No abstract

The isolation of a novel biologically active peptide, designated galanin, is described. The peptide was discovered by the detection of its C‐terminal amide structure in porcine intestinal extract using a chemical method. It was found that galanin consists of 29 amino acids and the complete amino acid sequence is: contract smooth muscle preparations from the rat and to cause a mild and sustained hyperglycemia in dog.

A polypeptide, which has potent and diverse biological action-including systemic vasodilation, hypotension, increased cardiac output, respiratory stimulation, and hyperglycemia-was isolated from the small intestine of the hog. The peptide has 28 amino acid residues and is chemically distinct from the kinins, "substance P," glucagon, and secretin.

In mammalian tissues the C-terminal amide structure has been found to occur only in neuroactive or hormonally-active peptides. About half known neuropeptide and peptide hormones have this unique chemical feature. Using a chemical detection method, a search for previously unknown peptides that possess the C-terminal amide structure in extracts of brain and intestine was carried out and a number of novel neuropeptides and hormonal peptides, designated neuropeptide Y, PHI, peptide YY, galanin and neuropeptide K were isolated. We recently performed a similar search in porcine pancreas and found a high concentration of a peptide having a glycine amide at its C-terminus. Here we report the isolation, primary structure and biological activity of this novel peptide. The 49-residue peptide strongly inhibits glucose-induced insulin release from the isolated perfused pancreas and was therefore named pancreastatin. It may be important in the regulation of insulin secretion and in the pathogenesis and treatment of diabetes mellitus.

No abstract