Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Angiotensin I-converting enzyme inhibitor peptides derived from the endostatin-containing NC1 fragment of human collagen XVIII

Author Farias, S. L. Google Scholar
Sabatini, R. A. Google Scholar
Sampaio, T. C. Google Scholar
Hirata, I. Y. Google Scholar
Cezari, MHS Google Scholar
Juliano, M. A. Google Scholar
Sturrock, E. D. Google Scholar
Carmona, A. K. Google Scholar
Juliano, L. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Universidade Federal do Rio de Janeiro (UFRJ)
Univ Cape Town
Abstract Extracellular matrix and soluble plasma proteins generate peptides that regulate biological activities such as cell growth, differentiation and migration. Bradykinin, a peptide released from kininogen by kallikreins, stimulates vasodilatation and endothelial tell proliferation. Various classes of substances can potentiate these biological actions of bradykinin. Among them, the best studied are bradykinin potentiating peptides (BPPs) derived from snake venom, which can also strongly inhibit angiotensin I-converting enzyme (ACE) activity. We identified and synthesized sequences resembling BPPs in the vicinity of potential proteolytic cleavage sites in the collagen XVIII molecule, close to endostatin. These peptides were screened as inhibitors of human recombinant wild-type ACE containing two intact functional domains; two full-length ACE mutants containing only a functional C- or N-domain catalytic site; and human testicular ACE, a natural form of the enzyme that only contains the C-domain. the BPP-like peptides inhibited ACE in the micromolar range and interacted preferentially with the C-domain. the proteolytic activity involved in the release of BPP-like peptides was studied in human serum and human umbilical-vein endothelial cells. the presence of enzymes able to release these peptides in blood led us to speculate on a physiological mechanism for the control of ACE activities.
Keywords ACE inhibitors
angiogenesis
bradykinin potentiating peptides
endostatin
Language English
Date 2006-05-01
Published in Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 387, n. 5, p. 611-616, 2006.
ISSN 1431-6730 (Sherpa/Romeo, impact factor)
Publisher Walter de Gruyter & Co
Extent 611-616
Origin http://dx.doi.org/10.1515/BC.2006.078
Access rights Closed access
Type Article
Web of Science ID WOS:000238135100015
URI http://repositorio.unifesp.br/handle/11600/28907

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