{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T21:31:27Z","timestamp":1790803887437,"version":"4.1.0"},"reference-count":84,"publisher":"Elsevier BV","issue":"2","license":[{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2019,2,1]],"date-time":"2019-02-01T00:00:00Z","timestamp":1548979200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2020,2,1]],"date-time":"2020-02-01T00:00:00Z","timestamp":1580515200000},"content-version":"vor","delay-in-days":365,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"funder":[{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP16KK0202"],"award-info":[{"award-number":["JP16KK0202"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["JP15K08265"],"award-info":[{"award-number":["JP15K08265"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001700","name":"Ministry of Education, Culture, Sports, Science and Technology","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100001700","id-type":"DOI","asserted-by":"publisher"}]},{"DOI":"10.13039\/501100001691","name":"Japan Society for the Promotion of Science","doi-asserted-by":"publisher","award":["B-17K16123"],"award-info":[{"award-number":["B-17K16123"]}],"id":[{"id":"10.13039\/501100001691","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["ajp.amjpathol.org","clinicalkey.com","clinicalkey.com.au","clinicalkey.es","clinicalkey.fr","clinicalkey.jp","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["The American Journal of Pathology"],"published-print":{"date-parts":[[2019,2]]},"DOI":"10.1016\/j.ajpath.2018.09.015","type":"journal-article","created":{"date-parts":[[2018,11,7]],"date-time":"2018-11-07T18:17:04Z","timestamp":1541614624000},"page":"308-319","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":12,"title":["The Accumulation of Heparan Sulfate S-Domains in Kidney Transthyretin Deposits Accelerates Fibril Formation and Promotes Cytotoxicity"],"prefix":"10.1016","volume":"189","author":[{"given":"Hirokazu","family":"Kameyama","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenji","family":"Uchimura","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Taro","family":"Yamashita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kaori","family":"Kuwabara","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mineyuki","family":"Mizuguchi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shang-Cheng","family":"Hung","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Keiichiro","family":"Okuhira","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomohiro","family":"Masuda","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tomoki","family":"Kosugi","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Takashi","family":"Ohgita","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hiroyuki","family":"Saito","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukio","family":"Ando","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kazuchika","family":"Nishitsuji","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.ajpath.2018.09.015_bib1","doi-asserted-by":"crossref","first-page":"485","DOI":"10.1016\/S0945-053X(98)90096-8","article-title":"Bio-specific sequences and domains in heparan sulphate and the regulation of cell growth and adhesion","volume":"17","author":"Lyon","year":"1998","journal-title":"Matrix Biol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib2","doi-asserted-by":"crossref","first-page":"357","DOI":"10.1172\/JCI13713","article-title":"Heparan sulfate: growth control with a restricted sequence menu","volume":"108","author":"Gallagher","year":"2001","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib3","doi-asserted-by":"crossref","first-page":"435","DOI":"10.1146\/annurev.biochem.71.110601.135458","article-title":"Order out of chaos: assembly of ligand binding sites in heparan sulfate","volume":"71","author":"Esko","year":"2002","journal-title":"Annu Rev Biochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib4","doi-asserted-by":"crossref","first-page":"5584","DOI":"10.1073\/pnas.1101194108","article-title":"Heparan sulfate\/heparin promotes transthyretin fibrillization through selective binding to a basic motif in the protein","volume":"108","author":"Noborn","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.ajpath.2018.09.015_bib5","first-page":"456","article-title":"The presence of heparan sulfate proteoglycans in the neuritic plaques and congophilic angiopathy in Alzheimer's disease","volume":"133","author":"Snow","year":"1988","journal-title":"Am J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib6","first-page":"1253","article-title":"Early accumulation of heparan sulfate in neurons and in the beta-amyloid protein-containing lesions of Alzheimer's disease and Down's syndrome","volume":"137","author":"Snow","year":"1990","journal-title":"Am J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib7","doi-asserted-by":"crossref","first-page":"537","DOI":"10.1016\/S0197-4580(02)00010-6","article-title":"Accumulation of heparan sulfate proteoglycans in cerebellar senile plaques","volume":"23","author":"van Horssen","year":"2002","journal-title":"Neurobiol Aging"},{"key":"10.1016\/j.ajpath.2018.09.015_bib8","doi-asserted-by":"crossref","first-page":"202","DOI":"10.1007\/BF00688210","article-title":"The ultrastructural localization of sulfated proteoglycans is identical in the amyloids of Alzheimer's disease and AA, AL, senile cardiac and medullary carcinoma-associated amyloidosis","volume":"78","author":"Young","year":"1989","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib9","first-page":"37","article-title":"Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: a histochemical study","volume":"53","author":"Snow","year":"1985","journal-title":"Lab Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib10","doi-asserted-by":"crossref","first-page":"1001","DOI":"10.1021\/bi101822y","article-title":"Sulfated glycosaminoglycans accelerate transthyretin amyloidogenesis by quaternary structural conversion","volume":"50","author":"Bourgault","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.ajpath.2018.09.015_bib11","doi-asserted-by":"crossref","first-page":"1681","DOI":"10.1046\/j.1471-4159.1999.721681.x","article-title":"The sulfate moieties of glycosaminoglycans are critical for the enhancement of beta-amyloid protein fibril formation","volume":"72","author":"Castillo","year":"1999","journal-title":"J Neurochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib12","doi-asserted-by":"crossref","first-page":"1101","DOI":"10.1046\/j.1432-1327.1999.00957.x","article-title":"Interactions of Alzheimer amyloid-beta peptides with glycosaminoglycans effects on fibril nucleation and growth","volume":"266","author":"McLaurin","year":"1999","journal-title":"Eur J Biochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib13","doi-asserted-by":"crossref","first-page":"32471","DOI":"10.1074\/jbc.M709870200","article-title":"Sulfated polysaccharides promote the assembly of amyloid beta(1-42) peptide into stable fibrils of reduced cytotoxicity","volume":"283","author":"Bravo","year":"2008","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib14","doi-asserted-by":"crossref","first-page":"4953","DOI":"10.1074\/jbc.M114.615401","article-title":"Differential effects on light chain amyloid formation depend on mutations and type of glycosaminoglycans","volume":"290","author":"Blancas-Mejia","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib15","doi-asserted-by":"crossref","first-page":"7172","DOI":"10.1074\/jbc.274.11.7172","article-title":"The heparin\/heparan sulfate-binding site on apo-serum amyloid A: implications for the therapeutic intervention of amyloidosis","volume":"274","author":"Ancsin","year":"1999","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib16","doi-asserted-by":"crossref","first-page":"67","DOI":"10.3109\/13506129.2016.1168292","article-title":"Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A","volume":"23","author":"Takase","year":"2016","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib17","doi-asserted-by":"crossref","first-page":"70","DOI":"10.1016\/j.biochi.2014.05.007","article-title":"Divergent effect of glycosaminoglycans on the in\u00a0vitro aggregation of serum amyloid A","volume":"104","author":"Aguilera","year":"2014","journal-title":"Biochimie"},{"key":"10.1016\/j.ajpath.2018.09.015_bib18","doi-asserted-by":"crossref","first-page":"E3138","DOI":"10.1073\/pnas.1301440110","article-title":"Heparan sulfate proteoglycans mediate internalization and propagation of specific proteopathic seeds","volume":"110","author":"Holmes","year":"2013","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.ajpath.2018.09.015_bib19","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1093\/glycob\/cwp205","article-title":"Heparan sulfate mediates amyloid-beta internalization and cytotoxicity","volume":"20","author":"Sandwall","year":"2010","journal-title":"Glycobiology"},{"key":"10.1016\/j.ajpath.2018.09.015_bib20","doi-asserted-by":"crossref","first-page":"24210","DOI":"10.1074\/jbc.M115.652545","article-title":"Cellular interaction and cytotoxicity of the Iowa mutation of apolipoprotein A-I (ApoA-IIowa) amyloid mediated by sulfate moieties of heparan sulfate","volume":"290","author":"Kuwabara","year":"2015","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib21","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1007\/s00401-009-0577-1","article-title":"Sulfation of heparan sulfate associated with amyloid-beta plaques in patients with Alzheimer's disease","volume":"119","author":"Bruinsma","year":"2010","journal-title":"Acta Neuropathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib22","doi-asserted-by":"crossref","first-page":"2056","DOI":"10.1016\/j.ajpath.2012.01.015","article-title":"Heparan sulfate subdomains that are degraded by Sulf accumulate in cerebral amyloid \u00df plaques of Alzheimer's disease: evidence from mouse models and patients","volume":"180","author":"Hosono-Fukao","year":"2012","journal-title":"Am J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib23","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1007\/s10719-017-9769-4","article-title":"Sulfated glycosaminoglycans in protein aggregation diseases","volume":"34","author":"Nishitsuji","year":"2017","journal-title":"Glycoconj J"},{"key":"10.1016\/j.ajpath.2018.09.015_bib24","doi-asserted-by":"crossref","DOI":"10.1007\/s10719-018-9833-8","article-title":"Heparan sulfate S-domains and extracellular sulfatases (Sulfs): their possible roles in protein aggregation diseases","author":"Nishitsuji","year":"2018","journal-title":"Glycoconj J"},{"key":"10.1016\/j.ajpath.2018.09.015_bib25","doi-asserted-by":"crossref","first-page":"673","DOI":"10.1177\/16.11.673","article-title":"X-ray diffraction studies on amyloid filaments","volume":"16","author":"Eanes","year":"1968","journal-title":"J Histochem Cytochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib26","doi-asserted-by":"crossref","first-page":"221","DOI":"10.3109\/13506129.2014.964858","article-title":"Nomenclature 2014: amyloid fibril proteins and clinical classification of the amyloidosis","volume":"21","author":"Sipe","year":"2014","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib27","doi-asserted-by":"crossref","first-page":"160","DOI":"10.3109\/13506120308998998","article-title":"Tabulation of human transthyretin (TTR) variants, 2003","volume":"10","author":"Connors","year":"2003","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib28","doi-asserted-by":"crossref","first-page":"1903","DOI":"10.1016\/S0021-9258(18)63184-9","article-title":"Studies on the protein-protein and protein-ligand interactions involved in retinol transport in plasma","volume":"245","author":"Raz","year":"1970","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib29","doi-asserted-by":"crossref","first-page":"104","DOI":"10.1172\/JCI111390","article-title":"Amyloid fibril protein in familial amyloidotic polyneuropathy, Portuguese type: definition of molecular abnormality in transthyretin (prealbumin)","volume":"74","author":"Saraiva","year":"1984","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib30","doi-asserted-by":"crossref","first-page":"255","DOI":"10.1080\/13506120802525285","article-title":"Serum transthyretin levels in senile systemic amyloidosis: effects of age, gender and ethnicity","volume":"15","author":"Buxbaum","year":"2008","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib31","doi-asserted-by":"crossref","first-page":"31","DOI":"10.1186\/1750-1172-8-31","article-title":"Guideline of transthyretin-related hereditary amyloidosis for clinicians","volume":"8","author":"Ando","year":"2013","journal-title":"Orphanet J Rare Dis"},{"key":"10.1016\/j.ajpath.2018.09.015_bib32","doi-asserted-by":"crossref","first-page":"385","DOI":"10.1038\/labinvest.3780246","article-title":"Amyloid and nonfibrillar deposits in mice transgenic for wild-type human transthyretin: a possible model for senile systemic amyloidosis","volume":"81","author":"Teng","year":"2001","journal-title":"Lab Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib33","doi-asserted-by":"crossref","first-page":"3095","DOI":"10.1007\/s00018-009-0109-0","article-title":"Transthyretin: the servant of many masters","volume":"66","author":"Buxbaum","year":"2009","journal-title":"Cell Mol Life Sci"},{"key":"10.1016\/j.ajpath.2018.09.015_bib34","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1002\/jms.3264","article-title":"Shotgun-proteomics-based clinical testing for diagnosis and classification of amyloidosis","volume":"48","author":"Theis","year":"2013","journal-title":"J Mass Spectrom"},{"key":"10.1016\/j.ajpath.2018.09.015_bib35","doi-asserted-by":"crossref","first-page":"21","DOI":"10.1080\/13506120601116419","article-title":"Heparan sulfate as a therapeutic target in amyloidogenesis: prospects and possible complications","volume":"14","author":"Kisilevsky","year":"2007","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib36","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1681\/ASN.2006050460","article-title":"Amyloidosis-associated kidney disease","volume":"17","author":"Dember","year":"2006","journal-title":"J Am Soc Nephrol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib37","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.2215\/CJN.08720811","article-title":"Transthyretin amyloidosis and the kidney","volume":"7","author":"Lobato","year":"2012","journal-title":"Clin J Am Soc Nephrol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib38","series-title":"Cell Biology of the Extracellular Matrix","first-page":"365","article-title":"The glomerular basement membrane: a selective macromolecular filter","author":"Farquhar","year":"1991"},{"key":"10.1016\/j.ajpath.2018.09.015_bib39","doi-asserted-by":"crossref","first-page":"10982","DOI":"10.1074\/jbc.M104852200","article-title":"Large, tissue-regulated domain diversity of heparan sulfates demonstrated by phage display antibodies","volume":"277","author":"Dennissen","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib40","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1093\/glycob\/cwp159","article-title":"Direct detection of HSulf-1 and HSulf-2 activities on extracellular heparan sulfate and their inhibition by PI-88","volume":"20","author":"Hossain","year":"2010","journal-title":"Glycobiology"},{"key":"10.1016\/j.ajpath.2018.09.015_bib41","doi-asserted-by":"crossref","first-page":"935","DOI":"10.1517\/14728222.2010.504718","article-title":"Sulf-2: an extracellular modulator of cell signaling and a cancer target candidate","volume":"14","author":"Rosen","year":"2010","journal-title":"Expert Opin Ther Targets"},{"key":"10.1016\/j.ajpath.2018.09.015_bib42","doi-asserted-by":"crossref","first-page":"459","DOI":"10.1038\/ng.792","article-title":"Common variation in GPC5 is associated with acquired nephrotic syndrome","volume":"43","author":"Okamoto","year":"2011","journal-title":"Nat Genet"},{"key":"10.1016\/j.ajpath.2018.09.015_bib43","doi-asserted-by":"crossref","first-page":"408","DOI":"10.4103\/1673-5374.179043","article-title":"Enzymatic remodeling of heparan sulfate: a therapeutic strategy for systemic and localized amyloidoses?","volume":"11","author":"Nishitsuji","year":"2016","journal-title":"Neural Regen Res"},{"key":"10.1016\/j.ajpath.2018.09.015_bib44","doi-asserted-by":"crossref","first-page":"630","DOI":"10.1681\/ASN.V133630","article-title":"A conditionally immortalized human podocyte cell line demonstrating nephrin and podocin expression","volume":"13","author":"Saleem","year":"2002","journal-title":"J Am Soc Nephrol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib45","doi-asserted-by":"crossref","first-page":"1013","DOI":"10.1006\/cyto.1997.0246","article-title":"Characterization of human recombinant interleukin 2 binding to heparin and heparan sulfate using an ELISA approach","volume":"9","author":"Najjam","year":"1997","journal-title":"Cytokine"},{"key":"10.1016\/j.ajpath.2018.09.015_bib46","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1016\/0003-2697(89)90046-8","article-title":"Fluorometric determination of amyloid fibrils in\u00a0vitro using the fluorescent dye, thioflavin T1","volume":"177","author":"Naiki","year":"1989","journal-title":"Anal Biochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib47","doi-asserted-by":"crossref","first-page":"17","DOI":"10.3109\/13506129.2015.1113167","article-title":"The polyphenol (-)-epigallocatechin-3-gallate prevents apoA-IIowa amyloidosis in\u00a0vitro and protects human embryonic kidney 293 cells against amyloid cytotoxicity","volume":"23","author":"Nakajima","year":"2016","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib48","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1186\/1471-2091-7-2","article-title":"HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: effects on VEGF, FGF-1, and SDF-1","volume":"7","author":"Uchimura","year":"2006","journal-title":"BMC Biochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib49","doi-asserted-by":"crossref","first-page":"693","DOI":"10.1177\/13.8.693","article-title":"Congo red as a stain for fluorescence microscopy of amyloid","volume":"13","author":"Puchtler","year":"1965","journal-title":"J Histochem Cytochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib50","doi-asserted-by":"crossref","first-page":"961","DOI":"10.1083\/jcb.119.4.961","article-title":"Developmental changes in heparan sulfate expression: in situ detection with mAbs","volume":"119","author":"David","year":"1992","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib51","doi-asserted-by":"crossref","first-page":"e54175","DOI":"10.1371\/journal.pone.0054175","article-title":"A consensus method for the prediction of \u201caggregation-prone\u201d peptides in globular proteins","volume":"8","author":"Tsolis","year":"2013","journal-title":"PLoS One"},{"key":"10.1016\/j.ajpath.2018.09.015_bib52","doi-asserted-by":"crossref","first-page":"224","DOI":"10.1002\/path.1759","article-title":"Amyloid deposits in transthyretin-derived amyloidosis: cleaved transthyretin is associated with distinct amyloid morphology","volume":"206","author":"Bergstrom","year":"2005","journal-title":"J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib53","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1016\/j.ajpath.2015.03.025","article-title":"Glypican-5 increases susceptibility to nephrotic damage in diabetic kidney","volume":"185","author":"Okamoto","year":"2015","journal-title":"Am J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib54","doi-asserted-by":"crossref","first-page":"805","DOI":"10.1093\/jb\/mvp128","article-title":"Amyloid formation by the model protein muscle acylphosphatase is accelerated by heparin and heparan sulphate through a scaffolding-based mechanism","volume":"146","author":"Motamedi-Shad","year":"2009","journal-title":"J Biochem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib55","doi-asserted-by":"crossref","first-page":"1337","DOI":"10.15252\/emmm.201505357","article-title":"A novel mechano-enzymatic cleavage mechanism underlies transthyretin amyloidogenesis","volume":"7","author":"Marcoux","year":"2015","journal-title":"EMBO Mol Med"},{"key":"10.1016\/j.ajpath.2018.09.015_bib56","doi-asserted-by":"crossref","first-page":"17062","DOI":"10.1074\/jbc.M500122200","article-title":"Heparan sulfate is a cellular receptor for purified infectious prions","volume":"280","author":"Horonchik","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib57","doi-asserted-by":"crossref","first-page":"17057","DOI":"10.1074\/jbc.M411314200","article-title":"PrPSc incorporation to cells requires endogenous glycosaminoglycan expression","volume":"280","author":"Hijazi","year":"2005","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib58","doi-asserted-by":"crossref","first-page":"30221","DOI":"10.1074\/jbc.270.50.30221","article-title":"Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells","volume":"270","author":"Shyng","year":"1995","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib59","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1002\/1873-3468.12426","article-title":"Heparin promotes fibril formation by the N-terminal fragment of amyloidogenic apolipoprotein A-I","volume":"590","author":"Mikawa","year":"2016","journal-title":"FEBS Lett"},{"key":"10.1016\/j.ajpath.2018.09.015_bib60","doi-asserted-by":"crossref","first-page":"257","DOI":"10.3109\/13506120108993822","article-title":"Serum transthyretin monomer in patients with familial amyloid polyneuropathy","volume":"8","author":"Sekijima","year":"2001","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib61","doi-asserted-by":"crossref","first-page":"25669","DOI":"10.1074\/jbc.M112.363895","article-title":"Heparan sulfate dissociates serum amyloid A (SAA) from acute-phase high-density lipoprotein, promoting SAA aggregation","volume":"287","author":"Noborn","year":"2012","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib62","doi-asserted-by":"crossref","first-page":"9579","DOI":"10.1074\/jbc.M111.290262","article-title":"Organ-specific sulfation patterns of heparan sulfate generated by extracellular sulfatases Sulf1 and Sulf2 in mice","volume":"287","author":"Nagamine","year":"2012","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib63","series-title":"Heptinstall's Pathology of the Kidney","author":"Jennette","year":"2007"},{"key":"10.1016\/j.ajpath.2018.09.015_bib64","doi-asserted-by":"crossref","first-page":"532","DOI":"10.1093\/ndt\/18.3.532","article-title":"Familial ATTR amyloidosis: microalbuminuria as a predictor of symptomatic disease and clinical nephropathy","volume":"18","author":"Lobato","year":"2003","journal-title":"Nephrol Dial Transplant"},{"key":"10.1016\/j.ajpath.2018.09.015_bib65","doi-asserted-by":"crossref","first-page":"27","DOI":"10.1080\/13506120410001673884","article-title":"End-stage renal disease and dialysis in hereditary amyloidosis TTR V30M: presentation, survival and prognostic factors","volume":"11","author":"Lobato","year":"2004","journal-title":"Amyloid"},{"key":"10.1016\/j.ajpath.2018.09.015_bib66","doi-asserted-by":"crossref","first-page":"451","DOI":"10.1152\/physrev.00055.2006","article-title":"Properties of the glomerular barrier and mechanisms of proteinuria","volume":"88","author":"Haraldsson","year":"2008","journal-title":"Physiol Rev"},{"key":"10.1016\/j.ajpath.2018.09.015_bib67","series-title":"Diseases of the Kidney","first-page":"2189","article-title":"Dysproteinemias: multiple myeloma, amyloidosis and related disorders","author":"Vaamonde","year":"1992"},{"key":"10.1016\/j.ajpath.2018.09.015_bib68","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1172\/JCI200113712","article-title":"Glypicans: proteoglycans with a surprise","volume":"108","author":"Filmus","year":"2001","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib69","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":"10.1016\/j.ajpath.2018.09.015_bib70","doi-asserted-by":"crossref","first-page":"2362","DOI":"10.1172\/JCI116126","article-title":"Rat glomerular mesangial cells synthesize basic fibroblast growth factor: release, upregulated synthesis, and mitogenicity in mesangial proliferative glomerulonephritis","volume":"90","author":"Floege","year":"1992","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib71","first-page":"107","article-title":"Basic fibroblast growth factor promotes proliferation of rat glomerular visceral epithelial cells in\u00a0vitro","volume":"141","author":"Takeuchi","year":"1992","journal-title":"Am J Pathol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib72","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1083\/jcb.132.3.487","article-title":"Heparan sulfate expression in polarized epithelial cells: the apical sorting of glypican (GPI-anchored proteoglycan) is inversely related to its heparan sulfate content","volume":"132","author":"Mertens","year":"1996","journal-title":"J Cell Biol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib73","doi-asserted-by":"crossref","first-page":"57","DOI":"10.1158\/0008-5472.CAN-06-1650","article-title":"Role for amplification and expression of glypican-5 in rhabdomyosarcoma","volume":"67","author":"Williamson","year":"2007","journal-title":"Cancer Res"},{"key":"10.1016\/j.ajpath.2018.09.015_bib74","doi-asserted-by":"crossref","first-page":"255","DOI":"10.3109\/08977199109000289","article-title":"Basic fibroblast growth factor stimulates glomerular mesangial cell proliferation through a protein kinase C-independent pathway","volume":"5","author":"Issandou","year":"1991","journal-title":"Growth Factors"},{"key":"10.1016\/j.ajpath.2018.09.015_bib75","doi-asserted-by":"crossref","first-page":"C182","DOI":"10.1152\/ajpcell.1989.256.1.C182","article-title":"Regulation of bovine glomerular endothelial cell growth in\u00a0vitro","volume":"256","author":"Ballermann","year":"1989","journal-title":"Am J Physiol"},{"key":"10.1016\/j.ajpath.2018.09.015_bib76","doi-asserted-by":"crossref","first-page":"1435","DOI":"10.1038\/ki.1995.433","article-title":"Long-term treatment of rats with FGF-2 results in focal segmental glomerulosclerosis","volume":"48","author":"Kriz","year":"1995","journal-title":"Kidney Int"},{"key":"10.1016\/j.ajpath.2018.09.015_bib77","doi-asserted-by":"crossref","first-page":"2809","DOI":"10.1172\/JCI118351","article-title":"Basic fibroblast growth factor augments podocyte injury and induces glomerulosclerosis in rats with experimental membranous nephropathy","volume":"96","author":"Floege","year":"1995","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib78","doi-asserted-by":"crossref","first-page":"2952","DOI":"10.1172\/JCI116918","article-title":"Infusion of platelet-derived growth factor or basic fibroblast growth factor induces selective glomerular mesangial cell proliferation and matrix accumulation in rats","volume":"92","author":"Floege","year":"1993","journal-title":"J Clin Invest"},{"key":"10.1016\/j.ajpath.2018.09.015_bib79","doi-asserted-by":"crossref","first-page":"E1339","DOI":"10.1073\/pnas.1102349108","article-title":"FGF2 gene transfer restores hippocampal functions in mouse models of Alzheimer's disease and has therapeutic implications for neurocognitive disorders","volume":"108","author":"Kiyota","year":"2011","journal-title":"Proc Natl Acad Sci U S A"},{"key":"10.1016\/j.ajpath.2018.09.015_bib80","doi-asserted-by":"crossref","first-page":"49175","DOI":"10.1074\/jbc.M205131200","article-title":"Cloning and characterization of two extracellular heparin-degrading endosulfatases in mice and humans","volume":"277","author":"Morimoto-Tomita","year":"2002","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib81","doi-asserted-by":"crossref","first-page":"1446","DOI":"10.1101\/gad.990702","article-title":"FGF signaling pathways in endochondral and intramembranous bone development and human genetic disease","volume":"16","author":"Ornitz","year":"2002","journal-title":"Genes Dev"},{"key":"10.1016\/j.ajpath.2018.09.015_bib82","doi-asserted-by":"crossref","first-page":"23906","DOI":"10.1016\/S0021-9258(20)80471-2","article-title":"Activating and inhibitory heparin sequences for FGF-2 (basic FGF): distinct requirements for FGF-1, FGF-2, and FGF-4","volume":"268","author":"Guimond","year":"1993","journal-title":"J Biol Chem"},{"key":"10.1016\/j.ajpath.2018.09.015_bib83","doi-asserted-by":"crossref","first-page":"743","DOI":"10.1016\/S1097-2765(00)00073-3","article-title":"Crystal structure of a ternary FGF-FGFR-heparin complex reveals a dual role for heparin in FGFR binding and dimerization","volume":"6","author":"Schlessinger","year":"2000","journal-title":"Mol Cell"},{"key":"10.1016\/j.ajpath.2018.09.015_bib84","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1016\/j.neulet.2006.03.047","article-title":"Amyloid beta-peptide1-42 alters tight junction protein distribution and expression in brain microvessel endothelial cells","volume":"401","author":"Marco","year":"2006","journal-title":"Neurosci Lett"}],"container-title":["The American Journal of Pathology"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002944018302803?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0002944018302803?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2025,9,12]],"date-time":"2025-09-12T16:32:54Z","timestamp":1757694774000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0002944018302803"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2019,2]]},"references-count":84,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2019,2]]}},"alternative-id":["S0002944018302803"],"URL":"https:\/\/doi.org\/10.1016\/j.ajpath.2018.09.015","relation":{},"ISSN":["0002-9440"],"issn-type":[{"value":"0002-9440","type":"print"}],"subject":[],"published":{"date-parts":[[2019,2]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"The Accumulation of Heparan Sulfate S-Domains in Kidney Transthyretin Deposits Accelerates Fibril Formation and Promotes Cytotoxicity","name":"articletitle","label":"Article Title"},{"value":"The American Journal of Pathology","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1016\/j.ajpath.2018.09.015","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2019 American Society for Investigative Pathology. Published by Elsevier Inc.","name":"copyright","label":"Copyright"}]}}