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

Hugo J V Pereira, Laura L Souza, Claudio M Costa-Neto, Maria Cristina O Salgado, Eduardo B Oliveira

University of São Paulo, Faculty of Medicine of Ribeirão Preto, Department of Biochemistry and Immunology Ribeirão Preto, SP 14049-900, Brazil.

Peptides 2012 Jan

filter terms:

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. Copyright © 2011 Elsevier Inc. All rights reserved.

Citation

Hugo J V Pereira, Laura L Souza, Claudio M Costa-Neto, Maria Cristina O Salgado, Eduardo B Oliveira. Carboxypeptidases A1 and A2 from the perfusate of rat mesenteric arterial bed differentially process angiotensin peptides. Peptides. 2012 Jan;33(1):67-76