Amylin, amyloid and age-related disease. 1996

G J Cooper, and C A Tse
Developmental Biology and Cancer Research Group, School of Medicine, University of Auckland, New Zealand.

Amylin, a 37-amino acid peptide, is cosecreted with insulin from the beta-cells of the pancreatic islets in normal response to physiological stimuli. It is the major protein of islet amyloid, which is usually present in the pancreases of people with non-insulin-dependent (type II) diabetes mellitus. Amylin elicits potent effects on carbohydrate metabolism in rodent tissues, causing insulin resistance in skeletal muscle and liver. A close structural relationship exists between amylin and the 2 calcitonin gene-related peptides, which are widely distributed neuropeptides and potent vasodilators. These exert biological effects similar to those of amylin on the organs primarily responsible for the regulation of carbohydrate metabolism. All 3 peptides are thought to cause their biological actions by binding to similar cell surface receptors. This article reviews the field of amylin and its role in the physiological regulation of carbohydrate metabolism, and in disease mechanisms associated with insulin resistance in diabetes mellitus, impaired glucose tolerance and essential hypertension. Potential therapeutic applications are also discussed.

UI MeSH Term Description Entries
D003924 Diabetes Mellitus, Type 2 A subclass of DIABETES MELLITUS that is not INSULIN-responsive or dependent (NIDDM). It is characterized initially by INSULIN RESISTANCE and HYPERINSULINEMIA; and eventually by GLUCOSE INTOLERANCE; HYPERGLYCEMIA; and overt diabetes. Type II diabetes mellitus is no longer considered a disease exclusively found in adults. Patients seldom develop KETOSIS but often exhibit OBESITY. Diabetes Mellitus, Adult-Onset,Diabetes Mellitus, Ketosis-Resistant,Diabetes Mellitus, Maturity-Onset,Diabetes Mellitus, Non-Insulin-Dependent,Diabetes Mellitus, Slow-Onset,Diabetes Mellitus, Stable,MODY,Maturity-Onset Diabetes Mellitus,NIDDM,Diabetes Mellitus, Non Insulin Dependent,Diabetes Mellitus, Noninsulin Dependent,Diabetes Mellitus, Noninsulin-Dependent,Diabetes Mellitus, Type II,Maturity-Onset Diabetes,Noninsulin-Dependent Diabetes Mellitus,Type 2 Diabetes,Type 2 Diabetes Mellitus,Adult-Onset Diabetes Mellitus,Diabetes Mellitus, Adult Onset,Diabetes Mellitus, Ketosis Resistant,Diabetes Mellitus, Maturity Onset,Diabetes Mellitus, Slow Onset,Diabetes, Maturity-Onset,Diabetes, Type 2,Ketosis-Resistant Diabetes Mellitus,Maturity Onset Diabetes,Maturity Onset Diabetes Mellitus,Non-Insulin-Dependent Diabetes Mellitus,Noninsulin Dependent Diabetes Mellitus,Slow-Onset Diabetes Mellitus,Stable Diabetes Mellitus
D005934 Glucagon A 29-amino acid pancreatic peptide derived from proglucagon which is also the precursor of intestinal GLUCAGON-LIKE PEPTIDES. Glucagon is secreted by PANCREATIC ALPHA CELLS and plays an important role in regulation of BLOOD GLUCOSE concentration, ketone metabolism, and several other biochemical and physiological processes. (From Gilman et al., Goodman and Gilman's The Pharmacological Basis of Therapeutics, 9th ed, p1511) Glucagon (1-29),Glukagon,HG-Factor,Hyperglycemic-Glycogenolytic Factor,Proglucagon (33-61),HG Factor,Hyperglycemic Glycogenolytic Factor
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000682 Amyloid A fibrous protein complex that consists of proteins folded into a specific cross beta-pleated sheet structure. This fibrillar structure has been found as an alternative folding pattern for a variety of functional proteins. Deposits of amyloid in the form of AMYLOID PLAQUES are associated with a variety of degenerative diseases. The amyloid structure has also been found in a number of functional proteins that are unrelated to disease. Amyloid Fibril,Amyloid Fibrils,Amyloid Substance,Fibril, Amyloid,Fibrils, Amyloid,Substance, Amyloid
D058228 Islet Amyloid Polypeptide A pancreatic beta-cell hormone that is co-secreted with INSULIN. It displays an anorectic effect on nutrient metabolism by inhibiting gastric acid secretion, gastric emptying and postprandial GLUCAGON secretion. Islet amyloid polypeptide can fold into AMYLOID FIBRILS that have been found as a major constituent of pancreatic AMYLOID DEPOSITS. Amlintide,Amylin,IAPP Precursor,IAPP Protein,Insulinoma Amyloid Polypeptide,Insulinoma Amyloid Polypeptide Precursor,Islet Amyloid Polypeptide Precursor,Pancreatic Amylin,Amylin, Pancreatic,Amyloid Polypeptide, Insulinoma,Amyloid Polypeptide, Islet,Polypeptide, Insulinoma Amyloid,Polypeptide, Islet Amyloid

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