Department of Medical Cell Biology and Immunology, Uppsala University, Uppsala, Sweden.
Physiol Rev. 2011 Jul;91(3):795-826. doi: 10.1152/physrev.00042.2009.
Islet amyloid polypeptide (IAPP, or amylin) is one of the major secretory products of β-cells of the pancreatic islets of Langerhans. It is a regulatory peptide with putative function both locally in the islets, where it inhibits insulin and glucagon secretion, and at distant targets. It has binding sites in the brain, possibly contributing also to satiety regulation and inhibits gastric emptying. Effects on several other organs have also been described. IAPP was discovered through its ability to aggregate into pancreatic islet amyloid deposits, which are seen particularly in association with type 2 diabetes in humans and with diabetes in a few other mammalian species, especially monkeys and cats. Aggregated IAPP has cytotoxic properties and is believed to be of critical importance for the loss of β-cells in type 2 diabetes and also in pancreatic islets transplanted into individuals with type 1 diabetes. This review deals both with physiological aspects of IAPP and with the pathophysiological role of aggregated forms of IAPP, including mechanisms whereby human IAPP forms toxic aggregates and amyloid fibrils.
胰岛淀粉样多肽（IAPP，或胰岛淀粉）是胰岛β细胞的主要分泌产物之一。它是一种调节肽，在胰岛内具有潜在的功能，可以抑制胰岛素和胰高血糖素的分泌，并在远处的靶标发挥作用。它在大脑中有结合位点，可能也有助于调节饱腹感并抑制胃排空。还描述了对其他几种器官的影响。IAPP 是通过其能够聚集形成胰岛淀粉样沉积而被发现的，这种沉积在人类 2 型糖尿病和少数其他哺乳动物（尤其是猴子和猫）的糖尿病中特别常见。聚集的 IAPP 具有细胞毒性，被认为对 2 型糖尿病中β细胞的丧失以及移植到 1 型糖尿病患者体内的胰岛具有至关重要的作用。本综述既涉及 IAPP 的生理方面，也涉及聚集形式的 IAPP 的病理生理作用，包括人类 IAPP 形成毒性聚集物和淀粉样纤维的机制。
