{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T13:53:21Z","timestamp":1791294801084,"version":"4.1.0"},"reference-count":197,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2014,12,1]],"date-time":"2014-12-01T00:00:00Z","timestamp":1417392000000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81270269"],"award-info":[{"award-number":["81270269"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81170278"],"award-info":[{"award-number":["81170278"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81370377"],"award-info":[{"award-number":["81370377"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81300158"],"award-info":[{"award-number":["81300158"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"DOI":"10.13039\/501100001809","name":"National Natural Science Foundation of China","doi-asserted-by":"crossref","award":["81300224"],"award-info":[{"award-number":["81300224"]}],"id":[{"id":"10.13039\/501100001809","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Aid Program for Science and Technology Innovative Research Team in Higher Educational Institutions of Hunan Province, China","award":["2008-244"],"award-info":[{"award-number":["2008-244"]}]}],"content-domain":{"domain":["atherosclerosis-journal.com","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Atherosclerosis"],"published-print":{"date-parts":[[2014,12]]},"DOI":"10.1016\/j.atherosclerosis.2014.10.016","type":"journal-article","created":{"date-parts":[[2014,10,18]],"date-time":"2014-10-18T10:20:47Z","timestamp":1413627647000},"page":"597-608","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":109,"title":["Lipoprotein lipase: From gene to atherosclerosis"],"prefix":"10.1016","volume":"237","author":[{"given":"Yuan","family":"Li","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ping-Ping","family":"He","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Da-Wei","family":"Zhang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xi-Long","family":"Zheng","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5058-7087","authenticated-orcid":false,"given":"Fracisco S.","family":"Cayabyab","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wei-Dong","family":"Yin","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chao-Ke","family":"Tang","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib1","doi-asserted-by":"crossref","first-page":"335","DOI":"10.1007\/s11883-004-0043-4","article-title":"Lipoprotein lipase and its role in regulation of plasma lipoproteins and cardiac risk","volume":"6","author":"Otarod","year":"2004","journal-title":"Curr. Atheroscler. Rep."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib2","doi-asserted-by":"crossref","first-page":"D388","DOI":"10.2741\/Goldberg","article-title":"Lipoprotein lipase: physiology, biochemistry, and molecular biology","volume":"6","author":"Goldberg","year":"2001","journal-title":"Front. Biosci. J. Virtual Libr."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib3","doi-asserted-by":"crossref","first-page":"753","DOI":"10.1007\/s00109-002-0384-9","article-title":"Lipoprotein lipase: structure, function, regulation, and role in disease","volume":"80","author":"Mead","year":"2002","journal-title":"J.\u00a0Mol. Med."},{"issue":"22","key":"10.1016\/j.atherosclerosis.2014.10.016_bib4","doi-asserted-by":"crossref","first-page":"10143","DOI":"10.1073\/pnas.88.22.10143","article-title":"Macrophages and smooth muscle cells express lipoprotein lipase in human and rabbit atherosclerotic lesions","volume":"88","author":"Yla-Herttuala","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib5","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/S0008-6363(02)00405-4","article-title":"The pivotal role of lipoprotein lipase in atherosclerosis","volume":"55","author":"Mead","year":"2002","journal-title":"Cardiovasc. Res."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib6","doi-asserted-by":"crossref","first-page":"E271","DOI":"10.1152\/ajpendo.90920.2008","article-title":"Lipoprotein lipase: from gene to obesity","volume":"297","author":"Wang","year":"2009","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib7","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.2174\/138945007783220614","article-title":"Lipases as modulators of atherosclerosis in murine models","volume":"8","author":"Brown","year":"2007","journal-title":"Curr. Drug Targets"},{"issue":"10","key":"10.1016\/j.atherosclerosis.2014.10.016_bib8","doi-asserted-by":"crossref","first-page":"4131","DOI":"10.1021\/bi00436a001","article-title":"Structure of the human lipoprotein lipase gene","volume":"28","author":"Deeb","year":"1989","journal-title":"Biochemistry"},{"issue":"7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib9","doi-asserted-by":"crossref","first-page":"993","DOI":"10.1194\/jlr.R200007-JLR200","article-title":"The lipase gene family","volume":"43","author":"Wong","year":"2002","journal-title":"J.\u00a0Lipid Res."},{"issue":"4796","key":"10.1016\/j.atherosclerosis.2014.10.016_bib10","doi-asserted-by":"crossref","first-page":"1638","DOI":"10.1126\/science.3823907","article-title":"Human lipoprotein lipase complementary DNA sequence","volume":"235","author":"Wion","year":"1987","journal-title":"Science"},{"issue":"14","key":"10.1016\/j.atherosclerosis.2014.10.016_bib11","doi-asserted-by":"crossref","first-page":"10319","DOI":"10.1016\/S0021-9258(17)34063-2","article-title":"Lipoprotein lipase domain function","volume":"269","author":"Wong","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib12","doi-asserted-by":"crossref","unstructured":"K.A. Dugi, H. L. Dichek, G. D. Talley, H. B. Brewer. Human lipoprotein lipase: the loop covering the catalytic site is essential for interaction with lipid substrates. J. Biol. Chem. 267.","DOI":"10.1016\/S0021-9258(19)74009-5"},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib13","doi-asserted-by":"crossref","first-page":"1180","DOI":"10.1016\/S0022-2275(20)31567-4","article-title":"Novel site in lipoprotein lipase (LPL415;-438) essential for substrate interaction and dimer stability","volume":"42","author":"Keiper","year":"2001","journal-title":"J.\u00a0Lipid Res."},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib14","doi-asserted-by":"crossref","first-page":"5594","DOI":"10.1073\/pnas.94.11.5594","article-title":"A\u00a0molecular biology-based approach to resolve the subunit orientation of lipoprotein lipase","volume":"94","author":"Wong","year":"1997","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"20","key":"10.1016\/j.atherosclerosis.2014.10.016_bib15","doi-asserted-by":"crossref","first-page":"5606","DOI":"10.1021\/bi00341a048","article-title":"Studies on inactivation of lipoprotein lipase: role of the dimer to monomer dissociation","volume":"24","author":"Osborne","year":"1985","journal-title":"Biochemistry"},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib16","doi-asserted-by":"crossref","first-page":"1483","DOI":"10.1038\/ng.2007.24","article-title":"Mutations in LMF1 cause combined lipase deficiency and severe hypertriglyceridemia","volume":"39","author":"Peterfy","year":"2007","journal-title":"Nat. Genet."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib17","doi-asserted-by":"crossref","first-page":"198","DOI":"10.1097\/MOL.0b013e32833854c0","article-title":"Lipase maturation factor 1: structure and role in lipase folding and assembly","volume":"21","author":"Doolittle","year":"2010","journal-title":"Curr. Opin. Lipidol."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib18","doi-asserted-by":"crossref","first-page":"1162","DOI":"10.1194\/jlr.M011155","article-title":"Lipase maturation factor 1 is required for endothelial lipase activity","volume":"52","author":"Ben-Zeev","year":"2011","journal-title":"J.\u00a0Lipid Res."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib19","doi-asserted-by":"crossref","first-page":"10727","DOI":"10.1074\/jbc.M108128200","article-title":"Maturation of lipoprotein lipase in the endoplasmic reticulum. Concurrent formation of functional dimers and inactive aggregates","volume":"277","author":"Ben-Zeev","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"issue":"22","key":"10.1016\/j.atherosclerosis.2014.10.016_bib20","doi-asserted-by":"crossref","first-page":"13206","DOI":"10.1016\/S0021-9258(18)51616-1","article-title":"Biosynthesis of lipoprotein lipase in cultured mouse adipocytes. II. Processing, subunit assembly, and intracellular transport","volume":"264","author":"Vannier","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"issue":"Pt 7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib21","doi-asserted-by":"crossref","first-page":"1095","DOI":"10.1242\/jcs.072538","article-title":"SorLA regulates the activity of lipoprotein lipase by intracellular trafficking","volume":"124","author":"Klinger","year":"2011","journal-title":"J.\u00a0Cell Sci."},{"issue":"Pt 2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib22","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1042\/bj2870337","article-title":"Regulation of the synthesis, processing and translocation of lipoprotein lipase","volume":"287","author":"Braun","year":"1992","journal-title":"Biochem. J."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib23","doi-asserted-by":"crossref","first-page":"1346","DOI":"10.2337\/diab.46.8.1346","article-title":"Differential effects of streptozotocin-induced diabetes on cardiac lipoprotein lipase activity","volume":"46","author":"Rodrigues","year":"1997","journal-title":"Diabetes"},{"issue":"25","key":"10.1016\/j.atherosclerosis.2014.10.016_bib24","doi-asserted-by":"crossref","first-page":"16564","DOI":"10.1016\/S0021-9258(18)55338-2","article-title":"Effect of chlorate on the sulfation of lipoprotein lipase and heparan sulfate proteoglycans. Sulfation of heparan sulfate proteoglycans affects lipoprotein lipase degradation","volume":"266","author":"Hoogewerf","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"issue":"9\u201310","key":"10.1016\/j.atherosclerosis.2014.10.016_bib25","doi-asserted-by":"crossref","first-page":"857","DOI":"10.1007\/s000180050031","article-title":"Cell surface heparan sulfate proteoglycans and lipoprotein metabolism","volume":"56","author":"Kolset","year":"1999","journal-title":"Cell. Mol. Life Sci. CMLS"},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib26","doi-asserted-by":"crossref","first-page":"7","DOI":"10.1093\/jb\/mvn040","article-title":"Heparan sulphate biosynthesis and disease","volume":"144","author":"Nadanaka","year":"2008","journal-title":"J.\u00a0Biochem."},{"issue":"25","key":"10.1016\/j.atherosclerosis.2014.10.016_bib27","doi-asserted-by":"crossref","first-page":"15753","DOI":"10.1074\/jbc.272.25.15753","article-title":"Endothelial cell heparanase modulation of lipoprotein lipase activity. Evidence that heparan sulfate oligosaccharide is an extracellular chaperone","volume":"272","author":"Pillarisetti","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib28","doi-asserted-by":"crossref","first-page":"894","DOI":"10.1161\/ATVBAHA.113.301309","article-title":"Endothelial heparanase regulates heart metabolism by stimulating lipoprotein lipase secretion from cardiomyocytes","volume":"33","author":"Wang","year":"2013","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib29","doi-asserted-by":"crossref","first-page":"1437","DOI":"10.1161\/01.ATV.12.12.1437","article-title":"Polarized binding of lipoprotein lipase to endothelial cells. Implications for its physiological actions","volume":"12","author":"Stins","year":"1992","journal-title":"Arterioscler. Thromb. J. Vasc. Biol.\/Am. Heart Assoc."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib30","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/0005-2760(90)90003-G","article-title":"Interaction of lipoprotein lipase with subendothelial extracellular matrix","volume":"1042","author":"Chajek-Shaul","year":"1990","journal-title":"Biochim. Biophys. Acta"},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib31","doi-asserted-by":"crossref","first-page":"2254","DOI":"10.1073\/pnas.88.6.2254","article-title":"Transport of lipoprotein lipase across endothelial cells","volume":"88","author":"Saxena","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib32","doi-asserted-by":"crossref","first-page":"8934","DOI":"10.1074\/jbc.M008813200","article-title":"Transcytosis of lipoprotein lipase across cultured endothelial cells requires both heparan sulfate proteoglycans and the very low density lipoprotein receptor","volume":"276","author":"Obunike","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib33","doi-asserted-by":"crossref","first-page":"329","DOI":"10.1016\/j.cardiores.2005.09.017","article-title":"Cardiac lipoprotein lipase: metabolic basis for diabetic heart disease","volume":"69","author":"Pulinilkunnil","year":"2006","journal-title":"Cardiovasc. Res."},{"issue":"22","key":"10.1016\/j.atherosclerosis.2014.10.016_bib34","doi-asserted-by":"crossref","first-page":"12880","DOI":"10.1016\/S0021-9258(19)38242-0","article-title":"Metabolism of endothelial cell-bound lipoprotein lipase. Evidence for heparan sulfate proteoglycan-mediated internalization and recycling","volume":"265","author":"Saxena","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib35","doi-asserted-by":"crossref","first-page":"1869","DOI":"10.1194\/jlr.R018689","article-title":"GPIHBP1, an endothelial cell transporter for lipoprotein lipase","volume":"52","author":"Young","year":"2011","journal-title":"J.\u00a0Lipid Res."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib36","doi-asserted-by":"crossref","first-page":"2690","DOI":"10.1194\/jlr.M031559","article-title":"Assessing mechanisms of GPIHBP1 and lipoprotein lipase movement across endothelial cells","volume":"53","author":"Davies","year":"2012","journal-title":"J.\u00a0Lipid Res."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib37","doi-asserted-by":"crossref","first-page":"279","DOI":"10.1016\/j.cmet.2007.02.002","article-title":"Glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1 plays a critical role in the lipolytic processing of chylomicrons","volume":"5","author":"Beigneux","year":"2007","journal-title":"Cell. Metab."},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib38","first-page":"3236","article-title":"Syndecan-1 is the primary heparan sulfate proteoglycan mediating hepatic clearance of triglyceride-rich lipoproteins in mice","volume":"119","author":"Stanford","year":"2009","journal-title":"J.\u00a0Clin. Invest."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib39","doi-asserted-by":"crossref","first-page":"849","DOI":"10.1016\/j.cmet.2014.01.017","article-title":"The GPIHBP1-LPL complex is responsible for the margination of triglyceride-rich lipoproteins in capillaries","volume":"19","author":"Goulbourne","year":"2014","journal-title":"Cell. Metab."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib40","doi-asserted-by":"crossref","first-page":"1997","DOI":"10.1194\/jlr.R200015-JLR200","article-title":"Lipoprotein lipase: genetics, lipid uptake, and regulation","volume":"43","author":"Merkel","year":"2002","journal-title":"J.\u00a0Lipid Res."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib41","doi-asserted-by":"crossref","first-page":"627","DOI":"10.1016\/j.bbalip.2011.12.004","article-title":"Cardiac lipoprotein lipase activity in the hypertrophied heart may be regulated by fatty acid flux","volume":"1821","author":"Hauton","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib42","doi-asserted-by":"crossref","first-page":"133","DOI":"10.1016\/S0021-9150(01)00622-0","article-title":"Effect of diet on adipose tissue and skeletal muscle VLDL receptor and LPL: implications for obesity and hyperlipidemia","volume":"161","author":"Roberts","year":"2002","journal-title":"Atherosclerosis"},{"issue":"10","key":"10.1016\/j.atherosclerosis.2014.10.016_bib43","doi-asserted-by":"crossref","first-page":"4622","DOI":"10.1128\/MCB.12.10.4622","article-title":"Characterization of the human lipoprotein lipase (LPL) promoter: evidence of two cis-regulatory regions, LP-alpha and LP-beta, of importance for the differentiation-linked induction of the LPL gene during adipogenesis","volume":"12","author":"Enerback","year":"1992","journal-title":"Mol. Cell. Biol."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib44","doi-asserted-by":"crossref","first-page":"1877","DOI":"10.1016\/S0022-2275(20)41891-7","article-title":"Lipoprotein lipase in lungs, spleen, and liver: synthesis and distribution","volume":"32","author":"Camps","year":"1991","journal-title":"J.\u00a0Lipid Res."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib45","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1472-6793-4-13","article-title":"Effects of heparin on the uptake of lipoprotein lipase in rat liver","volume":"4","author":"Neuger","year":"2004","journal-title":"BMC Physiol."},{"issue":"13","key":"10.1016\/j.atherosclerosis.2014.10.016_bib46","doi-asserted-by":"crossref","first-page":"7522","DOI":"10.1073\/pnas.121164498","article-title":"Tissue-specific overexpression of lipoprotein lipase causes tissue-specific insulin resistance","volume":"98","author":"Kim","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib47","doi-asserted-by":"crossref","first-page":"119","DOI":"10.1159\/000244227","article-title":"Lipoprotein lipase activity in developing rat brain areas","volume":"68","author":"Nunez","year":"1995","journal-title":"Biol. Neonate"},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib48","doi-asserted-by":"crossref","first-page":"510","DOI":"10.1016\/j.nbd.2003.12.001","article-title":"A\u00a0role for lipoprotein lipase during synaptic remodeling in the adult mouse brain","volume":"15","author":"Blain","year":"2004","journal-title":"Neurobiol. Dis."},{"issue":"Pt 2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib49","doi-asserted-by":"crossref","first-page":"321","DOI":"10.1042\/bj2980321","article-title":"Regulation of lipoprotein lipase activity and mRNA in the mammary gland of the lactating mouse","volume":"298","author":"Jensen","year":"1994","journal-title":"Biochem. J."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib50","doi-asserted-by":"crossref","first-page":"35","DOI":"10.1097\/MOL.0b013e32834d0b33","article-title":"New wrinkles in lipoprotein lipase biology","volume":"23","author":"Davies","year":"2012","journal-title":"Curr. Opin. Lipidol."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib51","doi-asserted-by":"crossref","first-page":"13","DOI":"10.1186\/1472-6793-12-13","article-title":"Linking nutritional regulation of Angptl4, Gpihbp1, and Lmf1 to lipoprotein lipase activity in rodent adipose tissue","volume":"12","author":"Kroupa","year":"2012","journal-title":"BMC Physiol."},{"issue":"Suppl.\u00a01","key":"10.1016\/j.atherosclerosis.2014.10.016_bib52","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1093\/humrep\/12.suppl_1.21","article-title":"Hormonal control of regional fat distribution","volume":"12","author":"Bjorntorp","year":"1997","journal-title":"Hum. Reprod."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib53","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1016\/0005-2760(93)90196-G","article-title":"Lipoprotein lipase gene expression: physiological regulators at the transcriptional and post-transcriptional level","volume":"1169","author":"Enerback","year":"1993","journal-title":"Biochim. Biophys. Acta"},{"issue":"19","key":"10.1016\/j.atherosclerosis.2014.10.016_bib54","doi-asserted-by":"crossref","first-page":"5336","DOI":"10.1002\/j.1460-2075.1996.tb00918.x","article-title":"PPARalpha and PPARgamma activators direct a distinct tissue-specific transcriptional response via a\u00a0PPRE in the lipoprotein lipase gene","volume":"15","author":"Schoonjans","year":"1996","journal-title":"EMBO J."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib55","doi-asserted-by":"crossref","first-page":"291","DOI":"10.2337\/diabetes.52.2.291","article-title":"PPAR-gamma activation mediates adipose depot-specific effects on gene expression and lipoprotein lipase activity: mechanisms for modulation of postprandial lipemia and differential adipose accretion","volume":"52","author":"Laplante","year":"2003","journal-title":"Diabetes"},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib56","doi-asserted-by":"crossref","first-page":"1117","DOI":"10.1194\/jlr.M021485","article-title":"Major involvement of mTOR in the PPARgamma-induced stimulation of adipose tissue lipid uptake and fat accretion","volume":"53","author":"Blanchard","year":"2012","journal-title":"J.\u00a0Lipid Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib57","doi-asserted-by":"crossref","first-page":"1268","DOI":"10.1073\/pnas.0337331100","article-title":"PPARdelta is a very low-density lipoprotein sensor in macrophages","volume":"100","author":"Chawla","year":"2003","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib58","doi-asserted-by":"crossref","first-page":"2434","DOI":"10.1073\/pnas.0510815103","article-title":"Peroxisome proliferator-activated receptor delta promotes very low-density lipoprotein-derived fatty acid catabolism in the macrophage","volume":"103","author":"Lee","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib59","doi-asserted-by":"crossref","first-page":"2275","DOI":"10.1194\/jlr.M005561","article-title":"VLDL hydrolysis by LPL activates PPAR-alpha through generation of unbound fatty acids","volume":"51","author":"Ruby","year":"2010","journal-title":"J.\u00a0Lipid Res."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib60","doi-asserted-by":"crossref","first-page":"3679","DOI":"10.1210\/en.2003-1401","article-title":"Retinoid X receptor gamma-deficient mice have increased skeletal muscle lipoprotein lipase activity and less weight gain when fed a high-fat diet","volume":"145","author":"Haugen","year":"2004","journal-title":"Endocrinology"},{"issue":"46","key":"10.1016\/j.atherosclerosis.2014.10.016_bib61","doi-asserted-by":"crossref","first-page":"43018","DOI":"10.1074\/jbc.M107823200","article-title":"Regulation of lipoprotein lipase by the oxysterol receptors, LXRalpha and LXRbeta","volume":"276","author":"Zhang","year":"2001","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib62","doi-asserted-by":"crossref","first-page":"38","DOI":"10.1006\/cyto.1997.0254","article-title":"Synergism between interferon gamma and tumour necrosis factor alpha in the regulation of lipoprotein lipase in the macrophage J774.2 cell line","volume":"10","author":"Tengku-Muhammad","year":"1998","journal-title":"Cytokine"},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib63","doi-asserted-by":"crossref","first-page":"1684","DOI":"10.1172\/JCI117844","article-title":"Tumor necrosis factor-alpha eliminates binding of NF-Y and an octamer-binding protein to the lipoprotein lipase promoter in 3T3-L1 adipocytes","volume":"95","author":"Morin","year":"1995","journal-title":"J.\u00a0Clin. Invest."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib64","doi-asserted-by":"crossref","first-page":"315","DOI":"10.1042\/BJ20071559","article-title":"Translational regulation of lipoprotein lipase in adipocytes: depletion of cellular protein kinase Calpha activates binding of the C subunit of protein kinase A to the 3\u2032-untranslated region of the lipoprotein lipase mRNA","volume":"413","author":"Unal","year":"2008","journal-title":"Biochem. J."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib65","doi-asserted-by":"crossref","first-page":"1423","DOI":"10.1093\/nar\/gki280","article-title":"A\u00a0critical role for the Sp1-binding sites in the transforming growth factor-beta-mediated inhibition of lipoprotein lipase gene expression in macrophages","volume":"33","author":"Irvine","year":"2005","journal-title":"Nucleic Acids Res."},{"issue":"45","key":"10.1016\/j.atherosclerosis.2014.10.016_bib66","doi-asserted-by":"crossref","first-page":"43281","DOI":"10.1074\/jbc.M202560200","article-title":"The translational regulation of lipoprotein lipase by epinephrine involves an RNA binding complex including the catalytic subunit of protein kinase A","volume":"277","author":"Ranganathan","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"issue":"52","key":"10.1016\/j.atherosclerosis.2014.10.016_bib67","doi-asserted-by":"crossref","first-page":"42580","DOI":"10.1074\/jbc.M507252200","article-title":"Calcium triggers folding of lipoprotein lipase into active dimers","volume":"280","author":"Zhang","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib68","doi-asserted-by":"crossref","first-page":"2191","DOI":"10.1172\/JCI116821","article-title":"Lipoprotein lipase regulation by insulin and glucocorticoid in subcutaneous and omental adipose tissues of obese women and men","volume":"92","author":"Fried","year":"1993","journal-title":"J.\u00a0Clin. Invest."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib69","doi-asserted-by":"crossref","first-page":"1926","DOI":"10.1194\/jlr.M800024-JLR200","article-title":"C-reactive protein enhances macrophage lipoprotein lipase expression","volume":"49","author":"Maingrette","year":"2008","journal-title":"J.\u00a0Lipid Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib70","first-page":"83","article-title":"MicroRNAs: processing, maturation, target recognition and regulatory functions","volume":"3","author":"Shukla","year":"2011","journal-title":"Mol. Cell. Pharmacol."},{"issue":"5985","key":"10.1016\/j.atherosclerosis.2014.10.016_bib71","doi-asserted-by":"crossref","first-page":"1566","DOI":"10.1126\/science.1189123","article-title":"MicroRNA-33 and the SREBP host genes cooperate to control cholesterol homeostasis","volume":"328","author":"Najafi-Shoushtari","year":"2010","journal-title":"Science"},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib72","doi-asserted-by":"crossref","first-page":"E198","DOI":"10.1152\/ajpendo.00179.2010","article-title":"Roles for miRNA-378\/378* in adipocyte gene expression and lipogenesis","volume":"299","author":"Gerin","year":"2010","journal-title":"Am. J. Physiol. Endocrinol. Metab."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib73","first-page":"6","article-title":"MicroRNA-29a regulates pro-inflammatory cytokine secretion and scavenger receptor expression by targeting LPL in oxLDL-stimulated dendritic cells","volume":"585","author":"Chen","year":"2011","journal-title":"FEBS Lett."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib74","doi-asserted-by":"crossref","first-page":"664","DOI":"10.1016\/j.bbrc.2011.09.120","article-title":"High fat diet induced downregulation of microRNA-467b increased lipoprotein lipase in hepatic steatosis","volume":"414","author":"Ahn","year":"2011","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib75","doi-asserted-by":"crossref","first-page":"428","DOI":"10.1016\/j.bbrc.2013.11.109","article-title":"The effects of miR-467b on lipoprotein lipase (LPL) expression, pro-inflammatory cytokine, lipid levels and atherosclerotic lesions in apolipoprotein E knockout mice","volume":"443","author":"Tian","year":"2014","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib76","doi-asserted-by":"crossref","first-page":"2421","DOI":"10.1194\/jlr.M900145-JLR200","article-title":"GPIHBP1 stabilizes lipoprotein lipase and prevents its inhibition by angiopoietin-like 3 and angiopoietin-like 4","volume":"50","author":"Sonnenburg","year":"2009","journal-title":"J.\u00a0Lipid Res."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib77","doi-asserted-by":"crossref","first-page":"54","DOI":"10.1016\/j.atherosclerosis.2014.02.008","article-title":"MicroRNA-27a\/b regulates cellular cholesterol efflux, influx and esterification\/hydrolysis in THP-1 macrophages","volume":"234","author":"Zhang","year":"2014","journal-title":"Atherosclerosis"},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib78","doi-asserted-by":"crossref","first-page":"76","DOI":"10.4161\/rna.27655","article-title":"Combinatorial regulation of lipoprotein lipase by microRNAs during mouse adipogenesis","volume":"11","author":"Bouvy-Liivrand","year":"2014","journal-title":"RNA Biol."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib79","doi-asserted-by":"crossref","first-page":"149","DOI":"10.2119\/molmed.2011.00183","article-title":"The interaction of ApoA-I and ABCA1 triggers signal transduction pathways to mediate efflux of cellular lipids","volume":"18","author":"Zhao","year":"2012","journal-title":"Mol. Med."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib80","doi-asserted-by":"crossref","first-page":"397","DOI":"10.1016\/j.bbrc.2004.05.003","article-title":"Mechanism of triglyceride lowering in mice expressing human apolipoprotein A5","volume":"319","author":"Fruchart-Najib","year":"2004","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"19","key":"10.1016\/j.atherosclerosis.2014.10.016_bib81","doi-asserted-by":"crossref","first-page":"2533","DOI":"10.1093\/hmg\/ddg255","article-title":"A\u00a0novel genetic variant in the apolipoprotein A5 gene is associated with hypertriglyceridemia","volume":"12","author":"Kao","year":"2003","journal-title":"Hum. Mol. Genet."},{"issue":"27","key":"10.1016\/j.atherosclerosis.2014.10.016_bib82","doi-asserted-by":"crossref","first-page":"25383","DOI":"10.1074\/jbc.M501589200","article-title":"Apolipoprotein A-V-heparin interactions: implications for plasma lipoprotein metabolism","volume":"280","author":"Lookene","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib83","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.atherosclerosis.2006.05.030","article-title":"Plasma apoAV levels are markedly elevated in severe hypertriglyceridemia and positively correlated with the APOA5 S19W polymorphism","volume":"193","author":"Henneman","year":"2007","journal-title":"Atherosclerosis"},{"issue":"43","key":"10.1016\/j.atherosclerosis.2014.10.016_bib84","doi-asserted-by":"crossref","first-page":"29554","DOI":"10.1074\/jbc.M802579200","article-title":"The acidic domain of GPIHBP1 is important for the binding of lipoprotein lipase and chylomicrons","volume":"283","author":"Gin","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib85","doi-asserted-by":"crossref","first-page":"2504","DOI":"10.1161\/ATVBAHA.110.210815","article-title":"Intravenous injection of apolipoprotein A-V reconstituted high-density lipoprotein decreases hypertriglyceridemia in apoav-\/- mice and requires glycosylphosphatidylinositol-anchored high-density lipoprotein-binding protein 1","volume":"30","author":"Shu","year":"2010","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"Pt 3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib86","doi-asserted-by":"crossref","first-page":"745","DOI":"10.1042\/bj3280745","article-title":"Nascent very-low-density lipoprotein triacylglycerol hydrolysis by lipoprotein lipase is inhibited by apolipoprotein E in a dose-dependent manner","volume":"328","author":"Jong","year":"1997","journal-title":"Biochem. J."},{"issue":"25","key":"10.1016\/j.atherosclerosis.2014.10.016_bib87","doi-asserted-by":"crossref","first-page":"14791","DOI":"10.1074\/jbc.271.25.14791","article-title":"Apolipoprotein E effectively inhibits lipoprotein lipase-mediated lipolysis of chylomicron-like triglyceride-rich lipid emulsions in\u00a0vitro and in\u00a0vivo","volume":"271","author":"Rensen","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib88","doi-asserted-by":"crossref","first-page":"4266","DOI":"10.1016\/S0021-9258(19)39557-2","article-title":"Lipoprotein ApoC-II activation of lipoprotein lipase. Modulation by apolipoprotein A-IV","volume":"265","author":"Goldberg","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib89","doi-asserted-by":"crossref","first-page":"4334","DOI":"10.1074\/jbc.M105421200","article-title":"Functional analyses of human apolipoprotein CII by site-directed mutagenesis: identification of residues important for activation of lipoprotein lipase","volume":"277","author":"Shen","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"issue":"47","key":"10.1016\/j.atherosclerosis.2014.10.016_bib90","doi-asserted-by":"crossref","DOI":"10.1074\/jbc.M113.495366","article-title":"Apolipoprotein C-I and C-III inhibit lipoprotein lipase activity by displacement of the enzyme from lipid droplets","volume":"288","author":"Larsson","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib91","doi-asserted-by":"crossref","first-page":"91","DOI":"10.1111\/j.1742-4658.2011.08401.x","article-title":"Characterization of a hypertriglyceridemic transgenic miniature pig model expressing human apolipoprotein CIII","volume":"279","author":"Wei","year":"2012","journal-title":"FEBS J."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib92","doi-asserted-by":"crossref","first-page":"867","DOI":"10.1007\/s11248-010-9467-5","article-title":"Hypertriglyceridemia and delayed clearance of fat load in transgenic rabbits expressing human apolipoprotein CIII","volume":"20","author":"Ding","year":"2011","journal-title":"Transgenic Res."},{"issue":"5908","key":"10.1016\/j.atherosclerosis.2014.10.016_bib93","doi-asserted-by":"crossref","first-page":"1702","DOI":"10.1126\/science.1161524","article-title":"A\u00a0null mutation in human APOC3 confers a favorable plasma lipid profile and apparent cardioprotection","volume":"322","author":"Pollin","year":"2008","journal-title":"Science"},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib94","doi-asserted-by":"crossref","first-page":"1298","DOI":"10.1194\/jlr.M001206","article-title":"A\u00a0role of apolipoprotein D in triglyceride metabolism","volume":"51","author":"Perdomo","year":"2010","journal-title":"J.\u00a0Lipid Res."},{"issue":"7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib95","doi-asserted-by":"crossref","first-page":"812","DOI":"10.1038\/nm.2347","article-title":"The transcription factor cyclic AMP-responsive element-binding protein H regulates triglyceride metabolism","volume":"17","author":"Lee","year":"2011","journal-title":"Nat. Med."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib96","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1097\/MOL.0b013e3283508fed","article-title":"The role of CREB-H transcription factor in triglyceride metabolism","volume":"23","author":"Lee","year":"2012","journal-title":"Curr. Opin. Lipidol."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib97","doi-asserted-by":"crossref","first-page":"782","DOI":"10.1016\/j.bbalip.2011.10.010","article-title":"Regulation of triglyceride metabolism by Angiopoietin-like proteins","volume":"1821","author":"Mattijssen","year":"2012","journal-title":"Biochim. Biophys. Acta"},{"issue":"20","key":"10.1016\/j.atherosclerosis.2014.10.016_bib98","doi-asserted-by":"crossref","first-page":"13735","DOI":"10.1074\/jbc.M807899200","article-title":"Identification of a new functional domain in angiopoietin-like 3 (ANGPTL3) and angiopoietin-like 4 (ANGPTL4) involved in binding and inhibition of lipoprotein lipase (LPL)","volume":"284","author":"Lee","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"issue":"48","key":"10.1016\/j.atherosclerosis.2014.10.016_bib99","doi-asserted-by":"crossref","first-page":"19751","DOI":"10.1073\/pnas.1217552109","article-title":"Atypical angiopoietin-like protein that regulates ANGPTL3","volume":"109","author":"Quagliarini","year":"2012","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib100","doi-asserted-by":"crossref","first-page":"129","DOI":"10.1016\/j.cmet.2007.07.009","article-title":"Hepatic proprotein convertases modulate HDL metabolism","volume":"6","author":"Jin","year":"2007","journal-title":"Cell. Metab."},{"issue":"37","key":"10.1016\/j.atherosclerosis.2014.10.016_bib101","doi-asserted-by":"crossref","first-page":"26410","DOI":"10.1074\/jbc.M113.501304","article-title":"Furin is the primary in\u00a0vivo convertase of angiopoietin-like 3 and endothelial lipase in hepatocytes","volume":"288","author":"Essalmani","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib102","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1161\/01.ATV.0000252827.51626.89","article-title":"Angiopoietin-like protein3 regulates plasma HDL cholesterol through suppression of endothelial lipase","volume":"27","author":"Shimamura","year":"2007","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"14","key":"10.1016\/j.atherosclerosis.2014.10.016_bib103","doi-asserted-by":"crossref","first-page":"11927","DOI":"10.1074\/jbc.M200325200","article-title":"Down-regulation of adipose tissue lipoprotein lipase during fasting requires that a gene, separate from the lipase gene, is switched on","volume":"277","author":"Bergo","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"issue":"46","key":"10.1016\/j.atherosclerosis.2014.10.016_bib104","doi-asserted-by":"crossref","first-page":"17450","DOI":"10.1073\/pnas.0604026103","article-title":"Angiopoietin-like protein 4 converts lipoprotein lipase to inactive monomers and modulates lipase activity in adipose tissue","volume":"103","author":"Sukonina","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"40","key":"10.1016\/j.atherosclerosis.2014.10.016_bib105","doi-asserted-by":"crossref","first-page":"28524","DOI":"10.1074\/jbc.M113.497602","article-title":"Angiopoietin-like protein 4 inhibition of lipoprotein lipase: evidence for reversible complex formation","volume":"288","author":"Lafferty","year":"2013","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib106","doi-asserted-by":"crossref","first-page":"138","DOI":"10.1016\/j.bbrc.2012.07.048","article-title":"Inactivation of lipoprotein lipase occurs on the surface of THP-1 macrophages where oligomers of angiopoietin-like protein 4 are formed","volume":"425","author":"Makoveichuk","year":"2012","journal-title":"Biochem. Biophys. Res. Commun."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib107","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1097\/MOL.0b013e32833ded83","article-title":"Triglyceride lipases and atherosclerosis","volume":"21","author":"Olivecrona","year":"2010","journal-title":"Curr. Opin. Lipidol."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib108","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1159\/000327774","article-title":"Fatty acids and hypoxia stimulate the expression and secretion of the adipokine ANGPTL4 (angiopoietin-like protein 4\/fasting-induced adipose factor) by human adipocytes","volume":"4","author":"Gonzalez-Muniesa","year":"2011","journal-title":"J.\u00a0Nutrigenet. Nutrigenom."},{"issue":"38","key":"10.1016\/j.atherosclerosis.2014.10.016_bib109","doi-asserted-by":"crossref","first-page":"25593","DOI":"10.1074\/jbc.M109.025452","article-title":"Angiopoietin-like 4 (ANGPTL4, fasting-induced adipose factor) is a direct glucocorticoid receptor target and participates in glucocorticoid-regulated triglyceride metabolism","volume":"284","author":"Koliwad","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib110","doi-asserted-by":"crossref","first-page":"645","DOI":"10.1194\/jlr.M043471","article-title":"Lipoprotein lipase activity is required for cardiac lipid droplet production","volume":"55","author":"Trent","year":"2014","journal-title":"J.\u00a0Lipid Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib111","doi-asserted-by":"crossref","first-page":"146","DOI":"10.1016\/j.tem.2013.12.005","article-title":"Regulation of lipoprotein lipase by Angptl4","volume":"25","author":"Dijk","year":"2014","journal-title":"Trends Endocrinol. Metab. TEM"},{"issue":"10","key":"10.1016\/j.atherosclerosis.2014.10.016_bib112","doi-asserted-by":"crossref","first-page":"e46212","DOI":"10.1371\/journal.pone.0046212","article-title":"Angiopoietin-like 4 mediates PPAR delta effect on lipoprotein lipase-dependent fatty acid uptake but not on beta-oxidation in myotubes","volume":"7","author":"Robciuc","year":"2012","journal-title":"PloS One"},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib113","doi-asserted-by":"crossref","first-page":"1712","DOI":"10.1161\/CIRCRESAHA.110.217380","article-title":"Induction of cardiac Angptl4 by dietary fatty acids is mediated by peroxisome proliferator-activated receptor beta\/delta and protects against fatty acid-induced oxidative stress","volume":"106","author":"Georgiadi","year":"2010","journal-title":"Circ. Res."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib114","doi-asserted-by":"crossref","first-page":"2223","DOI":"10.1161\/ATVBAHA.111.243519","article-title":"Human ATP-binding cassette G1 controls macrophage lipoprotein lipase bioavailability and promotes foam cell formation","volume":"32","author":"Olivier","year":"2012","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib115","doi-asserted-by":"crossref","first-page":"2433","DOI":"10.1194\/jlr.M600218-JLR200","article-title":"ABCA1 and ABCG1 or ABCG4 act sequentially to remove cellular cholesterol and generate cholesterol-rich HDL","volume":"47","author":"Vaughan","year":"2006","journal-title":"J.\u00a0Lipid Res."},{"issue":"49","key":"10.1016\/j.atherosclerosis.2014.10.016_bib116","doi-asserted-by":"crossref","first-page":"19719","DOI":"10.1073\/pnas.1113021108","article-title":"ATP binding cassette transporter G1 (ABCG1) is an intracellular sterol transporter","volume":"108","author":"Tarling","year":"2011","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib117","doi-asserted-by":"crossref","first-page":"2575","DOI":"10.1172\/JCI41280","article-title":"An intracellular role for ABCG1-mediated cholesterol transport in the regulated secretory pathway of mouse pancreatic beta cells","volume":"120","author":"Sturek","year":"2010","journal-title":"J.\u00a0Clin. Invest."},{"issue":"15","key":"10.1016\/j.atherosclerosis.2014.10.016_bib118","doi-asserted-by":"crossref","first-page":"9030","DOI":"10.1016\/S0021-9258(18)81898-1","article-title":"Insulin regulation of lipoprotein lipase activity in 3T3-L1 adipocytes is mediated at posttranscriptional and posttranslational levels","volume":"264","author":"Semenkovich","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib119","doi-asserted-by":"crossref","first-page":"179","DOI":"10.1016\/S0026-0495(97)90299-7","article-title":"Evidence for sex steroid inhibition of lipoprotein lipase in men: comparison of abdominal and femoral adipose tissue","volume":"46","author":"Ramirez","year":"1997","journal-title":"Metab. Clin. Exp."},{"issue":"15","key":"10.1016\/j.atherosclerosis.2014.10.016_bib120","doi-asserted-by":"crossref","first-page":"11404","DOI":"10.1074\/jbc.275.15.11404","article-title":"Estrogen suppresses transcription of lipoprotein lipase gene. Existence of a unique estrogen response element on the lipoprotein lipase promoter","volume":"275","author":"Homma","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"issue":"6 Pt 2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib121","first-page":"R1118","article-title":"Insulin and metabolic efficiency in rats. II. Effects of NE and cold exposure","volume":"251","author":"Bartness","year":"1986","journal-title":"Am. J. Physiol."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib122","doi-asserted-by":"crossref","first-page":"200","DOI":"10.1038\/nm.2297","article-title":"Brown adipose tissue activity controls triglyceride clearance","volume":"17","author":"Bartelt","year":"2011","journal-title":"Nat. Med."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib123","doi-asserted-by":"crossref","first-page":"1343","DOI":"10.1152\/japplphysiol.00971.2004","article-title":"Changes in lipoprotein lipase modulate tissue energy supply during stress","volume":"99","author":"Ricart-Jane","year":"2005","journal-title":"J.\u00a0Appl. Physiol."},{"issue":"17","key":"10.1016\/j.atherosclerosis.2014.10.016_bib124","doi-asserted-by":"crossref","first-page":"11553","DOI":"10.1074\/jbc.M512554200","article-title":"The lipoprotein lipase inhibitor ANGPTL3 is negatively regulated by thyroid hormone","volume":"281","author":"Fugier","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib125","doi-asserted-by":"crossref","first-page":"115","DOI":"10.1056\/NEJM199901143400207","article-title":"Atherosclerosis\u2013an inflammatory disease","volume":"340","author":"Ross","year":"1999","journal-title":"N.\u00a0Engl. J. Med."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib126","doi-asserted-by":"crossref","first-page":"503","DOI":"10.1016\/S0092-8674(01)00238-0","article-title":"Atherosclerosis. the road ahead","volume":"104","author":"Glass","year":"2001","journal-title":"Cell"},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib127","first-page":"610","article-title":"Effects of the lipoprotein lipase activator NO-1886 as a suppressor agent of atherosclerosis in aorta of mild diabetic rabbits","volume":"52","author":"Yin","year":"2002","journal-title":"Arzneimittel Forschung"},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib128","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1080\/15438600303732","article-title":"A\u00a0lipoprotein lipase-promoting agent, NO-1886, improves glucose and lipid metabolism in high fat, high sucrose-fed New Zealand white rabbits","volume":"4","author":"Yin","year":"2003","journal-title":"Int. J. Exp. Diabesity Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib129","doi-asserted-by":"crossref","first-page":"199","DOI":"10.1016\/j.phrs.2003.09.008","article-title":"NO-1886 inhibits size of adipocytes, suppresses plasma levels of tumor necrosis factor-alpha and free fatty acids, improves glucose metabolism in high-fat\/high-sucrose-fed miniature pigs","volume":"49","author":"Yin","year":"2004","journal-title":"Pharmacol. Res. Off. J. Italian Pharmacol. Soc."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib130","doi-asserted-by":"crossref","first-page":"1677","DOI":"10.1016\/S0022-2275(20)33414-3","article-title":"Overexpressed lipoprotein lipase protects against atherosclerosis in apolipoprotein E knockout mice","volume":"40","author":"Yagyu","year":"1999","journal-title":"J.\u00a0Lipid Res."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib131","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1161\/hq0102.101551","article-title":"Lipoprotein lipase in the arterial wall: linking LDL to the arterial extracellular matrix and much more","volume":"22","author":"Pentikainen","year":"2002","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib132","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/S0022-2275(20)32399-3","article-title":"Plasma and vessel wall lipoprotein lipase have different roles in atherosclerosis","volume":"41","author":"Clee","year":"2000","journal-title":"J.\u00a0Lipid Res."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib133","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1016\/S0022-2275(20)37569-6","article-title":"Lipoprotein lipase and lipolysis: central roles in lipoprotein metabolism and atherogenesis","volume":"37","author":"Goldberg","year":"1996","journal-title":"J.\u00a0Lipid Res."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib134","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1016\/S0022-2275(20)37147-9","article-title":"Lipoprotein lipase enhances human monocyte adhesion to aortic endothelial cells","volume":"38","author":"Mamputu","year":"1997","journal-title":"J.\u00a0Lipid Res."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib135","doi-asserted-by":"crossref","first-page":"6","DOI":"10.1161\/01.ATV.17.7.1414","article-title":"Lipoprotein lipase can function as a monocyte adhesion protein","volume":"17","author":"Obunike","year":"1997","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib136","doi-asserted-by":"crossref","first-page":"H2745","DOI":"10.1152\/ajpheart.00686.2006","article-title":"Lipolysis products from triglyceride-rich lipoproteins increase endothelial permeability, perturb zonula occludens-1 and F-actin, and induce apoptosis","volume":"292","author":"Eiselein","year":"2007","journal-title":"Am. J. Physiol. Heart Circ. Physiol."},{"issue":"7","key":"10.1016\/j.atherosclerosis.2014.10.016_bib137","doi-asserted-by":"crossref","first-page":"768","DOI":"10.1161\/01.RES.86.7.768","article-title":"Direct visualization of lipid deposition and reverse lipid transport in a perfused artery : roles of VLDL and HDL","volume":"86","author":"Rutledge","year":"2000","journal-title":"Circ. Res."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib138","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1196\/annals.1299.127","article-title":"Oxidation of LDL, atherogenesis, and apoptosis","volume":"1010","author":"Napoli","year":"2003","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib139","doi-asserted-by":"crossref","first-page":"1673","DOI":"10.1194\/jlr.R700001-JLR200","article-title":"Remnant-like lipoprotein particles impair endothelial function: direct and indirect effects on nitric oxide synthase","volume":"48","author":"Zheng","year":"2007","journal-title":"J.\u00a0Lipid Res."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib140","doi-asserted-by":"crossref","first-page":"628","DOI":"10.1016\/j.cjca.2010.12.075","article-title":"Remnant-like lipoproteins may accelerate endothelial progenitor cells senescence through inhibiting telomerase activity via the reactive oxygen species-dependent pathway","volume":"27","author":"Yang","year":"2011","journal-title":"Can. J. Cardiol."},{"issue":"19","key":"10.1016\/j.atherosclerosis.2014.10.016_bib141","first-page":"3479","article-title":"MicroRNA alterations in senescent endothelial progenitor cells induced by remnant-like lipoproteins","volume":"125","author":"Yang","year":"2012","journal-title":"Chin. Med. J."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib142","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1002\/mnfr.200700321","article-title":"Unsaturated fatty acids liberated from VLDL cause apoptosis in endothelial cells","volume":"52","author":"Reinbold","year":"2008","journal-title":"Mol. Nutr. food Res."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib143","first-page":"671","article-title":"Apoptosis, a major determinant of atherothrombosis","volume":"96","author":"Tedgui","year":"2003","journal-title":"Arch. des maladies du coeur des vaisseaux"},{"issue":"1\u20132","key":"10.1016\/j.atherosclerosis.2014.10.016_bib144","doi-asserted-by":"crossref","first-page":"168","DOI":"10.1016\/j.jchromb.2006.11.023","article-title":"Targeted quantitative analysis of fatty acids in atherosclerotic plaques by high sensitivity liquid chromatography\/tandem mass spectrometry","volume":"850","author":"Pettinella","year":"2007","journal-title":"J.\u00a0Chromatogr. B Anal. Technol. Biomed. Life Sci."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib145","doi-asserted-by":"crossref","first-page":"1383","DOI":"10.1038\/nm.2067","article-title":"Reducing endoplasmic reticulum stress through a macrophage lipid chaperone alleviates atherosclerosis","volume":"15","author":"Erbay","year":"2009","journal-title":"Nat. Med."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib146","doi-asserted-by":"crossref","first-page":"379","DOI":"10.1097\/MOL.0b013e32832fa5c4","article-title":"Toll-like receptor signaling links dietary fatty acids to the metabolic syndrome","volume":"20","author":"Fessler","year":"2009","journal-title":"Curr. Opin. Lipidol."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib147","doi-asserted-by":"crossref","first-page":"1240","DOI":"10.2741\/1300","article-title":"Direct effects of long-chain non-esterified fatty acids on vascular cells and their relevance to macrovascular complications of diabetes","volume":"9","author":"Oram","year":"2004","journal-title":"Front. Biosci. J. Virtual Libr."},{"issue":"30","key":"10.1016\/j.atherosclerosis.2014.10.016_bib148","doi-asserted-by":"crossref","first-page":"15416","DOI":"10.1016\/S0021-9258(19)37604-5","article-title":"Modification of low density lipoprotein by lipoprotein lipase or hepatic lipase induces enhanced uptake and cholesterol accumulation in cells","volume":"263","author":"Aviram","year":"1988","journal-title":"J.\u00a0Biol. Chem."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib149","doi-asserted-by":"crossref","first-page":"424","DOI":"10.1161\/01.ATV.0000152632.48937.2d","article-title":"Pitavastatin inhibits remnant lipoprotein-induced macrophage foam cell formation through ApoB48 receptor-dependent mechanism","volume":"25","author":"Kawakami","year":"2005","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib150","doi-asserted-by":"crossref","first-page":"660","DOI":"10.2337\/diabetes.50.3.660","article-title":"Direct regulatory effect of fatty acids on macrophage lipoprotein lipase: potential role of PPARs","volume":"50","author":"Michaud","year":"2001","journal-title":"Diabetes"},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib151","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1161\/ATVBAHA.108.182287","article-title":"n-3 fatty acids reduce arterial LDL-cholesterol delivery and arterial lipoprotein lipase levels and lipase distribution","volume":"29","author":"Chang","year":"2009","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib152","doi-asserted-by":"crossref","first-page":"401","DOI":"10.1016\/j.atherosclerosis.2014.03.022","article-title":"Incremental replacement of saturated fats by n-3 fatty acids in high-fat, high-cholesterol diets reduces elevated plasma lipid levels and arterial lipoprotein lipase, macrophages and atherosclerosis in LDLR-\/- mice","volume":"234","author":"Chang","year":"2014","journal-title":"Atherosclerosis"},{"issue":"23","key":"10.1016\/j.atherosclerosis.2014.10.016_bib153","doi-asserted-by":"crossref","first-page":"21763","DOI":"10.1074\/jbc.M501759200","article-title":"Free cholesterol-loaded macrophages are an abundant source of tumor necrosis factor-alpha and interleukin-6: model of NF-kappaB- and map kinase-dependent inflammation in advanced atherosclerosis","volume":"280","author":"Li","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib154","doi-asserted-by":"crossref","first-page":"470","DOI":"10.1016\/j.cardiores.2006.09.005","article-title":"Phagocytosis in atherosclerosis: molecular mechanisms and implications for plaque progression and stability","volume":"73","author":"Schrijvers","year":"2007","journal-title":"Cardiovasc. Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib155","doi-asserted-by":"crossref","first-page":"616","DOI":"10.2337\/diabetes.48.3.616","article-title":"Fatty acids modulate the composition of extracellular matrix in cultured human arterial smooth muscle cells by altering the expression of genes for proteoglycan core proteins","volume":"48","author":"Olsson","year":"1999","journal-title":"Diabetes"},{"issue":"Suppl.\u00a0l","key":"10.1016\/j.atherosclerosis.2014.10.016_bib156","doi-asserted-by":"crossref","first-page":"S207","DOI":"10.1194\/jlr.R800074-JLR200","article-title":"The role of oxidized phospholipids in atherosclerosis","volume":"50","author":"Berliner","year":"2009","journal-title":"J.\u00a0lipid Res."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib157","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1161\/CIRCRESAHA.111.256859","article-title":"Role of phospholipid oxidation products in atherosclerosis","volume":"111","author":"Lee","year":"2012","journal-title":"Circ. Res."},{"issue":"3","key":"10.1016\/j.atherosclerosis.2014.10.016_bib158","doi-asserted-by":"crossref","first-page":"331","DOI":"10.1165\/rcmb.2011-0153OC","article-title":"Differential regulation of endothelial cell permeability by high and low doses of oxidized 1-palmitoyl-2-arachidonyl-sn-glycero-3-phosphocholine","volume":"46","author":"Starosta","year":"2012","journal-title":"Am. J. Respir. Cell Mol. Biol."},{"issue":"41","key":"10.1016\/j.atherosclerosis.2014.10.016_bib159","doi-asserted-by":"crossref","first-page":"36011","DOI":"10.1074\/jbc.M111.265082","article-title":"Vav protein guanine nucleotide exchange factor regulates CD36 protein-mediated macrophage foam cell formation via calcium and dynamin-dependent processes","volume":"286","author":"Rahaman","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib160","doi-asserted-by":"crossref","first-page":"110","DOI":"10.1186\/1476-511X-11-110","article-title":"Toxicity of oxidized phospholipids in cultured macrophages","volume":"11","author":"Stemmer","year":"2012","journal-title":"Lipids health Dis."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib161","doi-asserted-by":"crossref","first-page":"7706","DOI":"10.4049\/jimmunol.0903594","article-title":"Oxidized phospholipids are more potent antagonists of lipopolysaccharide than inducers of inflammation","volume":"185","author":"Oskolkova","year":"2010","journal-title":"J.\u00a0Immunol."},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib162","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S0022-2275(20)33334-4","article-title":"Remnant lipoprotein metabolism: key pathways involving cell-surface heparan sulfate proteoglycans and apolipoprotein E","volume":"40","author":"Mahley","year":"1999","journal-title":"J.\u00a0Lipid Res."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib163","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1097\/00041433-199408000-00002","article-title":"Atherosclerosis and arterial influx of lipoproteins","volume":"5","author":"Nordestgaard","year":"1994","journal-title":"Curr. Opin. Lipidol."},{"issue":"14","key":"10.1016\/j.atherosclerosis.2014.10.016_bib164","doi-asserted-by":"crossref","first-page":"10160","DOI":"10.1016\/S0021-9258(18)82186-X","article-title":"Role of heparan sulfate proteoglycans in the binding and uptake of apolipoprotein E-enriched remnant lipoproteins by cultured cells","volume":"268","author":"Ji","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib165","doi-asserted-by":"crossref","first-page":"1273","DOI":"10.1194\/jlr.M000406","article-title":"VLDL lipolysis products increase VLDL fluidity and convert apolipoprotein E4 into a more expanded conformation","volume":"51","author":"Tetali","year":"2010","journal-title":"J.\u00a0lipid Res."},{"issue":"10","key":"10.1016\/j.atherosclerosis.2014.10.016_bib166","doi-asserted-by":"crossref","first-page":"2474","DOI":"10.1161\/01.ATV.19.10.2474","article-title":"Detection, quantification, and characterization of potentially atherogenic triglyceride-rich remnant lipoproteins","volume":"19","author":"Cohn","year":"1999","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib167","doi-asserted-by":"crossref","first-page":"98","DOI":"10.5551\/jat1994.1.98","article-title":"Uptake of remnant like particles (RLP) in diabetic patients from mouse peritoneal macrophages","volume":"1","author":"Tomono","year":"1994","journal-title":"J.\u00a0Atheroscler. Thromb."},{"issue":"16","key":"10.1016\/j.atherosclerosis.2014.10.016_bib168","doi-asserted-by":"crossref","first-page":"1918","DOI":"10.1161\/01.CIR.0000125278.58527.F3","article-title":"Elevated remnant-like particle cholesterol concentration: a characteristic feature of the atherogenic lipoprotein phenotype","volume":"109","author":"Twickler","year":"2004","journal-title":"Circulation"},{"issue":"1","key":"10.1016\/j.atherosclerosis.2014.10.016_bib169","doi-asserted-by":"crossref","first-page":"237","DOI":"10.1016\/j.atherosclerosis.2007.09.016","article-title":"Plasma remnant-like lipoprotein particles or LDL-C as major pathologic factors in sudden cardiac death cases","volume":"198","author":"Nakajima","year":"2008","journal-title":"Atherosclerosis"},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib170","doi-asserted-by":"crossref","first-page":"551","DOI":"10.1161\/01.ATV.15.5.551","article-title":"The response-to-retention hypothesis of early atherogenesis","volume":"15","author":"Williams","year":"1995","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib171","doi-asserted-by":"crossref","first-page":"471","DOI":"10.1097\/00041433-199810000-00012","article-title":"The response-to-retention hypothesis of atherogenesis reinforced","volume":"9","author":"Williams","year":"1998","journal-title":"Curr. Opin. Lipidol."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib172","doi-asserted-by":"crossref","first-page":"2211","DOI":"10.1161\/01.ATV.0000147163.54024.70","article-title":"Molecular interactions leading to lipoprotein retention and the initiation of atherosclerosis","volume":"24","author":"Khalil","year":"2004","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib173","doi-asserted-by":"crossref","first-page":"205","DOI":"10.1016\/S0021-9150(98)00107-5","article-title":"Association of apo B lipoproteins with arterial proteoglycans: pathological significance and molecular basis","volume":"139","author":"Camejo","year":"1998","journal-title":"Atherosclerosis"},{"issue":"6","key":"10.1016\/j.atherosclerosis.2014.10.016_bib174","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1046\/j.1365-2362.1998.00317.x","article-title":"Retention of fluorescent-labelled chylomicron remnants within the intima of the arterial wall\u2013evidence that plaque cholesterol may be derived from post-prandial lipoproteins","volume":"28","author":"Proctor","year":"1998","journal-title":"Eur. J. Clin. Invest."},{"issue":"49","key":"10.1016\/j.atherosclerosis.2014.10.016_bib175","doi-asserted-by":"crossref","first-page":"34629","DOI":"10.1074\/jbc.274.49.34629","article-title":"Lipoprotein lipase enhances the binding of native and oxidized low density lipoproteins to versican and biglycan synthesized by cultured arterial smooth muscle cells","volume":"274","author":"Olin","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"issue":"17","key":"10.1016\/j.atherosclerosis.2014.10.016_bib176","doi-asserted-by":"crossref","first-page":"5267","DOI":"10.1021\/bi962699k","article-title":"Interaction of lipoproteins with heparan sulfate proteoglycans and with lipoprotein lipase. Studies by surface plasmon resonance technique","volume":"36","author":"Lookene","year":"1997","journal-title":"Biochemistry"},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib177","doi-asserted-by":"crossref","first-page":"1504","DOI":"10.1172\/JCI116018","article-title":"Lipoprotein lipase-mediated uptake and degradation of low density lipoproteins by fibroblasts and macrophages","volume":"90","author":"Rumsey","year":"1992","journal-title":"J.\u00a0Clin. Invest."},{"issue":"34","key":"10.1016\/j.atherosclerosis.2014.10.016_bib178","doi-asserted-by":"crossref","first-page":"26293","DOI":"10.1074\/jbc.M002423200","article-title":"Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in low density lipoprotein receptor-deficient mice","volume":"275","author":"Babaev","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"issue":"12","key":"10.1016\/j.atherosclerosis.2014.10.016_bib179","doi-asserted-by":"crossref","first-page":"1697","DOI":"10.1172\/JCI6117","article-title":"Macrophage lipoprotein lipase promotes foam cell formation and atherosclerosis in\u00a0vivo","volume":"103","author":"Babaev","year":"1999","journal-title":"J.\u00a0Clin. Invest."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib180","doi-asserted-by":"crossref","first-page":"190","DOI":"10.1161\/01.ATV.13.2.190","article-title":"High macrophage lipoprotein lipase expression and secretion are associated in inbred murine strains with susceptibility to atherosclerosis","volume":"13","author":"Renier","year":"1993","journal-title":"Arterioscler. Thromb. J. Vasc. Biol.\/Am. Heart Assoc."},{"issue":"4","key":"10.1016\/j.atherosclerosis.2014.10.016_bib181","doi-asserted-by":"crossref","first-page":"1124","DOI":"10.1194\/jlr.M035568","article-title":"Macrophage lipoprotein lipase modulates the development of atherosclerosis but not adiposity","volume":"54","author":"Takahashi","year":"2013","journal-title":"J.\u00a0Lipid Res."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib182","doi-asserted-by":"crossref","first-page":"E53","DOI":"10.1161\/01.ATV.20.9.e53","article-title":"Role of macrophage-derived lipoprotein lipase in lipoprotein metabolism and atherosclerosis","volume":"20","author":"Van Eck","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"11","key":"10.1016\/j.atherosclerosis.2014.10.016_bib183","doi-asserted-by":"crossref","first-page":"1809","DOI":"10.1161\/hq1101.097805","article-title":"Macrophage-specific expression of human lipoprotein lipase accelerates atherosclerosis in transgenic apolipoprotein e knockout mice but not in C57BL\/6 mice","volume":"21","author":"Wilson","year":"2001","journal-title":"Arterioscler. Thromb. Vasc. Biol."},{"issue":"Suppl.\u00a02","key":"10.1016\/j.atherosclerosis.2014.10.016_bib184","doi-asserted-by":"crossref","first-page":"77","DOI":"10.2337\/diab.41.2.S77","article-title":"Role of lipoprotein lipase and apolipoprotein E secretion by macrophages in modulating lipoprotein uptake. Possible role in acceleration of atherosclerosis in diabetes","volume":"41","author":"Kraemer","year":"1992","journal-title":"Diabetes"},{"issue":"19","key":"10.1016\/j.atherosclerosis.2014.10.016_bib185","doi-asserted-by":"crossref","first-page":"8342","DOI":"10.1073\/pnas.88.19.8342","article-title":"Lipoprotein lipase enhances the binding of chylomicrons to low density lipoprotein receptor-related protein","volume":"88","author":"Beisiegel","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"2","key":"10.1016\/j.atherosclerosis.2014.10.016_bib186","doi-asserted-by":"crossref","first-page":"288","DOI":"10.1194\/jlr.M600292-JLR200","article-title":"Lipoprotein lipase-facilitated uptake of LDL is mediated by the LDL receptor","volume":"48","author":"Loeffler","year":"2007","journal-title":"J.\u00a0Lipid Res."},{"issue":"5","key":"10.1016\/j.atherosclerosis.2014.10.016_bib187","doi-asserted-by":"crossref","first-page":"2013","DOI":"10.1172\/JCI116081","article-title":"Lipoprotein lipase enhances binding of lipoproteins to heparan sulfate on cell surfaces and extracellular matrix","volume":"90","author":"Eisenberg","year":"1992","journal-title":"J.\u00a0Clin. Invest."},{"issue":"13","key":"10.1016\/j.atherosclerosis.2014.10.016_bib188","doi-asserted-by":"crossref","first-page":"9369","DOI":"10.1016\/S0021-9258(18)98359-6","article-title":"Low density lipoprotein receptor internalizes low density and very low density lipoproteins that are bound to heparan sulfate proteoglycans via lipoprotein lipase","volume":"268","author":"Mulder","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"issue":"23","key":"10.1016\/j.atherosclerosis.2014.10.016_bib189","doi-asserted-by":"crossref","first-page":"13841","DOI":"10.1073\/pnas.95.23.13841","article-title":"Catalytically inactive lipoprotein lipase expression in muscle of transgenic mice increases very low density lipoprotein uptake: direct evidence that lipoprotein lipase bridging occurs in\u00a0vivo","volume":"95","author":"Merkel","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U. S. A."},{"issue":"9","key":"10.1016\/j.atherosclerosis.2014.10.016_bib190","doi-asserted-by":"crossref","first-page":"7405","DOI":"10.1074\/jbc.M107914200","article-title":"Inactive lipoprotein lipase (LPL) alone increases selective cholesterol ester uptake in\u00a0vivo, whereas in the presence of active LPL it also increases triglyceride hydrolysis and whole particle lipoprotein uptake","volume":"277","author":"Merkel","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"issue":"39","key":"10.1016\/j.atherosclerosis.2014.10.016_bib191","doi-asserted-by":"crossref","first-page":"30355","DOI":"10.1074\/jbc.M910327199","article-title":"Lipoprotein lipase-mediated selective uptake from low density lipoprotein requires cell surface proteoglycans and is independent of scavenger receptor class B type 1","volume":"275","author":"Seo","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib192","doi-asserted-by":"crossref","first-page":"128","DOI":"10.1111\/j.1749-6632.2000.tb06307.x","article-title":"CD36 in atherosclerosis. The role of a class B macrophage scavenger receptor","volume":"902","author":"Nicholson","year":"2000","journal-title":"Ann. N. Y. Acad. Sci."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib193","doi-asserted-by":"crossref","first-page":"223","DOI":"10.1146\/annurev.bi.52.070183.001255","article-title":"Lipoprotein metabolism in the macrophage: implications for cholesterol deposition in atherosclerosis","volume":"52","author":"Brown","year":"1983","journal-title":"Annu. Rev. Biochem."},{"issue":"8","key":"10.1016\/j.atherosclerosis.2014.10.016_bib194","doi-asserted-by":"crossref","first-page":"1049","DOI":"10.1172\/JCI9259","article-title":"Targeted disruption of the class B scavenger receptor CD36 protects against atherosclerotic lesion development in mice","volume":"105","author":"Febbraio","year":"2000","journal-title":"J.\u00a0Clin. Invest."},{"issue":"42","key":"10.1016\/j.atherosclerosis.2014.10.016_bib195","doi-asserted-by":"crossref","first-page":"32523","DOI":"10.1074\/jbc.M003826200","article-title":"Defective uptake and utilization of long chain fatty acids in muscle and adipose tissues of CD36 knockout mice","volume":"275","author":"Coburn","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.atherosclerosis.2014.10.016_bib196","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1111\/j.1749-6632.2001.tb03944.x","article-title":"Role of CD36, the macrophage class B scavenger receptor, in atherosclerosis","volume":"947","author":"Nicholson","year":"2001","journal-title":"Ann. N. Y. Acad. Sci."},{"issue":"10","key":"10.1016\/j.atherosclerosis.2014.10.016_bib197","doi-asserted-by":"crossref","first-page":"2212","DOI":"10.1161\/01.ATV.20.10.2212","article-title":"Proliferative effect of lipoprotein lipase on human vascular smooth muscle cells","volume":"20","author":"Mamputu","year":"2000","journal-title":"Arterioscler. Thromb. Vasc. Biol."}],"container-title":["Atherosclerosis"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021915014014518?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021915014014518?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2022,4,20]],"date-time":"2022-04-20T03:36:57Z","timestamp":1650425817000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021915014014518"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2014,12]]},"references-count":197,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2014,12]]}},"alternative-id":["S0021915014014518"],"URL":"https:\/\/doi.org\/10.1016\/j.atherosclerosis.2014.10.016","relation":{},"ISSN":["0021-9150"],"issn-type":[{"value":"0021-9150","type":"print"}],"subject":[],"published":{"date-parts":[[2014,12]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Lipoprotein lipase: From gene to atherosclerosis","name":"articletitle","label":"Article Title"},{"value":"Atherosclerosis","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.atherosclerosis.2014.10.016","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"Copyright \u00a9 2014 Elsevier Ireland Ltd. All rights reserved.","name":"copyright","label":"Copyright"}]}}