Other Names: Islet Amyloid Polypeptide; IAPP
Amylin, also known as Islet Amyloid Polypeptide (IAPP), is secreted from pancreatic beta-cells in response to meals. It inhibits the appearance of new glucose the plasma by inhibiting the secretion of the hormone glucagon. Amylin functions synergistically with insulin to regulate blood glucose levels. It was recently shown that in healthy men a high-carbohydrate meal enhances amylin levels more than a high-fat meal [Eller, LK et al. Clin Endocrinol (Oxf). 68, 890 (2008)]. Amylin was negatively correlated with satiety and insulin and was posititively correlated to hunger and the desire to eat. Administered peripherally, amylin reduces food intake, slows weight gain and selectively reduces body fat in diet-induced obese rats. Amylin has been associated with type II diabetes for some time [Cooper, GJ et al. Proc Natl Acad Sci USA 84, 8628 (1987)], but a direct causitive role has been hard to establish. Large extracellular oligomers frequently occur in diabetic islets. The large oligomers were adjacent to amyloid fibrils and were associated with apoptosis. Recent results suggest that amylin can induce apoptic cell death in certain cultured cells and that may be relevant to the development of type II diabetes.Amylin inhibits bone reabsorption by osteoclasts, induces osteoblast proliferation and promotes bone formation [Naot, D and Cornish, J. Bone. 43, 183, (2008)].