Faculty Collaboration Database

Molecular cloning and sequencing of the cDNA for rat mesenteric arterial bed elastase-2, an angiotensin II-forming enzyme. J Cardiovasc Pharmacol 2002 May;39(5):628-35

Date

04/26/2002

Pubmed ID

11973405

DOI

10.1097/00005344-200205000-00002

Scopus ID

2-s2.0-0036233594 (requires institutional sign-in at Scopus site)   21 Citations

Abstract

A 28.5-kD protein expressed in rat mesenteric arterial bed (MAB) perfusate with angiotensin II-forming ability was previously characterized. This protein, a member of the elastase-2 family of enzymes, seems to be the only representative of this family of proteases to be secreted outside the digestive tract and implicated in the generation of angiotensin II. The cloning and sequencing of the cDNA for the rat MAB elastase-2 by using reverse transcription polymerase chain reaction are reported. The sequence of this cDNA was found to be identical to the sequence of the rat pancreatic elastase-2; the cDNA is 909 nucleotides in length plus a poly (A) tail and encodes a preproenzyme of 271 amino acids. Analysis of the putative amino acids in the extended angiotensin I binding site of the rat MAB elastase-2 reveals features that could explain the dipeptidyl carboxypeptidase-like activity required for efficient conversion of angiotensin I to angiotensin II. Additionally, the sequence reveals structural features that could contribute to the lack of activity of this enzyme toward angiotensin II. Rat MAB elastase-2 was expressed in mesenteric arteries and lung but not in aorta. These results may also indicate that rat MAB elastase-2 is expressed in resistance vessels but not in conduit vessels.

Author List

Santos CF, Oliveira EB, Salgado MC, Greene AS

MESH terms used to index this publication - Major topics in bold

Amino Acid Sequence
Angiotensin II
Animals
Base Sequence
Cloning, Molecular
DNA, Complementary
Male
Mesenteric Arteries
Molecular Sequence Data
Rats
Rats, Sprague-Dawley
Sequence Analysis, DNA
Serine Endopeptidases