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

Peptides. 2012 Jan;33(1):67-76. doi: 10.1016/j.peptides.2011.12.001. Epub 2011 Dec 9.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Angiotensin I / metabolism*
  • Angiotensin II / metabolism*
  • Angiotensinogen
  • Angiotensins / metabolism
  • Animals
  • Base Sequence
  • Carboxypeptidases A / genetics*
  • Carboxypeptidases A / metabolism*
  • Gene Expression Regulation, Enzymologic
  • In Vitro Techniques
  • Kinetics
  • Mesenteric Arteries / enzymology*
  • Mesenteric Arteries / metabolism
  • Molecular Sequence Data
  • Organ Specificity
  • Peptide Fragments / metabolism
  • Perfusion
  • Rats

Substances

  • Angiotensins
  • Peptide Fragments
  • angiotensin I (1-9)
  • proangiotensin-12, rat
  • Angiotensinogen
  • Angiotensin II
  • Angiotensin I
  • Carboxypeptidases A