{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,7,30]],"date-time":"2025-07-30T14:33:20Z","timestamp":1753886000826,"version":"3.41.2"},"reference-count":38,"publisher":"Wiley","issue":"1","license":[{"start":{"date-parts":[[2008,6,10]],"date-time":"2008-06-10T00:00:00Z","timestamp":1213056000000},"content-version":"vor","delay-in-days":161,"URL":"http:\/\/creativecommons.org\/licenses\/by\/3.0\/"}],"funder":[{"DOI":"10.13039\/501100004359","name":"Swedish Research Council","doi-asserted-by":"crossref","id":[{"id":"10.13039\/501100004359","id-type":"DOI","asserted-by":"crossref"}]},{"name":"Swedish Diabetes Association"},{"name":"Foundation in Memory of Lars Hierta"},{"name":"Lions Research Fund against Disease"},{"name":"European Union FP6 Program"},{"name":"\u00d6sterg\u00f6tland County Council"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Journal of Diabetes Research"],"published-print":{"date-parts":[[2008,1]]},"abstract":"<jats:p>Amyloid formation is cytotoxic and can activate the caspase cascade. Here, we monitor caspase\u20103\u2010like activity as reduction of fluorescence resonance energy transfer (FRET)  using the contstruct  pFRET2\u2010DEVD containing enhanced cyan fluorescent protin (EYFP) linked by the caspase\u20103 specific cleavage site residues DEVD. Beta\u2010TC\u20106 cells were transfected, and  the fluoorescence was measured at 440\u2009nm excitation and 535\u2009nm (EYFP) and 480\u2009nm (ECFP) emission wavelength. Cells were incubated with recombinant pro lset Amyloid Polypeptide (<jats:italic>rec<\/jats:italic> prolAPP) or the processing metabolites of prolAPP;   the N\u2010terminal flanking peptide withIAPP (<jats:italic>rec<\/jats:italic>N+IAPP); IAPP with the C\u2010terminal flanking peptied (<jats:italic>rec<\/jats:italic>IAPP+C) and lslet Amyloid  Polypeptide (<jats:italic>rec<\/jats:italic>IAPP) . Peptides were added in solubilized from (50\u2009<jats:italic>\u03bc<\/jats:italic>M) or as performed amyloid\u2010like fibrils, or as a combination of these. FRET was measured and incubation with a mixture of solubilized peptide and performed fibrils resulted in loss of  FRET and apoptosis was determined to occure in cells incubated with <jats:italic>rec<\/jats:italic>proIAPP (49%), <jats:italic>rec<\/jats:italic>N+IAPP (46%), <jats:italic>rec<\/jats:italic>IAPP (72%) and <jats:italic>rec<\/jats:italic>IAPP+C  (59%). These results show that proIAPP and the processing intermediates reside the same cell toxic capacity as IAPP, and they can all have a central role in the reduction of beta\u2010cell number in type 2 diabetes.<\/jats:p>","DOI":"10.1155\/2008\/865850","type":"journal-article","created":{"date-parts":[[2008,6,12]],"date-time":"2008-06-12T10:53:36Z","timestamp":1213268016000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":15,"title":["Real\u2010Time  Monitoring of Apoptosis by Caspase\u20103\u2010Like Protease Induced FRET Reduction Triggered by Amyloid Aggregation"],"prefix":"10.1155","volume":"2008","author":[{"given":"Johan F.","family":"Paulsson","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sebastian W.","family":"Schultz","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Martin","family":"K\u00f6hler","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ingo","family":"Leibiger","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Per-Olof","family":"Berggren","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Gunilla T.","family":"Westermark","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2008,6,10]]},"reference":[{"key":"e_1_2_7_1_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2006.04.014"},{"key":"e_1_2_7_2_2","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 E. 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