{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,24]],"date-time":"2026-09-24T23:17:20Z","timestamp":1790291840430,"version":"4.1.0"},"reference-count":66,"publisher":"Portland Press Ltd.","issue":"1","content-domain":{"domain":["portlandpress.com"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2010,11,15]]},"abstract":"<jats:p>Misfolding of the islet \u03b2-cell peptide hA (human amylin) into \u03b2-sheet-containing oligomers is linked to \u03b2-cell apoptosis and the pathogenesis of T2DM (Type 2 diabetes mellitus). In the present study, we have investigated the possible effects on hA misfolding of the chaperones HSP (heat-shock protein) 70, GRP78\/BiP (glucose-regulated protein of 78\u00a0kDa\/immunoglobulin heavy-chain-binding protein) and HSP40\/DnaJ. We demonstrate that hA underwent spontaneous time-dependent \u03b2-sheet formation and aggregation by thioflavin-T fluorescence in solution, whereas\u00a0rA (rat amylin) did not. HSP70, GRP78\/BiP and HSP40\/DnaJ each independently suppressed hA misfolding. Maximal molar protein\/hA ratios at which chaperone activity was detected were 1:200 (HSP70, HSP40\/DnaJ and GRP78\/BiP). By contrast, none of the chaperones modified the secondary structure of rA. hA, but not rA, was co-precipitated independently with HSP70 and GRP78\/BiP by anti-amylin antibodies. As these effects occur at molar ratios consistent with chaperone binding to relatively rare misfolded hA species, we conclude that HSP70 and GRP78\/BiP can detect and bind misfolded hA oligomers, thereby effectively protecting hA against bulk misfolding and irreversible aggregation. Defective \u03b2-cell chaperone biology could contribute to hA misfolding and initiation of apoptosis in T2DM.<\/jats:p>","DOI":"10.1042\/bj20100434","type":"journal-article","created":{"date-parts":[[2010,8,25]],"date-time":"2010-08-25T09:05:26Z","timestamp":1282727126000},"page":"113-121","update-policy":"https:\/\/doi.org\/10.1042\/crossmark_policy","source":"Crossref","is-referenced-by-count":46,"title":["The chaperone proteins HSP70, HSP40\/DnaJ and GRP78\/BiP suppress misfolding and formation of \u03b2-sheet-containing aggregates by human amylin: a potential role for defective chaperone biology in Type\u00a02 diabetes"],"prefix":"10.1042","volume":"432","author":[{"given":"Vita","family":"Chien","sequence":"first","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacqueline\u00a0F.","family":"Aitken","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Shaoping","family":"Zhang","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"},{"name":"Maurice Wilkins Centre for Molecular BioDiscovery, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Christina\u00a0M.","family":"Buchanan","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony","family":"Hickey","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Thomas","family":"Brittain","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Garth\u00a0J.\u00a0S.","family":"Cooper","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"},{"name":"Maurice Wilkins Centre for Molecular BioDiscovery, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"},{"name":"Medical Research Council Immunochemistry Unit, Department of Biochemistry, University of Oxford, Oxford OX1 3QU, U.K."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kerry\u00a0M.","family":"Loomes","sequence":"additional","affiliation":[{"name":"School of Biological Sciences, Faculty of Science, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"},{"name":"Maurice Wilkins Centre for Molecular BioDiscovery, University of Auckland, Private Bag 92019, Auckland 1142, New Zealand"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"288","published-online":{"date-parts":[[2010,10,25]]},"reference":[{"key":"2021112217350315600_B1","doi-asserted-by":"crossref","first-page":"1225","DOI":"10.1056\/NEJM198805123181902","article-title":"Impaired pulsatile secretion of insulin in relatives of patients with non-insulin-dependent diabetes","volume":"318","author":"O'Rahilly","year":"1988","journal-title":"N. 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