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

Autor 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
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade Federal do Rio de Janeiro (UFRJ)
Univ Cape Town
Resumo 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.
Palavra-chave ACE inhibitors
angiogenesis
bradykinin potentiating peptides
endostatin
Idioma Inglês
Data de publicação 2006-05-01
Publicado em Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 387, n. 5, p. 611-616, 2006.
ISSN 1431-6730 (Sherpa/Romeo, fator de impacto)
Publicador Walter de Gruyter & Co
Extensão 611-616
Fonte http://dx.doi.org/10.1515/BC.2006.078
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000238135100015
Endereço permanente http://repositorio.unifesp.br/handle/11600/28907

Exibir registro completo




Arquivo

Arquivo Tamanho Formato Visualização

Não existem arquivos associados a este item.

Este item está nas seguintes coleções

Buscar


Navegar

Minha conta