Carboxypeptidases A1 and A2 from the perfusate of rat mesenteric arterial bed differentially process angiotensin peptides
Contribuinte(s) |
UNIVERSIDADE DE SÃO PAULO |
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Data(s) |
31/10/2013
31/10/2013
02/08/2013
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Resumo |
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. Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) Fundacao de Amparo a Pesquisa do Estado de Sao Paulo (FAPESP) |
Identificador |
PEPTIDES, NEW YORK, v. 33, n. 1, supl. 1, Part 3, pp. 67-76, JAN, 2012 0196-9781 http://www.producao.usp.br/handle/BDPI/37053 10.1016/j.peptides.2011.12.001 |
Idioma(s) |
eng |
Publicador |
ELSEVIER SCIENCE INC NEW YORK |
Relação |
PEPTIDES |
Direitos |
closedAccess Copyright ELSEVIER SCIENCE INC |
Palavras-Chave | #CARBOXYPEPTIDASE #ANGIOTENSIN I #ANGIOTENSIN II #ANGIOTENSIN-(1-7) #ANGIOTENSIN-(1-12) #ACE2 #CONVERTING ENZYME #HUMAN HEART #CARDIOVASCULAR FUNCTION #SUBSTRATE-SPECIFICITY #GENE FAMILY #CATHEPSIN-A #CHYMASE #KIDNEY #PROANGIOTENSIN-12 #IDENTIFICATION #BIOCHEMISTRY & MOLECULAR BIOLOGY #PHARMACOLOGY & PHARMACY |
Tipo |
article original article publishedVersion |