| First Author | Peinado JR | Year | 2013 |
| Journal | FEBS Lett | Volume | 587 |
| Issue | 21 | Pages | 3406-11 |
| PubMed ID | 24042052 | Mgi Jnum | J:202473 |
| Mgi Id | MGI:5519162 | Doi | 10.1016/j.febslet.2013.09.006 |
| Citation | Peinado JR, et al. (2013) Blockade of islet amyloid polypeptide fibrillation and cytotoxicity by the secretory chaperones 7B2 and proSAAS. FEBS Lett 587(21):3406-11 |
| abstractText | 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. |
