{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,7,2]],"date-time":"2026-07-02T11:10:13Z","timestamp":1782990613631,"version":"3.54.5"},"reference-count":36,"publisher":"Elsevier BV","issue":"5","license":[{"start":{"date-parts":[[2013,2,1]],"date-time":"2013-02-01T00:00:00Z","timestamp":1359676800000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"},{"start":{"date-parts":[[2020,9,8]],"date-time":"2020-09-08T00:00:00Z","timestamp":1599523200000},"content-version":"vor","delay-in-days":2776,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Biological Chemistry"],"published-print":{"date-parts":[[2013,2]]},"DOI":"10.1074\/jbc.m112.438457","type":"journal-article","created":{"date-parts":[[2012,12,11]],"date-time":"2012-12-11T03:43:09Z","timestamp":1355197389000},"page":"3553-3559","source":"Crossref","is-referenced-by-count":32,"title":["Matrix Metalloproteinase-9 Reduces Islet Amyloid Formation by Degrading Islet Amyloid Polypeptide"],"prefix":"10.1016","volume":"288","author":[{"given":"Kathryn","family":"Aston-Mourney","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sakeneh","family":"Zraika","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jayalakshmi","family":"Udayasankar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shoba L.","family":"Subramanian","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pattie S.","family":"Green","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Steven E.","family":"Kahn","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rebecca L.","family":"Hull","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1074\/jbc.M112.438457_bib1","doi-asserted-by":"crossref","first-page":"417","DOI":"10.1007\/BF01219652","article-title":"The influence of amyloid deposits on the islet volume in maturity onset diabetes mellitus","volume":"15","author":"Westermark","year":"1978","journal-title":"Diabetologia"},{"key":"10.1074\/jbc.M112.438457_bib2","first-page":"151","article-title":"Islet amyloid, increased A-cells, reduced B-cells, and exocrine fibrosis: quantitative changes in the pancreas in type 2 diabetes","volume":"9","author":"Clark","year":"1988","journal-title":"Diabetes Res."},{"key":"10.1074\/jbc.M112.438457_bib3","doi-asserted-by":"crossref","first-page":"2632","DOI":"10.1016\/j.ajpath.2011.02.036","article-title":"\u03b2-Cell loss and \u03b2-cell apoptosis in human type 2 diabetes are related to islet amyloid deposition","volume":"178","author":"Jurgens","year":"2011","journal-title":"Am. J. Pathol."},{"key":"10.1074\/jbc.M112.438457_bib4","doi-asserted-by":"crossref","first-page":"634","DOI":"10.2337\/diab.39.5.634","article-title":"Evidence of cosecretion of islet amyloid polypeptide and insulin by \u03b2-cells","volume":"39","author":"Kahn","year":"1990","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib5","doi-asserted-by":"crossref","first-page":"756","DOI":"10.1038\/368756a0","article-title":"Pancreatic islet cell toxicity of amylin associated with type 2 diabetes mellitus","volume":"368","author":"Lorenzo","year":"1994","journal-title":"Nature"},{"key":"10.1074\/jbc.M112.438457_bib6","doi-asserted-by":"crossref","first-page":"53","DOI":"10.1042\/bj3430053","article-title":"Role of Ca2+ in apoptosis evoked by human amylin in pancreatic islet \u03b2-cells","volume":"343","author":"Bai","year":"1999","journal-title":"Biochem. J."},{"key":"10.1074\/jbc.M112.438457_bib7","doi-asserted-by":"crossref","first-page":"491","DOI":"10.2337\/diabetes.48.3.491","article-title":"The mechanism of islet amyloid polypeptide toxicity is membrane disruption by intermediate-sized toxic amyloid particles","volume":"48","author":"Janson","year":"1999","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib8","doi-asserted-by":"crossref","first-page":"626","DOI":"10.1007\/s00125-008-1255-x","article-title":"Oxidative stress is induced by islet amyloid formation and time-dependently mediates amyloid-induced \u03b2 cell apoptosis","volume":"52","author":"Zraika","year":"2009","journal-title":"Diabetologia"},{"key":"10.1074\/jbc.M112.438457_bib9","doi-asserted-by":"crossref","first-page":"5036","DOI":"10.1073\/pnas.87.13.5036","article-title":"Islet amyloid polypeptide: pinpointing amino acid residues linked to amyloid fibril formation","volume":"87","author":"Westermark","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.438457_bib10","doi-asserted-by":"crossref","first-page":"1811","DOI":"10.1021\/bi981658g","article-title":"Effects of sequential proline substitutions on amyloid formation by human amylin20\u201329","volume":"38","author":"Moriarty","year":"1999","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.438457_bib11","doi-asserted-by":"crossref","first-page":"1258","DOI":"10.1007\/BF00400803","article-title":"Chronic overproduction of islet amyloid polypeptide\/amylin in transgenic mice: lysosomal localization of human islet amyloid polypeptide and lack of marked hyperglycaemia or hyperinsulinaemia","volume":"36","author":"H\u00f6ppener","year":"1993","journal-title":"Diabetologia"},{"key":"10.1074\/jbc.M112.438457_bib12","doi-asserted-by":"crossref","first-page":"1457","DOI":"10.2337\/diab.43.12.1457","article-title":"Pancreatic expression and secretion of human islet amyloid polypeptide in a transgenic mouse","volume":"43","author":"D'Alessio","year":"1994","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib13","doi-asserted-by":"crossref","first-page":"7283","DOI":"10.1073\/pnas.93.14.7283","article-title":"Spontaneous diabetes mellitus in transgenic mice expressing human islet amyloid polypeptide","volume":"93","author":"Janson","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.438457_bib14","doi-asserted-by":"crossref","first-page":"3492","DOI":"10.1073\/pnas.93.8.3492","article-title":"Islet amyloid formation associated with hyperglycemia in transgenic mice with pancreatic \u03b2 cell expression of human islet amyloid polypeptide","volume":"93","author":"Verchere","year":"1996","journal-title":"Proc. Natl. Acad. Sci. U.S.A."},{"key":"10.1074\/jbc.M112.438457_bib15","doi-asserted-by":"crossref","first-page":"372","DOI":"10.2337\/diabetes.52.2.372","article-title":"Increased dietary fat promotes islet amyloid formation and \u03b2-cell secretory dysfunction in a transgenic mouse model of islet amyloid","volume":"52","author":"Hull","year":"2003","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib16","doi-asserted-by":"crossref","first-page":"166","DOI":"10.1007\/s00125-011-2338-7","article-title":"cJUN N-terminal kinase (JNK) activation mediates islet amyloid-induced \u03b2 cell apoptosis in cultured human islet amyloid polypeptide transgenic mouse islets","volume":"55","author":"Subramanian","year":"2012","journal-title":"Diabetologia"},{"key":"10.1074\/jbc.M112.438457_bib17","doi-asserted-by":"crossref","first-page":"18177","DOI":"10.1074\/jbc.M109.082032","article-title":"Neprilysin impedes islet amyloid formation by inhibition of fibril formation rather than peptide degradation","volume":"285","author":"Zraika","year":"2010","journal-title":"J. Biol. Chem."},{"key":"10.1074\/jbc.M112.438457_bib18","doi-asserted-by":"crossref","first-page":"2315","DOI":"10.2337\/diabetes.52.9.2315","article-title":"An insulin-degrading enzyme inhibitor decreases amylin degradation, increases amylin-induced cytotoxicity, and increases amyloid formation in insulinoma cell cultures","volume":"52","author":"Bennett","year":"2003","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib19","doi-asserted-by":"crossref","first-page":"2989","DOI":"10.1007\/s00125-012-2678-y","article-title":"Degradation of islet amyloid polypeptide by neprilysin","volume":"55","author":"Guan","year":"2012","journal-title":"Diabetologia"},{"key":"10.1074\/jbc.M112.438457_bib20","doi-asserted-by":"crossref","first-page":"7910","DOI":"10.1523\/JNEUROSCI.16-24-07910.1996","article-title":"Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-\u03b2 peptide1\u201340","volume":"16","author":"Backstrom","year":"1996","journal-title":"J. Neurosci."},{"key":"10.1074\/jbc.M112.438457_bib21","doi-asserted-by":"crossref","first-page":"1755","DOI":"10.1006\/bbrc.1994.2872","article-title":"Proteolysis of A\u03b2 peptide from Alzheimer disease brain by gelatinase A","volume":"205","author":"Roher","year":"1994","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1074\/jbc.M112.438457_bib22","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1152\/physrev.00048.2003","article-title":"Dual role of matrix metalloproteinases (matrixins) in intimal thickening and atherosclerotic plaque rupture","volume":"85","author":"Newby","year":"2005","journal-title":"Physiol. Rev."},{"key":"10.1074\/jbc.M112.438457_bib23","first-page":"47","article-title":"Gelatinases and inhibitors of gelatinases in pancreatic islets and islet cell tumors","volume":"10","author":"Tomita","year":"1997","journal-title":"Mod. Pathol."},{"key":"10.1074\/jbc.M112.438457_bib24","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1146\/annurev.cellbio.17.1.463","article-title":"How matrix metalloproteinases regulate cell behavior","volume":"17","author":"Sternlicht","year":"2001","journal-title":"Annu. Rev. Cell Dev. Biol."},{"key":"10.1074\/jbc.M112.438457_bib25","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.2337\/diabetes.54.7.2235","article-title":"Long-term treatment with rosiglitazone and metformin reduces the extent of, but does not prevent, islet amyloid deposition in mice expressing the gene for human islet amyloid polypeptide","volume":"54","author":"Hull","year":"2005","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib26","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.bbrc.2006.12.187","article-title":"Glucose- and time-dependence of islet amyloid formation in vitro","volume":"354","author":"Zraika","year":"2007","journal-title":"Biochem. Biophys. Res. Commun."},{"key":"10.1074\/jbc.M112.438457_bib27","doi-asserted-by":"crossref","first-page":"e11499","DOI":"10.1371\/journal.pone.0011499","article-title":"Gene expression profiles of \u03b2-cell enriched tissue obtained by laser capture microdissection from subjects with type 2 diabetes","volume":"5","author":"Marselli","year":"2010","journal-title":"PloS One"},{"key":"10.1074\/jbc.M112.438457_bib28","doi-asserted-by":"crossref","first-page":"827","DOI":"10.1083\/jcb.143.3.827","article-title":"TGF-\u03b2 plays a key role in morphogenesis of the pancreatic islets of Langerhans by controlling the activity of the matrix metalloproteinase MMP-2","volume":"143","author":"Miralles","year":"1998","journal-title":"J. Cell Biol."},{"key":"10.1074\/jbc.M112.438457_bib29","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1242\/dev.127.12.2617","article-title":"Impaired migration and delayed differentiation of pancreatic islet cells in mice lacking EGF receptors","volume":"127","author":"Miettinen","year":"2000","journal-title":"Development"},{"key":"10.1074\/jbc.M112.438457_bib30","doi-asserted-by":"crossref","first-page":"2612","DOI":"10.2337\/diabetes.54.9.2612","article-title":"Matrix metalloproteinases contribute to insulin insufficiency in Zucker diabetic fatty rats","volume":"54","author":"Zhou","year":"2005","journal-title":"Diabetes"},{"key":"10.1074\/jbc.M112.438457_bib31","doi-asserted-by":"crossref","first-page":"6427","DOI":"10.1021\/bi00076a016","article-title":"Comparative sequence specificities of human 72- and 92-kDa gelatinases (type IV collagenases) and PUMP (matrilysin)","volume":"32","author":"Netzel-Arnett","year":"1993","journal-title":"Biochemistry"},{"key":"10.1074\/jbc.M112.438457_bib32","doi-asserted-by":"crossref","first-page":"661","DOI":"10.1038\/90273","article-title":"Determination of protease cleavage site motifs using mixture-based oriented peptide libraries","volume":"19","author":"Turk","year":"2001","journal-title":"Nat. Biotechnol."},{"key":"10.1074\/jbc.M112.438457_bib33","doi-asserted-by":"crossref","first-page":"5724","DOI":"10.1111\/j.1742-4658.2006.05562.x","article-title":"The minimal amyloid-forming fragment of the islet amyloid polypeptide is a glycolipid-binding domain","volume":"273","author":"Levy","year":"2006","journal-title":"FEBS J."},{"key":"10.1074\/jbc.M112.438457_bib34","doi-asserted-by":"crossref","first-page":"705","DOI":"10.1021\/jp908436s","article-title":"Aggregation properties of the peptide fragments derived from the 17\u201329 region of the human and rat IAPP: a comparative study with two PEG-conjugated variants of the human sequence","volume":"114","author":"Mazzaglia","year":"2010","journal-title":"J. Phys. Chem. B"},{"key":"10.1074\/jbc.M112.438457_bib35","doi-asserted-by":"crossref","first-page":"1375","DOI":"10.1006\/jmbi.1999.3286","article-title":"Analysis of amylin cleavage products provides new insights into the amyloidogenic region of human amylin","volume":"294","author":"Nilsson","year":"1999","journal-title":"J. Mol. Biol."},{"key":"10.1074\/jbc.M112.438457_bib36","doi-asserted-by":"crossref","first-page":"3629","DOI":"10.1210\/jc.2004-0405","article-title":"Islet amyloid: a critical entity in the pathogenesis of type 2 diabetes","volume":"89","author":"Hull","year":"2004","journal-title":"J. Clin. Endocrinol. Metab."}],"container-title":["Journal of Biological Chemistry"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820464695?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S0021925820464695?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/syndication.highwire.org\/content\/doi\/10.1074\/jbc.M112.438457","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2022,1,4]],"date-time":"2022-01-04T15:25:34Z","timestamp":1641309934000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S0021925820464695"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2013,2]]},"references-count":36,"journal-issue":{"issue":"5","published-print":{"date-parts":[[2013,2]]}},"alternative-id":["S0021925820464695"],"URL":"https:\/\/doi.org\/10.1074\/jbc.m112.438457","relation":{},"ISSN":["0021-9258"],"issn-type":[{"value":"0021-9258","type":"print"}],"subject":[],"published":{"date-parts":[[2013,2]]}}}