Effect of pancreatic polypeptide and its C‐terminal hexapeptide on meal and secretin induced pancreatic secretion in dogs.
Effect of pancreatic polypeptide and its C‐terminal hexapeptide on meal and secretin induced pancreatic secretion in dogs.
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胰多肽及其C端六肽对膳食和促胰液素诱导的犬胰腺分泌的影响。
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发表时间：
1981
期刊：
影响因子：
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通讯作者：
J. Tasler
中科院分区：
文献类型：
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作者：
R. Chance;M. Cieszkowski;J. Jaworek;S. Konturek;J. Świerczek;J. Tasler
1.在输注牛胰多肽或其C-末端六肽之前和之后，测量了胃酸和胰腺碳酸氢盐和蛋白质分泌以及对进餐和胰泌素的免疫反应性血清胃泌素和胰多肽浓度。2.肝脏提取物膳食保持在胃中的pH 5.5（通过胃内滴定）产生了显着增加胃酸和胰腺蛋白分泌伴随着血清胃泌素和胰腺多肽水平的上升。外源性牛胰多肽对胃分泌和血清胃泌素的影响不大，但对胰腺分泌有明显的抑制作用。3.普通喂食肝粉可导致胰腺碳酸氢盐和蛋白质分泌显著增加，牛胰多肽或其C末端六肽可剂量依赖性地抑制胰腺碳酸氢盐和蛋白质分泌，抑制程度与血浆胰多肽的增量密切相关。4.牛胰多肽及其C末端六肽也以剂量依赖性方式抑制促胰液素和雨蛙素诱导的胰腺分泌。5.本研究表明，牛胰多肽至少部分通过直接作用于胰腺外分泌来抑制胰腺分泌，其生物活性存在于其C末端六肽片段中。
1. Gastric acid and pancreatic bicarbonate and protein secretion as well as immunoreactive serum gastrin and pancreatic polypeptide concentrations in response to a meal and secretin have been measured before and after infusion of bovine pancreatic polypeptide or its C‐terminal hexapeptide. 2. Liver extract meal kept in the stomach at pH 5.5 (by intragastric titration) produced a marked increase in gastric acid and pancreatic protein secretion accompanied by a rise in serum gastrin and pancreatic polypeptide levels. Exogenous bovine pancreatic polypeptide caused little change in gastric secretion and serum gastrin but resulted in a profound suppression of pancreatic secretion. 3. Ordinary feeding a liver meal produced a marked increase in pancreatic bicarbonate and protein secretion that was dose‐dependently inhibited by bovine pancreatic polypeptide or its C‐terminal hexapeptide, the degree of inhibition being closely correlated with the increments in plasma pancreatic polypeptide. 4. Bovine pancreatic polypeptide and its C‐terminal hexapeptide also inhibited secretin and caerulein‐induced pancreatic secretion in a dose‐dependent manner. 5. This study shows that bovine pancreatic polypeptide inhibits pancreatic secretion at least in part by acting directly on the exocrine pancreas and that its biological activity resides in its C‐terminal hexapeptide fragment.