In vitro binding and degradation of avian pancreatic polypeptide by chicken and rat tissues.
In vitro binding and degradation of avian pancreatic polypeptide by chicken and rat tissues.
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鸡和大鼠组织对禽胰多肽的体外结合和降解。
DOI：
10.1210/endo-113-2-508
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发表时间：
1983
期刊：
影响因子：
4.8
通讯作者：
R. Hazelwood
中科院分区：
文献类型：
--
作者：
M. Adamo;D. Dyckes;R. Hazelwood
通过研究胰多肽（PP）与鸡和大鼠质膜的结合和降解，研究了PP与鸡和大鼠靶组织的相互作用。鸡脑和肝脏的膜具有高度特异性的禽PP（APP）结合位点，而那些从鸡全胰腺和腺胃和十二指肠粘膜表现出很少或没有具体的[125 I]碘-APP结合。鸡肝特异性结合位点与APP的亲和力较低; 500 ng未标记APP/ml（1.2 × 10（-7）M），而鸡脑膜则有两个APP结合位点，高亲和力位点（Kd = 3.3 × 10（-10）M）和低亲和力位点（Kd = 1.8 × 10（-7）M）。与鸡脑细胞膜的结合过程保留了完整APP 1 -36的特异性，因为未标记的牛PP 1 -36（BPP 1 -36）在浓度为7 × 10（-9）M（未标记APP的IC 50水平的10倍）时抑制了50%的[125 I]碘-APP的特异性结合。APP和BPP的羧基末端五肽（APP 32 -36和BPP 32 -36）与鸡脑细胞膜APP结合位点相互作用，但不具有完整分子的完全结合活性。大鼠脑膜几乎没有APP特异性结合，没有BPP特异性结合。鸡肾膜降解更多的[125 I]碘-APP比任何其他鸡组织。降解过程被特异性抑制未标记的APP，并产生反应产物的分子量低于完整的APP。抗蛋白酶杆菌肽能够几乎完全降解抑制，但它的存在未能增加APP结合肾膜。它的结论是，鸡脑具有高亲和力APP结合位点，潜在的功能在生理浓度的多肽。肝膜上的APP结合位点可能在生理上无功能，而肾脏在APP的降解和清除方面相对于其他组织最活跃。
The interaction of pancreatic polypeptide (PP) with possible chicken and rat target tissues was investigated by characterizing the binding and degradation of [125I]iodo-PP by plasma membrane preparations in vitro. Membranes from chick brain and liver possessed highly specific avian PP (APP)-binding sites, while those from chick whole pancreas and proventricular and duodenal mucosa exhibited little or no specific [125I]iodo-APP binding. The affinity of the specific chick liver binding sites for APP was low; 500 ng unlabeled APP/ml (1.2 X 10(-7) M) were required for half-maximal displacement of [125I]iodo-APP. Chick brain membranes, on the other hand, possessed two orders of APP binding sites, a high affinity site (Kd = 3.3 X 10(-10) M) and a low affinity site (Kd = 1.8 X 10(-7) M). The binding process to chick brain membranes retained specificity for intact APP1-36, as unlabeled bovine PP1-36 (BPP1-36) inhibited specific binding of [125I]iodo-APP by 50% at a concentration of 7 X 10(-9) M (10 times the IC50 level of unlabeled APP). Carboxy-terminal pentapeptides of APP and BPP (APP32-36 and BPP32-36) interacted with the chick brain membrane APP-binding sites, but did not possess the full binding activity of the intact molecule. Membranes from rat brain exhibited little APP-specific binding and no BPP-specific binding. Chick kidney membranes degraded more [125I]iodo-APP than any other chicken tissue. The degradation process was specifically inhibited by unlabeled APP and yielded reaction products of lower molecular weight than intact APP. The antiprotease bacitracin was capable of virtually complete degradation inhibition, but its presence failed to increase APP binding by kidney membranes. It is concluded that chick brain possesses high affinity APP-binding sites, potentially functional at physiological concentrations of the polypeptide. APP-binding sites on liver membranes are probably physiologically nonfunctional, while the kidney is most active relative to other tissues in the degradation and, probably, clearance of APP.
人胰多肽在慢性肾衰竭和肝硬化中：肾脏和肝脏在胰多肽代谢中的作用。
DOI：
10.1210/jcem-51-3-573
发表时间：
1980
期刊：
The Journal of clinical endocrinology and metabolism
影响因子：
--
作者：
Boden,G;Master,RW;Owen,OE;Rudnick,MR
通讯作者：
Rudnick,MR
影响因子：
4.8
作者：
Kimmel,JR;Pollock,HG
通讯作者：
Pollock,HG
狗和大鼠肝细胞中胰腺激素的表面受体：激素-靶细胞相互作用的定性和定量差异。
DOI：
10.1073/pnas.79.7.2167
发表时间：
1982
影响因子：
11.1
作者：
Bonnevie-Nielsen,V;Polonsky,KS;Jaspan,JJ;Rubenstein,AH;Schwartz,TW;Tager,HS
通讯作者：
Tager,HS