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Amylin, also known as islet amyloid-like polypeptide (IAPP), is a polypeptide composed of 37 amino acid residues, stimulated by glucose or other nutrients, secreted by islet β cells and insulin at the same time. Studies have shown that the amino acid sequence of human amylin 20-29 is the sequence of amyloid production, which can produce amyloid accumulation in pancreatic islets, have toxic effects on β cells, and have been insulin secretion. Leading to insulin secretion disorder and β cell failure may play an important role in the secondary failure of sulfonylurea drugs and β cell failure in type 2 diabetes mellitus.
Amylin is co-located and secreted with insulin under the action of nutritional stimulation. Like insulin, amylin deficiency was found in patients with type 1 diabetes, while changes in plasma starch levels in patients with impaired glucose tolerance and type 2 diabetes were similar to those in insulin. It has been well confirmed that insulin regulates blood glucose control by promoting glucose release. Some research have showed the evidence in animals and diabetic patients that amylin regulates glucose inflow circulation by delaying the release of nutrients, so as to inhibiting the appearance of postprandial glucose and inhibiting the secretion of glucagon after meal. Therefore, we believe that the role of amylin is a supplement to insulin. Despite insulin replacement therapy, the problem of blood glucose control in diabetic patients may be due to amylin deficiency.
References
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