期刊
FEBS LETTERS
卷 587, 期 21, 页码 3406-3411出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2013.09.006
关键词
Type 2 diabetes; hIAPP; 7B2; proSAAS
资金
- NIH [DK49703]
The deposition of fibrillated human islet beta-cell peptide islet amyloid polypeptide (hIAPP) into amyloid plaques is characteristic of the pathogenesis of islet cell death during type 2 diabetes. We investigated the effects of the neuroendocrine secretory proteins 7B2 and proSAAS on hIAPP fibrillation in vitro and on cytotoxicity. In vitro, 21-kDa 7B2 and proSAAS blocked hIAPP fibrillation. Structure-function studies showed that a central region within 21-kDa 7B2 is important in this effect and revealed the importance of the N-terminal region of proSAAS. Both chaperones blocked the cytotoxic effects of exogenous hIAPP on Rin5f cells; 7B2 generated by overexpression was also effective. ProSAAS and 7B2 may perform a chaperone role as secretory anti-aggregants in normal islet cell function and in type 2 diabetes. Structured summary of protein interactions: hIAPP and hIAPP bind by fluorescence technology (View interaction) (C) 2013 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved.
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