific phospholipase D is an amphiphilic glycoprotein that in serum is associated with high density lipoproteins","volume":"206","author":"Hoener","year":"1992","journal-title":"Eur. J. Biochem."},{"key":"ref_215","doi-asserted-by":"crossref","first-page":"109","DOI":"10.1016\/0005-2736(92)90073-U","article-title":"A novel form of glycosylphosphatidylinositol-anchor converting activity with a specificity of a phospholipase D in mammalian liver membranes","volume":"1109","author":"Heller","year":"1992","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_216","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1042\/bj2790483","article-title":"Factors affecting the ability of glycosylphosphatidylinositol-specific phospholipase D to degrade the membrane anchors of cell surface proteins","volume":"279","author":"Low","year":"1991","journal-title":"Biochem. J."},{"key":"ref_217","doi-asserted-by":"crossref","first-page":"641","DOI":"10.1042\/bj20031326","article-title":"Effect of glycosylphosphatidylinositol (GPI)-phospholipase D overexpression on GPI metabolism","volume":"378","author":"Mann","year":"2004","journal-title":"Biochem. J."},{"key":"ref_218","doi-asserted-by":"crossref","first-page":"182","DOI":"10.1006\/abbi.1995.1219","article-title":"Characterization of glycosylphosphatidylinositol (GPI)-anchored NCAM on mouse skeletal muscle cell line C2C12: The structure of the GPI glycan and release during myogenesis","volume":"318","author":"Mukasa","year":"1995","journal-title":"Arch. Biochem. Biophys."},{"key":"ref_219","doi-asserted-by":"crossref","first-page":"225","DOI":"10.1002\/(SICI)1097-4652(199908)180:2<225::AID-JCP10>3.0.CO;2-2","article-title":"Cellular glycosylphosphatidylinositol-specific phospholipase D regulates urokinase receptor shedding and cell surface expression","volume":"180","author":"Wilhelm","year":"1999","journal-title":"J. Cell Physiol."},{"key":"ref_220","doi-asserted-by":"crossref","first-page":"158","DOI":"10.1016\/j.canlet.2005.03.028","article-title":"Evidence for CEA release from human colon cancer cells by an endogenous GPI-PLD enzyme","volume":"28","author":"Naghibalhossaini","year":"2006","journal-title":"Cancer Lett."},{"key":"ref_221","doi-asserted-by":"crossref","first-page":"167","DOI":"10.1126\/science.aaw2622","article-title":"Blood factors transfer beneficial effects of exercise on neurogenesis and cognition to the aged brain","volume":"369","author":"Horowitz","year":"2020","journal-title":"Science"},{"key":"ref_222","doi-asserted-by":"crossref","first-page":"14501","DOI":"10.1074\/jbc.RA120.014643","article-title":"PGAP6. A GPI-specific phospholipase A2, has narrow substrate specificity against GPI-anchored proteins","volume":"295","author":"Lee","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_223","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/0898-6568(95)00002-7","article-title":"Role of glycosyl-phosphatidylinositol hydrolysis as a mitogenic signal for epidermal growth factor","volume":"7","author":"Clemente","year":"1995","journal-title":"Cell. Signal."},{"key":"ref_224","doi-asserted-by":"crossref","first-page":"78","DOI":"10.1126\/science.1824727","article-title":"Glycosylphosphatidylinositol: A candidate system for IL-2 signal transduction","volume":"251","author":"Eardley","year":"1991","journal-title":"Science"},{"key":"ref_225","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1016\/0898-6568(95)00008-D","article-title":"An inositol phosphoglycan from Trypanosoma cruzi inhibits ACTH action in calf adrenocortical cells","volume":"7","author":"Vila","year":"1995","journal-title":"Cell. Signal."},{"key":"ref_226","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/0300-9084(91)90071-8","article-title":"Glycosyl phosphatidylinositol in thyroid: Cell signalling or protein anchor?","volume":"73","author":"Jacquemin","year":"1991","journal-title":"Biochimie"},{"key":"ref_227","doi-asserted-by":"crossref","first-page":"21601","DOI":"10.1016\/S0021-9258(19)36653-0","article-title":"Nerve growth factor stimulates the tyrosine phosphorylation of a 38-kDa protein that specifically associates with the src homology domain of phospholipase C-gamma 1","volume":"267","author":"Ohmichi","year":"1992","journal-title":"J. Biol. Chem."},{"key":"ref_228","doi-asserted-by":"crossref","first-page":"299","DOI":"10.1016\/S0014-5793(99)01172-2","article-title":"Tissue-inherent fate of GPI revealed by GPI-anchored GFP transgenesis","volume":"458","author":"Kondoh","year":"1999","journal-title":"FEBS Lett."},{"key":"ref_229","doi-asserted-by":"crossref","first-page":"160","DOI":"10.1038\/nm1179","article-title":"Angiotensin-converting enzyme is a GPI-anchored protein releasing factor crucial for fertilization","volume":"11","author":"Kondoh","year":"2005","journal-title":"Nat. Med."},{"key":"ref_230","doi-asserted-by":"crossref","first-page":"11339","DOI":"10.1038\/nm1105-1139","article-title":"Angiotensin-converting enzyme as a GPIase: A critical reevaluation","volume":"11","author":"Leisle","year":"2005","journal-title":"Nat. Med."},{"key":"ref_231","doi-asserted-by":"crossref","first-page":"1140","DOI":"10.1038\/nm1105-1140","article-title":"Male fertility is dependent on dipeptidase activity of testis ACE","volume":"11","author":"Fuchs","year":"2005","journal-title":"Nat. Med."},{"key":"ref_232","doi-asserted-by":"crossref","first-page":"2552","DOI":"10.1073\/pnas.95.5.2552","article-title":"Angiotensin-converting enzyme and male fertility","volume":"95","author":"Hagaman","year":"1998","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_233","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1126\/science.3016898","article-title":"Insulin-stimulated hydrolysis of a novel glycolipid generates modulators of cAMP phosphodiesterase","volume":"233","author":"Saltiel","year":"1986","journal-title":"Science"},{"key":"ref_234","doi-asserted-by":"crossref","first-page":"5413","DOI":"10.1021\/bi00475a001","article-title":"Structure, biosynthesis, and function of glycosylphosphatidylinositols","volume":"29","author":"Thomas","year":"1990","journal-title":"Biochemistry"},{"key":"ref_235","doi-asserted-by":"crossref","first-page":"244","DOI":"10.2337\/diacare.13.3.244","article-title":"Second messengers of insulin action","volume":"13","author":"Saltiel","year":"1990","journal-title":"Diabetes Care"},{"key":"ref_236","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1016\/S1054-3589(08)60932-1","article-title":"Insulin mediators and the mechanism of insulin action","volume":"24","author":"Romero","year":"1993","journal-title":"Adv. Pharmacol."},{"key":"ref_237","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1016\/0305-0491(96)00087-9","article-title":"Cell signalling by inositol phosphoglycans from different species","volume":"115","author":"Caro","year":"1996","journal-title":"Comp. Biochem. Physiol. B Biochem. Mol. Biol."},{"key":"ref_238","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1007\/BF03401978","article-title":"Diabetes and the role of inositol-containing lipids in insulin signaling","volume":"5","author":"Jones","year":"1999","journal-title":"Mol. Med."},{"key":"ref_239","doi-asserted-by":"crossref","first-page":"5450","DOI":"10.1073\/pnas.97.10.5450","article-title":"Molecular basis for a link between complement and the vascular complications of diabetes","volume":"97","author":"Acosta","year":"2000","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_240","doi-asserted-by":"crossref","first-page":"3499","DOI":"10.2337\/diabetes.51.12.3499","article-title":"Early complement activation and decreased levels of glycosylphosphatidylinositol-anchored complement inhibitors in human and experimental diabetic retinopathy","volume":"51","author":"Zhang","year":"2002","journal-title":"Diabetes"},{"key":"ref_241","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.cmet.2010.04.016","article-title":"GPIHBP1 is responsible for the entry of lipoproein lipase into capillaries","volume":"12","author":"Davies","year":"2010","journal-title":"Cell Metab."},{"key":"ref_242","first-page":"495","article-title":"Shedding and enrichment of the glycoplipid-anchored complement lysis inhibitor protectin (CD59) into milk fat globules","volume":"85","author":"Hakulinen","year":"1995","journal-title":"Immunology"},{"key":"ref_243","doi-asserted-by":"crossref","first-page":"188","DOI":"10.1046\/j.1365-2249.2001.01408.x","article-title":"Tears contain the complement regulator CD59 as well as decay-accelerating factor (DAF)","volume":"123","author":"Cocuzzi","year":"2001","journal-title":"Clin. Exp. Immunol."},{"key":"ref_244","doi-asserted-by":"crossref","first-page":"209","DOI":"10.1016\/j.imlet.2003.07.001","article-title":"Determination of CD59 protein in normal human serum by enzyme immunoassay, using octyl-glucoside detergent to release glycosyl-phosphatidyl-CD59 from lipid complex","volume":"90","author":"Landi","year":"2003","journal-title":"Immunol. Lett."},{"key":"ref_245","doi-asserted-by":"crossref","first-page":"670","DOI":"10.1002\/ajh.23478","article-title":"A specific and sensitive assay for blood levels of glycated CD59: A novel biomarker for diabetes","volume":"88","author":"Ghosh","year":"2013","journal-title":"Am. J. Hematol."},{"key":"ref_246","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/S0969-2126(00)00020-4","article-title":"Structure of a soluble, glycosylated form of the human complement regulatory protein CD59","volume":"2","author":"Fletcher","year":"1994","journal-title":"Structure"},{"key":"ref_247","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1006\/scdb.2000.0240","article-title":"Developmental roles of the glypicans","volume":"12","author":"David","year":"2001","journal-title":"Semin. Cell Dev. Biol."},{"key":"ref_248","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1186\/gb-2008-9-5-224","article-title":"Glypicans","volume":"9","author":"Filmus","year":"2008","journal-title":"Genome Biol."},{"key":"ref_249","doi-asserted-by":"crossref","first-page":"923","DOI":"10.1007\/s00018-007-7471-6","article-title":"Fine-tuning of cell signaling by glypicans","volume":"68","author":"Fico","year":"2011","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_250","doi-asserted-by":"crossref","first-page":"2289","DOI":"10.2337\/db11-1395","article-title":"Glypican-4 enhances insulin signaling via interaction with the insulin receptor and serves as a novel adipokine","volume":"61","author":"Ussar","year":"2012","journal-title":"Diabetes"},{"key":"ref_251","doi-asserted-by":"crossref","first-page":"538","DOI":"10.1194\/jlr.R063032","article-title":"GPI-AP release in cellular, developmental, and reproductive biology","volume":"57","author":"Fujihara","year":"2016","journal-title":"J. Lipid Res."},{"key":"ref_252","doi-asserted-by":"crossref","unstructured":"Puig, B., Altmeppen, H.G., Linsenmeier, L., Chakroun, K., Wegwitz, F., Piontek, U.K., Tatzelt, J., Bate, C., Magnus, T., and Glatzel, M. (2019). GPI-anchor signal sequence influences PrPC sorting, shedding and signalling, and impacts on different pathomechanistic aspects of prion disease in mice. PLoS Pathog., 15.","DOI":"10.1371\/journal.ppat.1007520"},{"key":"ref_253","doi-asserted-by":"crossref","first-page":"0069-21.2021","DOI":"10.1523\/ENEURO.0069-21.2021","article-title":"Heparan sulfated glypican-4 is released from astrocytes by proteolytic shedding and GPI-anchor cleavage mechanisms","volume":"8","author":"Huang","year":"2021","journal-title":"eNeuro"},{"key":"ref_254","doi-asserted-by":"crossref","first-page":"63","DOI":"10.1016\/0005-2736(81)90512-5","article-title":"Exfoliation of membrane ecto-enzymes in the form of microvesicles","volume":"645","author":"Trams","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_255","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1083\/jcb.97.2.329","article-title":"Receptor-mediated endocytosis of transferrin and recycling of the transferrin receptor in rat reticulocytes","volume":"97","author":"Harding","year":"1983","journal-title":"J. Cell Biol."},{"key":"ref_256","doi-asserted-by":"crossref","first-page":"967","DOI":"10.1016\/0092-8674(83)90040-5","article-title":"Fate of the transferrin receptor during maturation of sheep reticulocytes in vitro: Selective externalization of the receptor","volume":"33","author":"Pan","year":"1983","journal-title":"Cell"},{"key":"ref_257","doi-asserted-by":"crossref","first-page":"942","DOI":"10.1083\/jcb.101.3.942","article-title":"Electron microscopic evidence for externalization of the transferrin receptor in vesicular form in sheep reticulocytes","volume":"101","author":"Pan","year":"1985","journal-title":"J. Cell Biol."},{"key":"ref_258","doi-asserted-by":"crossref","first-page":"9412","DOI":"10.1016\/S0021-9258(18)48095-7","article-title":"Vesicle formation during reticulocyte maturation. Association of plasma membrane activities with released vesicles (exosomes)","volume":"262","author":"Johnstone","year":"1987","journal-title":"J. Biol. Chem."},{"key":"ref_259","first-page":"27","article-title":"Exosome formation during maturation of mammalian and avian reticulocytes: Evidence that exosome release is a major route for externalisation of obsolete membrane proteins","volume":"147","author":"Johnstone","year":"1991","journal-title":"J. Cell. Pathol."},{"key":"ref_260","doi-asserted-by":"crossref","first-page":"214","DOI":"10.1016\/j.bcmd.2005.03.002","article-title":"Revisiting the road to the discovery of exosomes","volume":"34","author":"Johnstone","year":"2003","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_261","doi-asserted-by":"crossref","first-page":"2345","DOI":"10.4049\/jimmunol.146.7.2345","article-title":"Inhibition of homologous complement by CD59 is mediated by a species-selective recognition conferred through binding to C8 within C5b-8 or C9 within C5b-9","volume":"146","author":"Rollins","year":"1991","journal-title":"J. Immunol."},{"key":"ref_262","doi-asserted-by":"crossref","first-page":"2573","DOI":"10.1182\/blood.V91.7.2573","article-title":"Decay-Accelerating factor (CD55) and membrane inhibitor of reactive lysis (CD59) are released within exosomes during in vitro maturation of reticulocytes","volume":"91","author":"Rabesandrata","year":"1998","journal-title":"Blood"},{"key":"ref_263","doi-asserted-by":"crossref","first-page":"9683","DOI":"10.1073\/pnas.0308413101","article-title":"Cells release prions in association with exosomes","volume":"101","author":"Fevrier","year":"2004","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_264","doi-asserted-by":"crossref","first-page":"11170","DOI":"10.1074\/jbc.M312105200","article-title":"Dual mechanisms for shedding of the cellular prion protein","volume":"279","author":"Parkin","year":"2004","journal-title":"J. Biol. Chem."},{"key":"ref_265","doi-asserted-by":"crossref","unstructured":"M\u00fcller, G.A. (2018). Glycosylphosphatidylinositol-Anchored Proteins and Their Release from Cells\u2014From Phenomenon to Meaning, Nova Science Publishers\u2014Biochemistry Research Trends. [1st ed.].","DOI":"10.1016\/j.abb.2018.08.009"},{"key":"ref_266","doi-asserted-by":"crossref","first-page":"3791","DOI":"10.1182\/blood.V94.11.3791","article-title":"Activated platelets release two types of membrane vesicles: Microvesicles by surface shedding and exosomes derived from exocytosis of multivesicular bodies and alpha-granules","volume":"94","author":"Heijnen","year":"1999","journal-title":"Blood"},{"key":"ref_267","doi-asserted-by":"crossref","first-page":"441","DOI":"10.1055\/s-2004-833479","article-title":"Platelet secretory mechanism","volume":"30","author":"Reed","year":"2004","journal-title":"Semin. Thromb. Hemost."},{"key":"ref_268","doi-asserted-by":"crossref","first-page":"1099","DOI":"10.1084\/jem.173.5.1099","article-title":"Cytotoxic T lymphocyte granules are secretory lysosomes containing both perforin and granzymes","volume":"173","author":"Peters","year":"1991","journal-title":"J. Exp. Med."},{"key":"ref_269","doi-asserted-by":"crossref","first-page":"3235","DOI":"10.4049\/jimmunol.168.7.3235","article-title":"TCR activation of human T cells induces the production of exosomes bearing the TCR\/CD3\/zeta complex","volume":"168","author":"Blanchard","year":"2002","journal-title":"J. Immunol."},{"key":"ref_270","doi-asserted-by":"crossref","first-page":"2892","DOI":"10.1002\/1521-4141(2001010)31:10<2892::AID-IMMU2892>3.0.CO;2-I","article-title":"\u2018Tolerosomes\u2019 are produced by intestinal epithelial cells","volume":"31","author":"Karlsson","year":"2001","journal-title":"Eur. J. Immunol."},{"key":"ref_271","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1053\/gast.2001.26263","article-title":"Intestinal epithelial cells secrete exosome-like vesicles","volume":"121","author":"Raposo","year":"2001","journal-title":"Gastroenterology"},{"key":"ref_272","doi-asserted-by":"crossref","first-page":"1161","DOI":"10.1084\/jem.183.3.1161","article-title":"B lymphocytes secrete antigen-presenting vesicles","volume":"183","author":"Raposo","year":"1996","journal-title":"J. Exp. Med."},{"key":"ref_273","doi-asserted-by":"crossref","first-page":"594","DOI":"10.1038\/nm0598-594","article-title":"Eradication of established murine tumours using a novel cell-free vaccine: Dendritic cell-derived exosomes","volume":"4","author":"Zitvogel","year":"1998","journal-title":"Nat. Med."},{"key":"ref_274","doi-asserted-by":"crossref","first-page":"297","DOI":"10.1038\/85438","article-title":"Tumor-derived exosomes are a source of shared tumor rejection antigens for CTL cross-priming","volume":"7","author":"Wolfers","year":"2001","journal-title":"Nat. Med."},{"key":"ref_275","doi-asserted-by":"crossref","first-page":"163","DOI":"10.1016\/S0022-1759(00)00321-5","article-title":"Analysis of antigen presenting cell derived exosomes, based on immuno-magnetic isolation and flow cytometry","volume":"247","author":"Clayton","year":"2001","journal-title":"J. Immunol. Methods"},{"key":"ref_276","doi-asserted-by":"crossref","first-page":"553","DOI":"10.1042\/CBI20090391","article-title":"Hsp70 binds to PrPC in the process of PrPC release via exosomes from THP-1 monocytes","volume":"35","author":"Wang","year":"2011","journal-title":"Cell Biol. Int."},{"key":"ref_277","doi-asserted-by":"crossref","first-page":"642","DOI":"10.1016\/j.mcn.2005.12.003","article-title":"Exosomes are released by cultured cortical neurones","volume":"31","author":"Faure","year":"2006","journal-title":"Mol. Cell. Neurosci."},{"key":"ref_278","first-page":"299","article-title":"Human NKG2D-ligands cell biology strategies to ensure immune recognition","volume":"3","author":"Reyburn","year":"2012","journal-title":"Front. Immunol."},{"key":"ref_279","doi-asserted-by":"crossref","first-page":"295","DOI":"10.1042\/BJ20130194","article-title":"A GPI anchor explains the unique biological features of the common NKG2D-ligand allele MICA*0008","volume":"454","author":"Ashiru","year":"2013","journal-title":"Biochem. J."},{"key":"ref_280","first-page":"8","article-title":"NKG2D ligands as therapeutic targets","volume":"13","author":"Spear","year":"2013","journal-title":"Cancer Immun."},{"key":"ref_281","doi-asserted-by":"crossref","first-page":"e28497","DOI":"10.4161\/onci.28497","article-title":"Secretory pathways generating immunosuppressive NKG2D ligands: New targets for therapeutic intervention","volume":"3","year":"2014","journal-title":"Oncoimmunology"},{"key":"ref_282","doi-asserted-by":"crossref","unstructured":"Takeda, Y., Kurota, Y., Kato, T., Ito, H., Araki, A., Nara, H., Saitoh, S., Tanaka, N., Tsuchiya, N., and Asao, H. (2021). GPI-80 augments NF-\u03baB activation in tumor cells. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms222112027"},{"key":"ref_283","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1038\/sj.bjp.0704860","article-title":"Pharmacological analysis for mechanisms of GPI-80 release from tumour necrosis-\u03b1-stimulated human neutrophils","volume":"137","author":"Nitto","year":"2002","journal-title":"Br. J. Pharmacol."},{"key":"ref_284","doi-asserted-by":"crossref","first-page":"189","DOI":"10.1016\/0165-0378(93)90007-5","article-title":"The glycosylphosphatidylinositol-anchored lymphocyte antigen CDw52 is associated with the epididymal maturation of human spermatozoa","volume":"23","author":"Hale","year":"1993","journal-title":"J. Reprod. Immunol."},{"key":"ref_285","doi-asserted-by":"crossref","unstructured":"Parra, A., Padilla, L., Lucas, X., Rodriguez-Martinez, H., Barranco, I., and Roca, J. (2023). Seminal extracellular vesicles and their involvement in male (in)fertility: A systematic review. Int. J. Mol. Sci., 24.","DOI":"10.3390\/ijms24054818"},{"key":"ref_286","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1111\/j.1365-2605.2005.00543.x","article-title":"A minor fraction of a high-affinity folate binding protein from the epididymis is associated with membranous vesicles and spermatozoa in human semen","volume":"28","author":"Malm","year":"2005","journal-title":"Int. J. Androl."},{"key":"ref_287","doi-asserted-by":"crossref","first-page":"1557","DOI":"10.1016\/j.fertnstert.2005.10.070","article-title":"Levels of P34H, a sperm protein of epididymal origin, as a predictor of conventional in vitro fertilization outcome","volume":"85","author":"Sullivan","year":"2006","journal-title":"Fertil. Steril."},{"key":"ref_288","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.bcmd.2005.03.005","article-title":"Role of exosomes in sperm maturation during the transit along the male reproductive tract","volume":"35","author":"Sullivan","year":"2005","journal-title":"Blood Cells Mol. Dis."},{"key":"ref_289","doi-asserted-by":"crossref","first-page":"3365","DOI":"10.1242\/jcs.113.19.3365","article-title":"Exosome: From internal vesicle of the multivesicular body to intercellular signaling device","volume":"113","author":"Denzer","year":"2000","journal-title":"J. Cell Sci."},{"key":"ref_290","doi-asserted-by":"crossref","first-page":"1867","DOI":"10.1242\/jcs.110.16.1867","article-title":"Aggregation reroutes molecules from a recycling to a vesicle-mediated secretion pathway during reticulocyte maturation","volume":"110","author":"Vidal","year":"1997","journal-title":"J. Cell Sci."},{"key":"ref_291","doi-asserted-by":"crossref","first-page":"3673","DOI":"10.1080\/15384101.2015.1100773","article-title":"Tetraspan cargo adaptors usher GPI-anchored proteins into multivesicular bodies","volume":"14","author":"MacDonald","year":"2015","journal-title":"Cell Cycle"},{"key":"ref_292","doi-asserted-by":"crossref","first-page":"e17180","DOI":"10.7554\/eLife.17180","article-title":"Tetherin is an exosomal tether","volume":"5","author":"Edgar","year":"2016","journal-title":"eLife"},{"key":"ref_293","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1016\/j.addr.2020.08.006","article-title":"Exosomes and GPI-anchored proteins: Judicious pairs for investigating biomarkers from body fluids","volume":"161\u2013162","author":"Vidal","year":"2020","journal-title":"Adv. Drug Deliv. Rev."},{"key":"ref_294","first-page":"247","article-title":"Microvesicles\/exosomes as potential novel biomarkers of metabolic diseases","volume":"5","year":"2012","journal-title":"Diabetes Metab. Syndr. Obes."},{"key":"ref_295","doi-asserted-by":"crossref","first-page":"499","DOI":"10.1016\/0014-4827(87)90324-7","article-title":"Endothelial cell plasma membrane obtained by chemically induced vesiculation","volume":"170","author":"Moldovan","year":"1987","journal-title":"Exp. Cell Res."},{"key":"ref_296","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/0009-8981(77)90054-7","article-title":"Spontaneous shedding of plasma membrane fragments by human cells in vivo and in vitro","volume":"81","author":"Wieme","year":"1977","journal-title":"Clin. Chim. Acta"},{"key":"ref_297","doi-asserted-by":"crossref","first-page":"881","DOI":"10.1042\/bj1880881","article-title":"The isolation and characterization of 60 nm vesicles (\u2018nanovesicles\u2019) produced during ionophore A23187-induced budding of human erythrocytes","volume":"188","author":"Allan","year":"1980","journal-title":"Biochem. J."},{"key":"ref_298","doi-asserted-by":"crossref","first-page":"433","DOI":"10.1042\/bj1980433","article-title":"Ca2+-induced biochemical changes in human erythrocytes and their relation to microvesiculation","volume":"198","author":"Allan","year":"1981","journal-title":"Biochem. J."},{"key":"ref_299","first-page":"5944","article-title":"Circulating membrane vesicles in leukemic blood","volume":"45","author":"Carr","year":"1984","journal-title":"Cancer Res."},{"key":"ref_300","doi-asserted-by":"crossref","first-page":"210","DOI":"10.1016\/0005-2736(84)90464-4","article-title":"Vesiculation of platelet plasma membranes. Dilauroylglycerophosphocholine-induced shedding of a platelet plasma membrane fraction enriched in acetylcholinesterase activity","volume":"778","author":"Kobayashi","year":"1984","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_301","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/0014-5793(89)80246-7","article-title":"Characterization of vesicles, containing an acylated oligopeptide, released by human colon adenocarcinoma cells. NMR and biochemical studies","volume":"246","author":"Masella","year":"1989","journal-title":"FEBS Lett."},{"key":"ref_302","doi-asserted-by":"crossref","first-page":"1481","DOI":"10.1182\/blood.V74.5.1481.1481","article-title":"Enrichment of two glycosyl-phosphatidylinositol-anchored proteins, acetylcholinesterase and decay accelerating factor, in vesicles released from human red blood cells","volume":"74","author":"Kuypers","year":"1989","journal-title":"Blood"},{"key":"ref_303","doi-asserted-by":"crossref","first-page":"345","DOI":"10.1160\/TH03-05-0294","article-title":"Sustained elevated amounts of circulating procoagulant membrane microparticles and soluble GPV after acute myocardial infarction in diabetes mellitus","volume":"91","author":"Morel","year":"2004","journal-title":"Thromb. Haemost."},{"key":"ref_304","doi-asserted-by":"crossref","first-page":"3172","DOI":"10.1182\/blood-2010-06-290460","article-title":"Cell-derived vesicles exposing coagulant tissue factor in saliva","volume":"117","author":"Berckmans","year":"2011","journal-title":"Blood"},{"key":"ref_305","doi-asserted-by":"crossref","first-page":"2857","DOI":"10.1002\/art.10587","article-title":"Cell-derived microparticles in synovial fluid from inflamed arthritic joints support coagulation exclusively via a factor VII-dependent mechanism","volume":"46","author":"Berckmans","year":"2002","journal-title":"Arthritis Rheum."},{"key":"ref_306","doi-asserted-by":"crossref","first-page":"45","DOI":"10.1016\/j.jri.2013.02.002","article-title":"Procoagulant tissue factor-exposing vesicles in human seminal fluid","volume":"98","author":"Franz","year":"2013","journal-title":"J. Reprod. Immunol."},{"key":"ref_307","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1111\/j.1365-2362.2008.02058.x","article-title":"CD31+\/Annexin V+ microparticles in healthy offsprings of patients with coronary artery disease","volume":"39","author":"Bulut","year":"2009","journal-title":"Eur. J. Clin. Investig."},{"key":"ref_308","doi-asserted-by":"crossref","first-page":"61","DOI":"10.1016\/j.jri.2007.03.008","article-title":"Microparticles and immunomodulation in pregnancy and pre-eclampsia","volume":"76","author":"Redman","year":"2007","journal-title":"J. Reprod. Immunol."},{"key":"ref_309","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1042\/CS20140623","article-title":"Dynamic microvesicle release and clearance within the cardiovascular system: Triggers and mechanisms","volume":"129","author":"Ayers","year":"2015","journal-title":"Clin. Sci."},{"key":"ref_310","doi-asserted-by":"crossref","first-page":"R57","DOI":"10.1530\/JOE-15-0201","article-title":"Microvesicles and exosomes: New players in metabolic and cardiovascular disease","volume":"228","author":"Lawson","year":"2016","journal-title":"J. Endocrinol."},{"key":"ref_311","doi-asserted-by":"crossref","first-page":"2492858","DOI":"10.1155\/2016\/2492858","article-title":"The impact of lipoprotein-associated oxidative stress on cell-specific microvesicle release in patients with familial hypercholesterolemia","volume":"2016","author":"Nielsen","year":"2016","journal-title":"Oxid. Med. Cell. Longev."},{"key":"ref_312","doi-asserted-by":"crossref","first-page":"294","DOI":"10.1046\/j.1537-2995.1993.33493242635.x","article-title":"Time-dependent loss of surface complement regulatory activity during storage of donor blood","volume":"33","author":"Long","year":"1993","journal-title":"Transfusion"},{"key":"ref_313","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1042\/bj2980661","article-title":"Saponin-induced release of cell-surface-anchored Thy-1 by serum glycosylphosphatidylinositol-specific phospholipase D","volume":"298","author":"Bergman","year":"1994","journal-title":"Biochem. J."},{"key":"ref_314","doi-asserted-by":"crossref","first-page":"529","DOI":"10.1042\/bj3050529","article-title":"Streptolysin-O induces release of glycosylphosphatidylinositol-anchored alkaline phosphatase from ROS cells by vesiculation independently of phospholipase action","volume":"305","author":"Xie","year":"1995","journal-title":"Biochem. J."},{"key":"ref_315","doi-asserted-by":"crossref","first-page":"43","DOI":"10.1016\/j.tcb.2008.11.003","article-title":"Shedding microvesicles: Artefacts no more","volume":"19","author":"Cocucci","year":"2009","journal-title":"Trends Cell Biol."},{"key":"ref_316","doi-asserted-by":"crossref","first-page":"2317","DOI":"10.1016\/j.bbapap.2013.04.005","article-title":"Blood\/plasma secretome and microvesicles","volume":"1834","author":"Inal","year":"2013","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_317","doi-asserted-by":"crossref","first-page":"12800","DOI":"10.1073\/pnas.1516594112","article-title":"TMEM16F is required for phosphatidylserine exposure and microparticle release in activated mouse platelets","volume":"112","author":"Fujii","year":"2015","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_318","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1111\/j.1365-2141.2007.06514.x","article-title":"Plasma microparticles and vascular disorders","volume":"137","author":"Lynch","year":"2007","journal-title":"Br. J. Haematol."},{"key":"ref_319","doi-asserted-by":"crossref","first-page":"1603","DOI":"10.1242\/jcs.064386","article-title":"Microvesicles: Mediators of extracellular communication during cancer progression","volume":"123","author":"Clancy","year":"2010","journal-title":"J. Cell Sci."},{"key":"ref_320","doi-asserted-by":"crossref","first-page":"2697","DOI":"10.1007\/s00018-015-1906-2","article-title":"Extracellular vesicles and atherosclerotic diseases","volume":"72","author":"Chistiakov","year":"2015","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_321","doi-asserted-by":"crossref","first-page":"27066","DOI":"10.3402\/jev.v4.27066","article-title":"Biological properties of extracellular vesicles and their physiological functions","volume":"4","author":"Siljander","year":"2015","journal-title":"J. Extracell. Vesicles"},{"key":"ref_322","doi-asserted-by":"crossref","first-page":"3850","DOI":"10.1210\/en.2006-1479","article-title":"Identification and characterization of microvesicles secreted by 3T3-L1 adipocytes: Redox- and hormone-dependent induction of milk fat globule-epidermal growth factor 8-associated microvesicles","volume":"148","author":"Aoki","year":"2007","journal-title":"Endocrinology"},{"key":"ref_323","doi-asserted-by":"crossref","first-page":"97","DOI":"10.3109\/13813455.2010.485205","article-title":"Synthetic phosphoinositolglycans regulate lipid metabolism between rat adipocytes via release of GPI-protein-harbouring adiposomes","volume":"116","author":"Schulz","year":"2010","journal-title":"Arch. Physiol. Biochem."},{"key":"ref_324","doi-asserted-by":"crossref","first-page":"187","DOI":"10.4236\/ajmb.2012.23020","article-title":"Release of exosomes and microvesicles harbouring specific RNAs and glycosylphosphatidylinositol-anchored proteins from rat and human adipocytes is controlled by histone methylation","volume":"2","author":"Schneider","year":"2012","journal-title":"Am. J. Mol. Biol."},{"key":"ref_325","doi-asserted-by":"crossref","first-page":"324","DOI":"10.1016\/j.cellsig.2008.10.021","article-title":"Induced release of membrane vesicles and exosomes from rat adipocytes containing lipid droplet, lipid raft and glycosylphosphatidylinositol-anchored proteins","volume":"21","author":"Jung","year":"2009","journal-title":"Cell. Signal."},{"key":"ref_326","doi-asserted-by":"crossref","first-page":"723","DOI":"10.1016\/j.bbrc.2010.07.008","article-title":"Adipocyte-derived microvesicles contain RNA that is transported into macrophages and might be secreted into blood circulation","volume":"398","author":"Ogawa","year":"2010","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_327","first-page":"12774","article-title":"Association of (c)AMP-degrading glycosylphosphatidylinositol-anchored proteins with lipid droplets is induced by palmitate, H2O2 and the sulfonylurea drug, glimepiride, in rat adipocytes","volume":"47","author":"Over","year":"2008","journal-title":"Biochemistry"},{"key":"ref_328","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1038\/bjp.2008.146","article-title":"Hydrogen peroxide-induced translocation of glycolipid-anchored (c)AMP-hydrolases to lipid droplets mediates inhibition of lipolysis in rat adipocytes","volume":"154","author":"Wied","year":"2008","journal-title":"Br. J. Pharmacol."},{"key":"ref_329","doi-asserted-by":"crossref","first-page":"878","DOI":"10.1111\/j.1476-5381.2010.00724.x","article-title":"Transfer of the glycosylphosphatidylinositol-anchored 5\u2032-nucleotidase CD73 from adiposomes into rat adipocytes stimulates lipid synthesis","volume":"160","author":"Jung","year":"2010","journal-title":"Br. J. Pharmacol."},{"key":"ref_330","first-page":"1207","article-title":"Microvesicles released from rat adipocytes and harbouring glycosylphosphatidylinositol-anchored proteins transfer RNA stimulating lipid synthesis","volume":"23","author":"Schneider","year":"2010","journal-title":"Cell. Signal."},{"key":"ref_331","doi-asserted-by":"crossref","first-page":"1531","DOI":"10.1038\/oby.2011.29","article-title":"Upregulation of lipid synthesis in small rat adipocytes by microvesicle-associated CD73 from large adipocytes","volume":"19","author":"Schneider","year":"2011","journal-title":"Obesity"},{"key":"ref_332","doi-asserted-by":"crossref","first-page":"1021","DOI":"10.1016\/j.metabol.2010.10.007","article-title":"Glycosylphosphatidylinositol-anchored proteins coordinate lipolysis inhibition between large and small adipocytes","volume":"60","author":"Wied","year":"2011","journal-title":"Metabolism"},{"key":"ref_333","first-page":"27","article-title":"Lipid storage in large and small rat adipocytes by vesicle-associated glycosylphosphatidylinositol-anchored proteins","volume":"Volume 52","author":"Richter","year":"2010","journal-title":"Results and Problems in Cell Differentiation: Sensory and Metabolic Control of Energy Balance"},{"key":"ref_334","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1016\/j.ejphar.2008.08.034","article-title":"Coordinated regulation of esterification and lipolysis by palmitate, H2O2 and the anti-diabetic sulfonylurea drug, glimepiride, in rat adipocytes","volume":"597","author":"Wied","year":"2008","journal-title":"Eur. J. Pharmacol."},{"key":"ref_335","doi-asserted-by":"crossref","first-page":"1513","DOI":"10.1124\/mol.107.043935","article-title":"Translocation of glycosylphosphatidylinositol-anchored proteins from plasma membrane microdomains to lipid droplets in rat adipocytes is induced by palmitate, H2O2 and the sulfonylurea drug, glimepiride","volume":"73","author":"Wied","year":"2008","journal-title":"Mol. Pharmacol."},{"key":"ref_336","doi-asserted-by":"crossref","first-page":"901","DOI":"10.1038\/bjp.2008.146","article-title":"Translocation of glycosylphosphatidylinositol-anchored proteins to lipid droplets and inhibition of lipolysis in rat adipocytes is mediated by reactive oxygen species","volume":"154","author":"Wied","year":"2008","journal-title":"Br. J. Pharmacol."},{"key":"ref_337","doi-asserted-by":"crossref","first-page":"5149","DOI":"10.1021\/la0470986","article-title":"Measurement of the anchorage force between GPI-anchored alkaline phosphatase and supported membranes by AFM force spectroscopy","volume":"21","author":"Cross","year":"2005","journal-title":"Langmuir"},{"key":"ref_338","doi-asserted-by":"crossref","first-page":"189","DOI":"10.18388\/abp.2004_3610","article-title":"Insertion of GPI-anchored alkaline phosphatase into supported membranes: A combined AFM and fluorescence microscopy study","volume":"51","author":"Rieu","year":"2004","journal-title":"Acta Biochim. Pol."},{"key":"ref_339","doi-asserted-by":"crossref","first-page":"476","DOI":"10.1016\/j.jcis.2008.01.043","article-title":"Rat osseous plate alkaline phosphatase as Langmuir monolayer\u2014An infrared study at the air-water interface","volume":"320","author":"Caseli","year":"2008","journal-title":"J. Colloid Interface Sci."},{"key":"ref_340","doi-asserted-by":"crossref","first-page":"4090","DOI":"10.1021\/la047292s","article-title":"Effect of molecular surface packing on the enzymatic activity modulation of an anchored protein on phospholipid Langmuir monolayers","volume":"21","author":"Caseli","year":"2005","journal-title":"Langmuir"},{"key":"ref_341","doi-asserted-by":"crossref","first-page":"1315","DOI":"10.1016\/j.bbrc.2005.06.049","article-title":"GPI-alkaline phosphatase insertion into phosphatidylcholine monolayers: Phase behavior and morphology changes","volume":"333","author":"Kouzayha","year":"2005","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"ref_342","doi-asserted-by":"crossref","first-page":"493","DOI":"10.1016\/j.jcis.2006.05.055","article-title":"A thermodynamic study of GPI-anchored and soluble form of alkaline phosphatase films at the air-water interface","volume":"301","author":"Ronzon","year":"2006","journal-title":"J. Colloid Interface Sci."},{"key":"ref_343","doi-asserted-by":"crossref","first-page":"1675","DOI":"10.1172\/JCI118594","article-title":"GPI-anchored complement regulatory proteins in seminal plasma. An analysis of their physical conditions and the mechanisms of their binding to exogenous cells","volume":"97","author":"Rooney","year":"1996","journal-title":"J. Clin. Investig."},{"key":"ref_344","doi-asserted-by":"crossref","first-page":"E212","DOI":"10.1152\/ajpendo.00079.2019","article-title":"Chip-based sensing for release of unprocessed cell surface proteins in vitro and in serum and its (patho)physiological relevance","volume":"317","author":"Herling","year":"2019","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"ref_345","doi-asserted-by":"crossref","first-page":"111307","DOI":"10.1016\/j.mad.2020.111307","article-title":"Age-dependent membrane release and degradation of full-length glycosylphosphatidylinositol-anchored proteins in rats","volume":"190","author":"Ussar","year":"2020","journal-title":"Mech. Ageing Dev."},{"key":"ref_346","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1080\/13813455.2018.1498904","article-title":"Membrane insertion and intracellular transfer of glycosylphosphatidylinositol-anchored proteins: Potential therapeutic applications","volume":"126","year":"2020","journal-title":"Arch. Physiol. Biochem."},{"key":"ref_347","doi-asserted-by":"crossref","first-page":"574","DOI":"10.1096\/fasebj.10.5.8621057","article-title":"Cell-surface engineering with GPI-anchored proteins","volume":"10","author":"Medof","year":"1996","journal-title":"FASEB J."},{"key":"ref_348","doi-asserted-by":"crossref","unstructured":"Zaruba, M., Roschitz, L., Sami, H., Ogris, M., Gerner, W., and Metzner, C. (2021). Surface modification of E. coli outer membrane vesicles with glycosylphosphatidylinositol-anchored proteins: Generating pro\/eukaryote chimera constructs. Membranes, 11.","DOI":"10.3390\/membranes11060428"},{"key":"ref_349","doi-asserted-by":"crossref","first-page":"6759","DOI":"10.1016\/S0021-9258(17)39914-3","article-title":"Selective extraction of membrane-bound proteins by phospholipid vesicles","volume":"252","author":"Bouma","year":"1977","journal-title":"J. Biol. Chem."},{"key":"ref_350","doi-asserted-by":"crossref","first-page":"134","DOI":"10.3109\/00365516609051809","article-title":"Intestinal alkaline phosphatase in human lymph and serum","volume":"18","author":"Keiding","year":"1966","journal-title":"Scand. J. Clin. Lab. Investig."},{"key":"ref_351","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/0304-4165(81)90194-X","article-title":"Distribution of soluble and membranous forms of alkaline phosphatase in the small intestine of the rat","volume":"676","author":"Young","year":"1981","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_352","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1136\/gut.13.6.471","article-title":"Hormone-elicited enzyme release by the small intestinal wall","volume":"13","author":"Adelson","year":"1972","journal-title":"Gut"},{"key":"ref_353","doi-asserted-by":"crossref","first-page":"445","DOI":"10.1016\/S0016-5085(19)33076-8","article-title":"Hormonal control of intestinal alkaline phosphatase secretion in the dog","volume":"65","author":"Dyck","year":"1973","journal-title":"Gastroenterology"},{"key":"ref_354","first-page":"G461","article-title":"Effect of fat feeding on intestinal alkaline phosphatase activity in tissue and serum","volume":"241","author":"Young","year":"1981","journal-title":"Am. J. Physiol."},{"key":"ref_355","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/0167-4889(91)90213-H","article-title":"Rat intestinal alkaline phosphatase secretion into lumen and serum is coordinately regulated","volume":"1091","author":"Eliakim","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_356","doi-asserted-by":"crossref","first-page":"20614","DOI":"10.1016\/S0021-9258(19)47107-X","article-title":"Isolation and characterization of a small intestinal surfactant-like particle containing alkaline phosphatase and other digestive enzymes","volume":"264","author":"Eliakim","year":"1989","journal-title":"J. Biol. Chem."},{"key":"ref_357","doi-asserted-by":"crossref","first-page":"1355","DOI":"10.1172\/JCI114306","article-title":"Intestinal surfactant-like material: A novel secretory product of the enterocyte","volume":"84","author":"Eliakim","year":"1989","journal-title":"J. Clin. Investig."},{"key":"ref_358","doi-asserted-by":"crossref","first-page":"G1325","DOI":"10.1152\/ajpgi.00379.2007","article-title":"Intestinal alkaline phosphatase: Selective endocytosis from the enterocyte brush border during fat absorption","volume":"293","author":"Hansen","year":"2007","journal-title":"Am. J. Physiol. Gastrointest. Liver Physiol."},{"key":"ref_359","doi-asserted-by":"crossref","first-page":"136","DOI":"10.3109\/09687688.2010.542552","article-title":"Dietary free fatty acids form alkaline phosphatase-enriched microdomains in the intestinal brush border membrane","volume":"28","author":"Hansen","year":"2011","journal-title":"Mol. Membr. Biol."},{"key":"ref_360","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1172\/JCI116986","article-title":"A possible role for rat intestinal surfactant-like particles in transepithelial triacylglycerol transport","volume":"93","author":"Mahmood","year":"1994","journal-title":"J. Clin. Investig."},{"key":"ref_361","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1136\/gut.39.3.353","article-title":"Abundance of surfactant-like particles reflects mucosal integrity in patients with peptic ulcer disease","volume":"39","author":"Eliakim","year":"1996","journal-title":"Gut"},{"key":"ref_362","doi-asserted-by":"crossref","first-page":"2452","DOI":"10.1007\/s00018-007-7277-6","article-title":"A new look at adipocyte lipid droplets: Towards a role in the sensing of triacylglycerol stores?","volume":"64","author":"Dugail","year":"2007","journal-title":"Cell. Mol. Life Sci."},{"key":"ref_363","first-page":"514","article-title":"Filling up adipocytes with lipids. Lessons from caveolin-1 deficiency","volume":"1791","author":"Blouin","year":"2008","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_364","doi-asserted-by":"crossref","first-page":"373","DOI":"10.1038\/nrm1912","article-title":"Lipid droplets: A unified view of a dynamic organelle","volume":"7","author":"Martin","year":"2006","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_365","doi-asserted-by":"crossref","first-page":"170","DOI":"10.1007\/BF02534441","article-title":"A method for isolation of milk fat globules","volume":"21","author":"Patton","year":"1986","journal-title":"Lipids"},{"key":"ref_366","first-page":"59","article-title":"Histochemical and biochemical observatioins on milk-fat-globule membranes from several mammalian species","volume":"40","author":"Welsch","year":"1990","journal-title":"Acta Histochem."},{"key":"ref_367","first-page":"820","article-title":"Expression and function of the complement membrane attack complex inhibitor CD59 protectin on human breast cancer cells","volume":"71","author":"Hakulinen","year":"1994","journal-title":"Lab. Investig."},{"key":"ref_368","first-page":"4664","article-title":"Experimental therapy of human breast tumors with 131I-labeled monoclonal antibodies prepared against the human milk fat globule","volume":"48","author":"Ceriani","year":"1988","journal-title":"Cancer Res."},{"key":"ref_369","doi-asserted-by":"crossref","first-page":"633","DOI":"10.1093\/oxfordjournals.jbchem.a122524","article-title":"Isolation from human erythrocytes of a new membrane protein which inhibits the formation of complement transmembrane channels","volume":"104","author":"Sugita","year":"1988","journal-title":"J. Biochem."},{"key":"ref_370","doi-asserted-by":"crossref","first-page":"637","DOI":"10.1084\/jem.170.3.637","article-title":"CD59, an LY-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells","volume":"170","author":"Davis","year":"1989","journal-title":"J. Exp. Med."},{"key":"ref_371","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1172\/JCI114172","article-title":"Isolation and characterization of a membrane protein from normal human erythrocytes that inhibits reactive lysis of the erythrocytes of paroxysmal nocturnal hemoglobinuria","volume":"84","author":"Holguin","year":"1989","journal-title":"J. Clin. Investig."},{"key":"ref_372","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1093\/intimm\/1.2.205","article-title":"A novel membrane glycoprotein capable of inhibiting membrane attack by homologous complement","volume":"1","author":"Okada","year":"1989","journal-title":"Int. Immunol."},{"key":"ref_373","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1038\/nature03504","article-title":"Lipoprotein particles are required for Hedgehog and Wingless signalling","volume":"435","author":"Panakova","year":"2005","journal-title":"Nature"},{"key":"ref_374","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1038\/nrm2414","article-title":"Multiple roles for lipids in the Hedgehog signalling pathway","volume":"9","author":"Eaton","year":"2008","journal-title":"Nat. Rev. Mol. Cell Biol."},{"key":"ref_375","doi-asserted-by":"crossref","first-page":"172","DOI":"10.1038\/nature03494","article-title":"FGF-induced vesicular release of Sonic hedgehog and retinoic acid in leftward nodal flow is critical for left-right determination","volume":"435","author":"Tanaka","year":"2005","journal-title":"Nature"},{"key":"ref_376","first-page":"1","article-title":"Human protectin (CD59), an 18000-20000 MW complement lysis restricting factor, inhibits C5b-8 catalyzed insertion of C9 into lipid bilayer","volume":"71","author":"Meri","year":"1990","journal-title":"Immunology"},{"key":"ref_377","first-page":"28","article-title":"High-density lipoproteins can act as carriers of glycophosphoinositol lipid-anchored CD59 in human plasma","volume":"82","author":"Jauhiainen","year":"1994","journal-title":"Immunology"},{"key":"ref_378","doi-asserted-by":"crossref","first-page":"4941","DOI":"10.4049\/jimmunol.151.9.4941","article-title":"Interactions of soluble CD59 with the terminal complement complexes: CD59 and C9 compete for a nascent epitope on C8","volume":"151","author":"Lehto","year":"1993","journal-title":"J. Immunol."},{"key":"ref_379","doi-asserted-by":"crossref","first-page":"341","DOI":"10.1097\/00041433-199908000-00008","article-title":"The assembly and secretion of apolipoprotein B-containing lipoproteins","volume":"10","author":"Olofsson","year":"1999","journal-title":"Curr. Opin. Lipidol."},{"key":"ref_380","doi-asserted-by":"crossref","first-page":"749","DOI":"10.1111\/j.1476-5381.2009.00360.x","article-title":"Induced translocation of glycosylphosphatidylinositol-anchored proteins from lipid droplets to adiposomes in rat adipocytes","volume":"158","author":"Jung","year":"2009","journal-title":"Br. J. Pharmacol."},{"key":"ref_381","doi-asserted-by":"crossref","first-page":"1259","DOI":"10.1021\/bi701413t","article-title":"Inhibition of lipolysis by palmitate, H2O2 and the sulfonylurea drug, glimepiride, in rat adipocytes depends on cAMP degradation by lipid droplets","volume":"47","author":"Wied","year":"2008","journal-title":"Biochemistry"},{"key":"ref_382","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1111\/j.1600-0854.2006.00532.x","article-title":"Hitch-hiking between cells on lipoprotein particles","volume":"8","author":"Neumann","year":"2007","journal-title":"Traffic"},{"key":"ref_383","doi-asserted-by":"crossref","first-page":"716","DOI":"10.1038\/35079648","article-title":"A freely diffusible form of Sonic hedgehog mediates long-range signalling","volume":"411","author":"Zeng","year":"2001","journal-title":"Nature"},{"key":"ref_384","doi-asserted-by":"crossref","first-page":"30","DOI":"10.1038\/435030a","article-title":"Developmental biology: Morphogens hitch a greasy ride","volume":"435","author":"Mann","year":"2005","journal-title":"Nature"},{"key":"ref_385","doi-asserted-by":"crossref","first-page":"4357","DOI":"10.1242\/dev.01301","article-title":"Synergistic and antagonistic roles of the Sonic hedgehog N- and C-terminal lipids","volume":"131","author":"Feng","year":"2004","journal-title":"Development"},{"key":"ref_386","doi-asserted-by":"crossref","first-page":"143","DOI":"10.1016\/j.devcel.2005.01.008","article-title":"Hedgehog signaling: From the Drosophila cuticle to anti-cancer drugs","volume":"8","author":"Briscoe","year":"2005","journal-title":"Dev. Cell"},{"key":"ref_387","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1084\/jem.177.5.1409","article-title":"Physiologic relevance of the membrane attack complex inhibitory protein CD59 in human seminal plasma: CD59 is present on extracellular organelles (prostasomes), binds cell membranes, and inhibits complement-mediated lysis","volume":"177","author":"Rooney","year":"1993","journal-title":"J. Exp. Med."},{"key":"ref_388","doi-asserted-by":"crossref","first-page":"217","DOI":"10.1016\/0304-4165(91)90155-A","article-title":"Alkaline phosphatase isoforms in bile and serum and their generation from cells in vitro","volume":"1074","author":"Raymond","year":"1991","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_389","doi-asserted-by":"crossref","unstructured":"M\u00fcller, G.A., and M\u00fcller, T.D. (2022). Biological role of the intercellular transfer of glycosylphosphatidylinositol-anchored proteins: Stimulation of lipid and glycogen synthesis. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23137418"},{"key":"ref_390","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0304-4157(85)90008-5","article-title":"The prostasome: Its secretion and function in man","volume":"822","author":"Ronquist","year":"1985","journal-title":"Biochim. Biophys. Acta"},{"key":"ref_391","doi-asserted-by":"crossref","first-page":"118","DOI":"10.1111\/j.1399-0039.1990.tb01767.x","article-title":"The CAMPATH-1 antigen","volume":"35","author":"Hale","year":"1990","journal-title":"Tissue Antigens"},{"key":"ref_392","doi-asserted-by":"crossref","first-page":"490","DOI":"10.1111\/j.1365-2249.1992.tb06986.x","article-title":"Soluble forms of membrane cofactor protein (CD46, MCP) are present in plasma, tears and seminal fluid in normal subject","volume":"89","author":"Hara","year":"1992","journal-title":"Clin. Exp. Immunol."},{"key":"ref_393","doi-asserted-by":"crossref","first-page":"145","DOI":"10.1016\/0165-2478(93)90024-V","article-title":"A monoclonal antibody against human decay accelerating factor (DAF, CD55), D17, which lacks reactivity with semen-DAF","volume":"37","author":"Hara","year":"1993","journal-title":"Immunol. Lett."},{"key":"ref_394","doi-asserted-by":"crossref","first-page":"E462","DOI":"10.1152\/ajpendo.00504.2019","article-title":"Upregulated phospholipase D activity toward glycosylphosphatidylinositol-anchored proteins in micelle-like serum complexes in metabolically deranged rats and humans","volume":"318","year":"2020","journal-title":"Am. J. Physiol. Endocrinol. Metabol."},{"key":"ref_395","first-page":"A19","article-title":"Signatures of complete glycosylphosphatidylinositol-anchored proteins in serum are correlated with distinct metabolic states of obese rats. Adipositas\u2014Mehr (als) Gewicht","volume":"11","author":"Herling","year":"2017","journal-title":"Adipositas"},{"key":"ref_396","first-page":"S358","article-title":"A chip-based biosensor for the detection of glycosylphosphatidylinositol-anchored proteins in serum as stress biomarkers","volume":"62","author":"Herling","year":"2017","journal-title":"Biomed. Eng. Biomed. Tech."},{"key":"ref_397","first-page":"274","article-title":"Biosensing of intact glycosylphosphatidylinositol-anchored proteins in serum as biomarkers for stress-induced diseases","volume":"282","year":"2015","journal-title":"FEBS J."},{"key":"ref_398","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1126\/science.175.4023.720","article-title":"The fluid mosaic model of the structure of cell membranes","volume":"175","author":"Singer","year":"1972","journal-title":"Science"},{"key":"ref_399","doi-asserted-by":"crossref","unstructured":"Nicolson, G.L., and de Mattos, G.F. (2022). Fifty years of the fluid-mosaic model of biomembrane structure and organization and its importance in biomedicine with particular emphasis on membrane lipid replacement. Biomedicines, 10.","DOI":"10.3390\/biomedicines10071711"},{"key":"ref_400","doi-asserted-by":"crossref","unstructured":"Chen, Y., Huang, L., Qi, X., and Chen, C. (2019). Insulin receptor trafficking: Consequences for insulin sensitivity and diabetes. Int. J. Mol. Sci., 20.","DOI":"10.3390\/ijms20205007"},{"key":"ref_401","doi-asserted-by":"crossref","first-page":"680","DOI":"10.3389\/fpls.2020.00680","article-title":"The beginning of the end: Initial steps in the degradation of plasma membrane proteins","volume":"11","author":"Schwihla","year":"2020","journal-title":"Front. Plant Sci."},{"key":"ref_402","doi-asserted-by":"crossref","first-page":"102259","DOI":"10.1016\/j.isci.2021.102259","article-title":"Exploring the landscape of ectodomain shedding by quantitative protein terminomics","volume":"24","author":"Tsumagari","year":"2021","journal-title":"iScience"},{"key":"ref_403","doi-asserted-by":"crossref","first-page":"e99456","DOI":"10.15252\/embj.201899456","article-title":"Proteolytic ectodomain shedding of membrane proteins in mammals\u2014Hardware, concepts, and recent development","volume":"37","author":"Lichtenthaler","year":"2018","journal-title":"EMBO J."},{"key":"ref_404","doi-asserted-by":"crossref","unstructured":"Hanneken, A., Mercado, M., and Maher, P. (2021). Constitutive and regulated shedding of soluble FGF receptors releases biologically active inhibitors of FGF-2. Int. J. Mol. Sci., 22.","DOI":"10.3390\/ijms22052712"},{"key":"ref_405","doi-asserted-by":"crossref","unstructured":"Koo, C.Z., Matthews, A.L., Harrison, N., Szyroka, J., Nieswandt, B., Gardiner, E.E., Poulter, N.S., and Tomlinson, M.G. (2022). The platelet collagen receptor GPVI is cleaved by Tspan15\/ADAM10 and Tspan33\/ADAM10 molecular scissors. Int. J. Mol. Sci., 23.","DOI":"10.3390\/ijms23052440"},{"key":"ref_406","doi-asserted-by":"crossref","first-page":"675940","DOI":"10.3389\/fonc.2021.675940","article-title":"Advances in biological function and clinical application of small extracellular vesicle membrane proteins","volume":"11","author":"Huang","year":"2021","journal-title":"Front. Oncol."},{"key":"ref_407","doi-asserted-by":"crossref","unstructured":"Ko, S.Y., and Naora, H. (2020). Extracellular vesicle membrane-associated proteins: Emerging roles in tumor angiogenesis and anti-angiogenesis therapy resistance. Int. J. Mol. Sci., 21.","DOI":"10.3390\/ijms21155418"},{"key":"ref_408","doi-asserted-by":"crossref","first-page":"619","DOI":"10.1038\/ncb1725","article-title":"Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells","volume":"10","author":"Meehan","year":"2008","journal-title":"Nat. Cell. Biol."},{"key":"ref_409","doi-asserted-by":"crossref","first-page":"17","DOI":"10.1186\/s12943-021-01307-9","article-title":"Intercellular transfer of exosomal wild type EGFR triggers Osimertinib resistance in non-small cell lung cancer","volume":"20","author":"Wu","year":"2021","journal-title":"Mol. Cancer"},{"key":"ref_410","doi-asserted-by":"crossref","first-page":"2014","DOI":"10.4161\/cc.8.13.8988","article-title":"Microvesicles: Messengers and mediators of tumor progression","volume":"8","author":"Meehan","year":"2009","journal-title":"Cell Cycle"},{"key":"ref_411","doi-asserted-by":"crossref","first-page":"329","DOI":"10.4103\/2045-8932.114760","article-title":"On the origin of microparticles: From \u201cplatelet dust\u201d to mediators of intercellular communication","volume":"3","author":"Hargett","year":"2013","journal-title":"Pulm. Circ."},{"key":"ref_412","doi-asserted-by":"crossref","first-page":"e12144","DOI":"10.1002\/jev2.12144","article-title":"A brief history of nearly EV-erything\u2014The rise and rise of extracellular vesicles","volume":"10","author":"Couch","year":"2021","journal-title":"J. Extracell. Vesicles"}],"container-title":["Biomolecules"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/2218-273X\/13\/5\/855\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,10]],"date-time":"2025-10-10T19:37:49Z","timestamp":1760125069000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/2218-273X\/13\/5\/855"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2023,5,18]]},"references-count":412,"journal-issue":{"issue":"5","published-online":{"date-parts":[[2023,5]]}},"alternative-id":["biom13050855"],"URL":"https:\/\/doi.org\/10.3390\/biom13050855","relation":{},"ISSN":["2218-273X"],"issn-type":[{"value":"2218-273X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2023,5,18]]}}}