Tatemoto K, Efendić S, Mutt V, Makk G, Feistner G J, Barchas J D
Nature. 1986;324(6096):476-8. doi: 10.1038/324476a0.
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.
在哺乳动物组织中,已发现C末端酰胺结构仅存在于神经活性或激素活性肽中。大约一半已知的神经肽和肽类激素具有这种独特的化学特征。利用化学检测方法,对脑和肠提取物中具有C末端酰胺结构的先前未知肽进行了搜索,并分离出了一些新型神经肽和激素肽,分别命名为神经肽Y、PHI、肽YY、甘丙肽和神经肽K。我们最近在猪胰腺中进行了类似的搜索,发现了一种在其C末端具有甘氨酸酰胺的肽的高浓度存在。在此,我们报告这种新型肽的分离、一级结构和生物活性。这种由49个氨基酸残基组成的肽强烈抑制从离体灌注胰腺中葡萄糖诱导的胰岛素释放,因此被命名为胰抑制素。它可能在胰岛素分泌的调节以及糖尿病的发病机制和治疗中具有重要意义。