Tissue expression and secretion of amylin.
Amylin and insulin are co-localized within the same secretory granules of pancreatic beta-cells. Acutely, the secreted ratio of amylin:insulin is comparatively invariant, but long-standing hyperglycemia may favor induction of amylin synthesis and secretion over that of insulin. Amylin is also found in much lesser quantities in the gut and other tissues. In humans, both type 1 diabetes mellitus and the later stages of type 2 diabetes mellitus are characterized by deficiency of both insulin and amylin secretion. The severity of amylin deficiency appears to correlate with the severity of insulin deficiency. This concordance of deficiencies in amylin and insulin secretion observed with the progression of diabetes mellitus is consistent with their co-localization in pancreatic beta-cells. Amylin is cleared mainly by proteolytic degradation at the kidney. The terminal t1/2 for rat amylin in rats is approximately 13 min, and that for pramlintide in humans is approximately 20-45 min.
Young
Andrew
A
Amylin Pharmaceuticals, Inc., San Diego, California, USA.
D000682:Amyloid / Q000096:biosynthesis* / Q000378:metabolism* / Q000494:pharmacology; D000818:Animals; D006801:Humans; D007004:Hypoglycemic Agents / Q000494:pharmacology; D050417:Insulin-Secreting Cells / Q000378:metabolism*; D058228:Islet Amyloid Polypeptide
D000682:Amyloid; D007004:Hypoglycemic Agents; D058228:Islet Amyloid Polypeptide