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


Autoria(s): Pereira, Hugo J. V.; Souza, Laura L.; Costa Neto, Claudio Miguel da; Salgado, Maria Cristina O.; Oliveira, Eduardo B.
Contribuinte(s)

UNIVERSIDADE DE SÃO PAULO

Data(s)

31/10/2013

31/10/2013

02/08/2013

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

http://dx.doi.org/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