{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,1]],"date-time":"2026-10-01T12:48:29Z","timestamp":1790858909595,"version":"4.1.0"},"reference-count":45,"publisher":"Elsevier BV","issue":"8","license":[{"start":{"date-parts":[[2013,8,1]],"date-time":"2013-08-01T00:00:00Z","timestamp":1375315200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2013,8,1]],"date-time":"2013-08-01T00:00:00Z","timestamp":1375315200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/legal\/tdmrep-license"},{"start":{"date-parts":[[2023,1,11]],"date-time":"2023-01-11T00:00:00Z","timestamp":1673395200000},"content-version":"vor","delay-in-days":3450,"URL":"http:\/\/www.elsevier.com\/open-access\/userlicense\/1.0\/"}],"content-domain":{"domain":["li.uscap.org","elsevier.com","sciencedirect.com"],"crossmark-restriction":true},"short-container-title":["Laboratory Investigation"],"published-print":{"date-parts":[[2013,8]]},"DOI":"10.1038\/labinvest.2013.83","type":"journal-article","created":{"date-parts":[[2013,7,1]],"date-time":"2013-07-01T08:44:17Z","timestamp":1372668257000},"page":"911-920","update-policy":"https:\/\/doi.org\/10.1016\/elsevier_cm_policy","source":"Crossref","is-referenced-by-count":41,"title":["Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis"],"prefix":"10.1016","volume":"93","author":[{"given":"Yohei","family":"Misumi","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Yukio","family":"Ando","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"N\u00e1dia P","family":"Gon\u00e7alves","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maria J","family":"Saraiva","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1038\/labinvest.2013.83_bib1","doi-asserted-by":"crossref","first-page":"1057","DOI":"10.1001\/archneur.62.7.1057","article-title":"Transthyretin-related familial amyloidotic polyneuropathy","volume":"62","author":"Ando","year":"2005","journal-title":"Arch Neurol"},{"key":"10.1038\/labinvest.2013.83_bib2","doi-asserted-by":"crossref","first-page":"398","DOI":"10.1038\/nrcardio.2010.67","article-title":"Transthyretin-related amyloidoses and the heart: a clinical overview","volume":"7","author":"Rapezzi","year":"2010","journal-title":"Nat Rev Cardiol"},{"issue":"Suppl 4","key":"10.1038\/labinvest.2013.83_bib3","doi-asserted-by":"crossref","first-page":"16427","DOI":"10.1073\/pnas.202495199","article-title":"Sequence-dependent denaturation energetics: a major determinant in amyloid disease diversity","volume":"99","author":"Hammarstr\u00f6m","year":"2002","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1038\/labinvest.2013.83_bib4","doi-asserted-by":"crossref","first-page":"253","DOI":"10.1002\/path.2411","article-title":"Amyloid fibril composition is related to the phenotype of hereditary transthyretin V30M amyloidosis","volume":"216","author":"Ihse","year":"2008","journal-title":"J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib5","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1016\/0046-8177(91)90227-G","article-title":"Familial amyloidotic polyneuropathy type 1 in Kumamoto, Japan: a clinicopathologic, histochemical, immunohistochemical, and ultrastructural study","volume":"22","author":"Takahashi","year":"1991","journal-title":"Hum Pathol"},{"key":"10.1038\/labinvest.2013.83_bib6","doi-asserted-by":"crossref","first-page":"1993","DOI":"10.1016\/S0002-9440(10)63050-7","article-title":"Deposition of transthyretin in early stages of familial amyloidotic polyneuropathy: evidence for toxicity of nonfibrillar aggregates","volume":"159","author":"Sousa","year":"2001","journal-title":"Am J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib7","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1038\/labinvest.3700107","article-title":"Deposition and passage of transthyretin through the blood-nerve barrier in recipients of familial amyloid polyneuropathy livers","volume":"84","author":"Sousa","year":"2004","journal-title":"Lab Invest"},{"key":"10.1038\/labinvest.2013.83_bib8","doi-asserted-by":"crossref","first-page":"280","DOI":"10.1016\/j.neurobiolaging.2008.04.001","article-title":"The heat shock response modulates transthyretin deposition in the peripheral and autonomic nervous systems","volume":"31","author":"Santos","year":"2010","journal-title":"Neurobiol Aging"},{"key":"10.1038\/labinvest.2013.83_bib9","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1002\/lt.21395","article-title":"Marked regression of abdominal fat amyloid in patients with familial amyloid polyneuropathy during long-term follow-up after liver transplantation","volume":"14","author":"Tsuchiya","year":"2008","journal-title":"Liver Transpl"},{"key":"10.1038\/labinvest.2013.83_bib10","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1016\/j.humpath.2010.06.014","article-title":"Wild-type transthyretin significantly contributes to the formation of amyloid fibrils in familial amyloid polyneuropathy patients with amyloidogenic transthyretin Val30Met","volume":"42","author":"Tsuchiya-Suzuki","year":"2011","journal-title":"Hum Pathol"},{"key":"10.1038\/labinvest.2013.83_bib11","doi-asserted-by":"crossref","first-page":"8598","DOI":"10.1016\/S0021-9258(18)68346-2","article-title":"Plasma transthyretin. Tissue sites of degradation and turnover in the rat","volume":"263","author":"Makover","year":"1988","journal-title":"J Biol Chem"},{"key":"10.1038\/labinvest.2013.83_bib12","doi-asserted-by":"crossref","first-page":"662","DOI":"10.1111\/j.1432-1033.1997.00662.x","article-title":"Comparative stability and clearance of [Met30]transthyretin and [Met119]transthyretin","volume":"249","author":"Longo Alves","year":"1997","journal-title":"Eur J Biochem"},{"key":"10.1038\/labinvest.2013.83_bib13","doi-asserted-by":"crossref","first-page":"14420","DOI":"10.1074\/jbc.M010869200","article-title":"Internalization of transthyretin. Evidence of a novel yet unidentified receptor-associated protein (RAP)-sensitive receptor","volume":"276","author":"Sousa","year":"2001","journal-title":"J Biol Chem"},{"key":"10.1038\/labinvest.2013.83_bib14","doi-asserted-by":"crossref","first-page":"38176","DOI":"10.1074\/jbc.M002886200","article-title":"Evidence for the role of megalin in renal uptake of transthyretin","volume":"275","author":"Sousa","year":"2000","journal-title":"J Biol Chem"},{"key":"10.1038\/labinvest.2013.83_bib15","doi-asserted-by":"crossref","first-page":"3220","DOI":"10.1523\/JNEUROSCI.6012-08.2009","article-title":"Transthyretin internalization by sensory neurons is megalin mediated and necessary for its neuritogenic activity","volume":"29","author":"Fleming","year":"2009","journal-title":"J Neurosci"},{"key":"10.1038\/labinvest.2013.83_bib16","doi-asserted-by":"crossref","first-page":"517","DOI":"10.1016\/j.bbadis.2008.05.005","article-title":"Anti-apoptotic treatment reduces transthyretin deposition in a transgenic mouse model of Familial Amyloidotic Polyneuropathy","volume":"1782","author":"Macedo","year":"2008","journal-title":"Biochim Biophys Acta"},{"key":"10.1038\/labinvest.2013.83_bib17","doi-asserted-by":"crossref","first-page":"2415","DOI":"10.1021\/bi00223a017","article-title":"Production of recombinant human transthyretin with biological activities toward the understanding of the molecular basis of familial amyloidotic polyneuropathy (FAP)","volume":"30","author":"Furuya","year":"1991","journal-title":"Biochemistry"},{"key":"10.1038\/labinvest.2013.83_bib18","doi-asserted-by":"crossref","first-page":"21998","DOI":"10.1074\/jbc.M602302200","article-title":"Endoplasmic reticulum stress associated with extracellular aggregates. Evidence from transthyretin deposition in familial amyloid polyneuropathy","volume":"281","author":"Teixeira","year":"2006","journal-title":"J Biol Chem"},{"key":"10.1038\/labinvest.2013.83_bib19","doi-asserted-by":"crossref","first-page":"131","DOI":"10.1042\/BJ20070689","article-title":"Comparative in vitroex vivo activities of selected inhibitors of transthyretin aggregation: relevance in drug design","volume":"408","author":"Cardoso","year":"2007","journal-title":"Biochem J"},{"key":"10.1038\/labinvest.2013.83_bib20","doi-asserted-by":"crossref","first-page":"2012","DOI":"10.2353\/ajpath.2007.070403","article-title":"Induction of tau pathology by intracerebral infusion of amyloid-\u03b2-containing brain extract and by amyloid-\u03b2 deposition in APP \u00d7 Tau transgenic mice","volume":"171","author":"Bolmont","year":"2007","journal-title":"Am J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib21","first-page":"1497","article-title":"Analysis of amyloid deposition in a transgenic mouse model of homozygous familial amyloidotic polyneuropathy","volume":"150","author":"Kohno","year":"1997","journal-title":"Am J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib22","doi-asserted-by":"crossref","first-page":"481","DOI":"10.1002\/path.2618","article-title":"Chain reaction of amyloid fibril formation with induction of basement membrane in familial amyloidotic polyneuropathy","volume":"219","author":"Misumi","year":"2009","journal-title":"J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib23","first-page":"272","article-title":"An interaction between basement membrane and Alzheimer amyloid precursor proteins suggests a role in the pathogenesis of Alzheimer's disease","volume":"72","author":"Narindrasorasak","year":"1995","journal-title":"Lab Invest"},{"key":"10.1038\/labinvest.2013.83_bib24","doi-asserted-by":"crossref","first-page":"858","DOI":"10.3858\/emm.2009.41.12.096","article-title":"Fibroblasts in three dimensional matrices: cell migration and matrix remodeling","volume":"41","author":"Rhee","year":"2009","journal-title":"Exp Mol Med"},{"key":"10.1038\/labinvest.2013.83_bib25","first-page":"249","article-title":"Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study","volume":"141","author":"Yamaguchi","year":"1992","journal-title":"Am J Pathol"},{"key":"10.1038\/labinvest.2013.83_bib26","doi-asserted-by":"crossref","first-page":"148","DOI":"10.1016\/j.brainres.2009.05.098","article-title":"The activation of cannabinoid CB2 receptors stimulates in situin vitro beta-amyloid removal by human macrophages","volume":"1283","author":"Tol\u00f3n","year":"2009","journal-title":"Brain Res"},{"key":"10.1038\/labinvest.2013.83_bib27","doi-asserted-by":"crossref","first-page":"1136","DOI":"10.1093\/ndt\/17.6.1136","article-title":"Phagocytosis of dialysis-related amyloid deposits by macrophages","volume":"17","author":"Argil\u00e9s","year":"2002","journal-title":"Nephrol Dial Transplant"},{"key":"10.1038\/labinvest.2013.83_bib28","doi-asserted-by":"crossref","first-page":"138","DOI":"10.3109\/13506129.2012.711391","article-title":"AA-Amyloid is cleared by endogenous immunological mechanisms","volume":"19","author":"Nystr\u00f6m","year":"2012","journal-title":"Amyloid"},{"key":"10.1038\/labinvest.2013.83_bib29","doi-asserted-by":"crossref","first-page":"1942","DOI":"10.1073\/pnas.0904532106","article-title":"Mechanism of amyloid plaque formation suggests an intracellular basis of Abeta pathogenicity","volume":"107","author":"Friedrich","year":"2010","journal-title":"Proc Natl Acad Sci USA"},{"key":"10.1038\/labinvest.2013.83_bib30","doi-asserted-by":"crossref","first-page":"1905","DOI":"10.1002\/art.10335","article-title":"A pulse-chase study tracking the conversion of macrophage-endocytosed serum amyloid A into extracellular amyloid","volume":"46","author":"Kluve-Beckerman","year":"2002","journal-title":"Arthritis Rheum"},{"key":"10.1038\/labinvest.2013.83_bib31","doi-asserted-by":"crossref","first-page":"249","DOI":"10.1161\/CIRCHEARTFAILURE.108.788687","article-title":"Matrix metalloproteinases and their tissue inhibitors in cardiac amyloidosis: relationship to structural, functional myocardial changes and to light chain amyloid deposition","volume":"1","author":"Biolo","year":"2008","journal-title":"Circ Heart Fail"},{"key":"10.1038\/labinvest.2013.83_bib32","doi-asserted-by":"crossref","first-page":"240","DOI":"10.1111\/j.1750-3639.2008.00132.x","article-title":"Abeta-degrading enzymes in Alzheimer's disease","volume":"18","author":"Miners","year":"2008","journal-title":"Brain Pathol"},{"key":"10.1038\/labinvest.2013.83_bib33","doi-asserted-by":"crossref","first-page":"983","DOI":"10.1111\/j.1471-4159.1992.tb09352.x","article-title":"Characterization of neutral proteinases from Alzheimer-affected and control brain specimens: identification of calcium-dependent metalloproteinases from the hippocampus","volume":"58","author":"Backstrom","year":"1992","journal-title":"J Neurochem"},{"key":"10.1038\/labinvest.2013.83_bib34","doi-asserted-by":"crossref","first-page":"124","DOI":"10.1096\/fj.04-2022fje","article-title":"Up-regulation of the extracellular matrix remodeling genes, biglycan, neutrophil gelatinase-associated lipocalin, and matrix metalloproteinase-9 in familial amyloid polyneuropathy","volume":"19","author":"Sousa","year":"2005","journal-title":"FASEB J"},{"key":"10.1038\/labinvest.2013.83_bib35","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1096\/fj.05-4509com","article-title":"Doxycycline disrupts transthyretin amyloid: evidence from studies in a FAP transgenic mice model","volume":"20","author":"Cardoso","year":"2006","journal-title":"FASEB J"},{"key":"10.1038\/labinvest.2013.83_bib36","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1155\/2008\/549872","article-title":"Extracellular matrix markers for disease progression and follow-up of therapies in familial amyloid polyneuropathy V30M TTR-related","volume":"25","author":"Cardoso","year":"2008","journal-title":"Dis Markers"},{"key":"10.1038\/labinvest.2013.83_bib37","doi-asserted-by":"crossref","first-page":"101","DOI":"10.1007\/s11248-012-9632-0","article-title":"Human TTRV30M localization within podocytes in a transgenic mouse model of transthyretin related amyloidosis: does the environment play a role?","volume":"22","author":"Petrakis","year":"2013","journal-title":"Transgenic Res"},{"key":"10.1038\/labinvest.2013.83_bib38","doi-asserted-by":"crossref","first-page":"e14343","DOI":"10.1371\/journal.pone.0014343","article-title":"Uptake of aggregating transthyretin by fat body in a Drosophila model for TTR-associated amyloidosis","volume":"5","author":"Pokrzywa","year":"2010","journal-title":"PLoS One"},{"key":"10.1038\/labinvest.2013.83_bib39","doi-asserted-by":"crossref","first-page":"46","DOI":"10.1093\/ndt\/18.1.46","article-title":"Cellular uptake of beta2M and AGE-beta2M in synovial fibroblasts and macrophages","volume":"18","author":"O'Neill","year":"2003","journal-title":"Nephrol Dial Transplant"},{"key":"10.1038\/labinvest.2013.83_bib40","doi-asserted-by":"crossref","first-page":"141","DOI":"10.1016\/j.brainres.2011.02.078","article-title":"Regulation of matrix metalloproteinase 2 by oligomeric amyloid \u03b2 protein","volume":"1387","author":"Li","year":"2011","journal-title":"Brain Res"},{"key":"10.1038\/labinvest.2013.83_bib41","doi-asserted-by":"crossref","first-page":"120","DOI":"10.3389\/fphar.2012.00120","article-title":"Astrocytes as a source for extracellular matrix molecules and cytokines","volume":"3","author":"Wiese","year":"2012","journal-title":"Front Pharmacol"},{"key":"10.1038\/labinvest.2013.83_bib42","doi-asserted-by":"crossref","first-page":"453","DOI":"10.1038\/nm838","article-title":"Adult mouse astrocytes degrade amyloid-beta in vitroin situ","volume":"9","author":"Wyss-Coray","year":"2003","journal-title":"Nat Med"},{"key":"10.1038\/labinvest.2013.83_bib43","doi-asserted-by":"crossref","first-page":"3052","DOI":"10.1016\/j.febslet.2011.08.027","article-title":"Astrocytes contain amyloid-\u03b2 annular protofibrils in Alzheimer's disease brains","volume":"585","author":"Lasagna-Reeves","year":"2011","journal-title":"FEBS Lett"},{"key":"10.1038\/labinvest.2013.83_bib44","doi-asserted-by":"crossref","first-page":"1023","DOI":"10.1016\/j.jaad.2010.09.735","article-title":"Role of oligomers in the amyloidogenesis of primary cutaneous amyloidosis","volume":"65","author":"Clos","year":"2011","journal-title":"J Am Acad Dermatol"},{"key":"10.1038\/labinvest.2013.83_bib45","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"}],"container-title":["Laboratory Investigation"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/www.nature.com\/articles\/labinvest201383.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/labinvest201383","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0023683722009138?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0023683722009138?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"http:\/\/www.nature.com\/articles\/labinvest201383.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,9,20]],"date-time":"2025-09-20T19:33:31Z","timestamp":1758396811000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0023683722009138"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,8]]},"references-count":45,"journal-issue":{"issue":"8","published-print":{"date-parts":[[2013,8]]}},"alternative-id":["S0023683722009138"],"URL":"https:\/\/doi.org\/10.1038\/labinvest.2013.83","relation":{},"ISSN":["0023-6837"],"issn-type":[{"value":"0023-6837","type":"print"}],"subject":[],"published":{"date-parts":[[2013,8]]},"assertion":[{"value":"Elsevier","name":"publisher","label":"This article is maintained by"},{"value":"Fibroblasts endocytose and degrade transthyretin aggregates in transthyretin-related amyloidosis","name":"articletitle","label":"Article Title"},{"value":"Laboratory Investigation","name":"journaltitle","label":"Journal Title"},{"value":"https:\/\/doi.org\/10.1038\/labinvest.2013.83","name":"articlelink","label":"CrossRef DOI link to publisher maintained version"},{"value":"article","name":"content_type","label":"Content Type"},{"value":"\u00a9 2013 United States & Canadian Academy of Pathology.","name":"copyright","label":"Copyright"}]}}