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Am J Physiol Heart Circ Physiol (April 24, 2003). doi:10.1152/ajpheart.00818.2002
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Submitted on September 19, 2002
Accepted on April 15, 2003

Functional role, cellular source and tissue distribution of rat elastase-2, an angiotensin II-forming enzyme

Carlos F. Santos1, Marcos Antonio V. Caprio1, Eduardo B. Oliveira1, Maria Christina O. Salgado1, Daniela N. Schippers2, Diane H. Munzenmaier2, and Andrew S. Greene2*

1 Department of Pharmacology, University of Sao Paulo, School of Medicine of Ribeirao Preto, Ribeirao Preto, Sao Paulo, Brazil; Department of Biotechnology and Bioengineering Center, Medical College of Wisconsin, Milwaukee, WI, USA
2 Department of Physiology, Medical College of Wisconsin, Milwaukee, WI, USA; Department of Biotechnology and Bioengineering Center, Medical College of Wisconsin, Milwaukee, WI, USA

* To whom correspondence should be addressed. E-mail: agreene{at}mcw.edu.

We have recently described a chymostatin-sensitive elastase-2 as the major angiotensin (Ang) II-forming enzyme in the perfusate of rat mesenteric arterial bed (MAB) with the same cDNA sequence as rat pancreatic elastase-2. The role of this enzyme in generating Ang II was examined in the rat isolated and perfused MAB. The vasoconstrictor effect elicited by Ang I and the renin substrate tetradecapeptide was only partially inhibited by captopril but abolished by the combination of captopril and chymostatin or N-acetyl-Ala-Ala-Pro-Leu-chloromethylketone (Ac-AAPL-CK, inhibitor originally developed for human elastase-2). The effect induced by [Pro11-D-Ala12]-Ang I, an Ang 1 converting enzyme (ACE)-resistant biologically inactive precursor of Ang II, was blocked by chymostatin or Ac-AAPL-CK. It was also demonstrated that cultured rat mesenteric endothelial cells synthesize elastase-2 and that the mRNA for this enzyme can be detected in different rat tissues such as pancreas, MAB, lung, heart, kidney, liver and spleen. In conclusion, the demonstration of a functional alternative pathway to ACE for Ang II generation in rat MAB and that cultured MAB endothelial cells are capable of producing and secreting elastase-2 represents strong evidence of a physiological role for this enzyme in rat vasculature.




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