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Carboxypeptidases A1 and A2 from the perfusate of rat mesenteric arterial bed differentially process angiotensin peptides

机译:大鼠肠系膜动脉床灌流液中的羧肽酶A1和A2差异地处理血管紧张素肽

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摘要

Here we report the isolation of carboxypeptidases A1 and A2 (CPA1 and CPA2) from the rat mesenteric arterial bed perfusate, which were found to be identical with their pancreatic counterparts. Angiotensin (Ang) I, Ang II, Ang-(1-9) and Ang-(1-12) were differentially processed by these enzymes, worthy mentioning the peculiar CPA1-catalyzed conversion of Ang II to Ang-(1-7) and the CPA2-mediated formation of Ang I from Ang-(1-12). We detected gene transcripts for CPA1 and CPA2 in mesentery and other extrapancreatic tissues, indicating that these CPAs might play a role in the renin-angiotensin system in addition to their functions as digestive enzymes. (C) 2011 Elsevier Inc. All rights reserved.
机译:在这里,我们报告从大鼠肠系膜动脉床灌流液中分离出羧肽酶A1和A2(CPA1和CPA2),发现它们与胰腺对应物相同。这些酶对血管紧张素(Ang)I,Ang II,Ang-(1-9)和Ang-(1-12)进行了差异处理,值得一提的是CPA1催化的Ang II向Ang-(1-7)的独特转化。和CPA2介导的Ang I从Ang-(1-12)的形成。我们在肠系膜和其他胰腺外组织中检测到了CPA1和CPA2的基因转录物,表明这些CPA除了作为消化酶起作用外,还可能在肾素-血管紧张素系统中起作用。 (C)2011 Elsevier Inc.保留所有权利。

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