{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2023,11,15]],"date-time":"2023-11-15T04:40:45Z","timestamp":1700023245823},"reference-count":45,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2013,1,2]],"date-time":"2013-01-02T00:00:00Z","timestamp":1357084800000},"content-version":"vor","delay-in-days":1737,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Cell Biology International"],"published-print":{"date-parts":[[2008,4]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Amyloid deposition is a common feature of Alzheimer's disease and type 2 diabetes related to \u03b2\u2010amyloid peptides (\u03b2A) and human amylin (hA), respectively. Both \u03b2A and hA form aggregates and fibrils and kill cultured cells. To investigate whether \u03b2A and hA display peptide\u2010specific toxicity on cultured islet \u03b2\u2010cells, we examined the effects of <jats:sup>1\u201340<\/jats:sup>\u03b2A and <jats:sup>25\u201335<\/jats:sup>\u03b2A peptides on hA\u2010mediated cell death and [<jats:sup>125<\/jats:sup>I\u2010Tyr<jats:sup>37<\/jats:sup>]hA precipitation. Synthetic hA aggregated in solution and evoked both conformation\u2010 and sequence\u2010dependent cell death. While neither <jats:sup>1\u201340<\/jats:sup>\u03b2A nor <jats:sup>25\u201335<\/jats:sup>\u03b2A was toxic to islet \u03b2\u2010cells, they suppressed hA\u2010evoked cell death in a concentration\u2010dependent and saturable manner. Only <jats:sup>1\u201340<\/jats:sup>\u03b2A, but not <jats:sup>25\u201335<\/jats:sup>\u03b2A, showed trophic effects on cultured islet \u03b2\u2010cells and inhibited the precipitation of [<jats:sup>125<\/jats:sup>I]hA caused by hA. These results suggest that <jats:sup>25\u201335<\/jats:sup>\u03b2A does not interfere with hA\u2010mediated fibril formation. Suppression of hA\u2010evoked death of cultured pancreatic islet \u03b2\u2010cells by the \u03b2A peptides is likely to occur through a competing interaction at these cells.<\/jats:p>","DOI":"10.1016\/j.cellbi.2007.12.016","type":"journal-article","created":{"date-parts":[[2008,1,14]],"date-time":"2008-01-14T12:44:37Z","timestamp":1200314677000},"page":"447-455","update-policy":"http:\/\/dx.doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":2,"title":["\u03b2\u2010Amyloid peptides <sup>1\u201340<\/sup>\u03b2A and <sup>25\u201335<\/sup>\u03b2A suppress human amylin\u2010mediated death of RINm5F islet \u03b2\u2010cells with distinct actions on fibril 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