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Amyloidogenicity and cytotoxicity of islet amyloid polypeptide

2001; Wiley; Volume: 60; Issue: 6 Linguagem: Inglês

10.1002/1097-0282(2001)60

1097-0282

Aphrodite Kapurniotu,

Pancreatitis Pathology and Treatment

Peptide ScienceVolume 60, Issue 6 p. 438-459 Amyloidogenicity and cytotoxicity of islet amyloid polypeptide Aphrodite Kapurniotu, Corresponding Author Aphrodite Kapurniotu [email protected] Physiological-Chemical Institute, University of Tübingen, Hoppe-Seylerstrasse 4, D-72076 Tübingen, GermanyPhysiological-Chemical Institute, University of Tübingen, Hoppe-Seylerstrasse 4, D-72076 Tübingen, GermanySearch for more papers by this author Aphrodite Kapurniotu, Corresponding Author Aphrodite Kapurniotu [email protected] Physiological-Chemical Institute, University of Tübingen, Hoppe-Seylerstrasse 4, D-72076 Tübingen, GermanyPhysiological-Chemical Institute, University of Tübingen, Hoppe-Seylerstrasse 4, D-72076 Tübingen, GermanySearch for more papers by this author First published: 12 January 2004 https://doi.org/10.1002/1097-0282(2001)60:6 3.0.CO;2-ACitations: 93Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onEmailFacebookTwitterLinkedInRedditWechat Abstract Insoluble amyloid formation by islet amyloid polypeptide (IAPP) in the islets of Langerhans of the pancreas is a major pathophysiological feature of noninsulin dependent diabetes mellitus (NIDDM) or type II diabetes. Because in vivo formed amyloid colocalizes with areas of cell degeneration and IAPP amyloid aggregates are cytotoxic per se, the process of IAPP amyloid formation has been strongly associated with the progressive pancreatic cell degeneration and thus much of the pathology of type II diabetes. IAPP is a pancreatic polypeptide of 37 residues that, in its soluble form, is believed to play a role as a regulator of glucose homeostasis. The molecular cause and mechanism of the conversion of soluble IAPP into insoluble amyloid aggregates in vivo and its role in disease progress still remain to be clarified. Nevertheless, in the past few years significant progress has been made in understanding the amyloidogenesis pathway of IAPP in vitro and gaining insight into the structural and conformational “requirements” of IAPP amyloidogenesis and related cytotoxic effects. Importantly, several of the studies have revealed significant similarities of the above features of IAPP to other amyloidogenic polypeptides such as the β-amyloid polypeptide Aβ. This suggests that, at the molecular level, amyloidogenesis, and possibly related cell degeneration and disease pathogenesis by completely different polypeptide sequences, may obey to common structural and conformational “rules” and follow similar molecular pathways. 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