| Primary Identifier | IPR000443 | Type | Family |
| Short Name | IAPP |
| description | Islet amyloid polypeptide (IAPP) (also known as diabetes-associated peptideor amylin) is a pancreatic islet hormone that is stored with insulin in betacell granules []. IAPP has a propensity to form islet cell-disrupting amyloid deposits, and opposes the action of insulin in peripheral tissues; the peptide may therefore have a significant role in the development of Type2 diabetes mellitus []. It is thought that an intrinsic structural motif ofIAPP, which only occurs in species that develop age-associated or Type 2 diabetes (e.g., Homo sapiens (Human) and Felis silvestris catus (Cat)), is linked to its amyloidogenicity [].IAPP is a short, 37-residue peptide. The hormone selectively inhibits insulin-stimulated glucose utilisation and glycogen deposition in muscle,but does not affect adipocyte glucose metabolism. The sequences of amylinand the calcitonin gene-related peptides (CGRPs) show strong similarity:both peptides have a conserved N-terminal intramolecular disulphide bridge,and both have a C-terminal glycine, which suggests that the C-terminalresidue of amylin, like that of CGRP, is amidated [].Near- and far-UV CD spectra of human alpha CGRP, analogues and fragments ofCGRP, and amylin have been recorded in aqueous solution and in trifluoro-ethanol/water mixtures []. The peptides were shown to contain significantamounts of α-helix in aqueous solution, this amount increasing upon addition of TFE. Amylin appears to contain less helix than CGRP []. |
