Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme

Substrate phosphorylation affects degradation and interaction to endopeptidase 24.15, neurolysin, and angiotensin-converting enzyme

Autor Machado, MFM Google Scholar
Cunha, F. M. Google Scholar
Berti, D. A. Google Scholar
Heimann, A. S. Google Scholar
Klitzke, C. F. Google Scholar
Rioli, V Google Scholar
Oliveira, V Google Scholar
Ferro, E. S. Google Scholar
Instituição Univ Cidade São Paulo
Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Ptoteimax Biotecnol LTDA
CEPID
Resumo Recent findings from our laboratory suggest that intracellular peptides containing putative post-translational modification sites (i.e., phosphorylation) could regulate specific protein interactions. Here, we extend our previous observations showing that peptide phosphorylation changes the kinetic parameters of structurally related endopeptidase EP24.15 (EC 3.4.24.15), neurolysin (EC 3.4.24.16), and angiotensin-converting enzyme (EC 3.4.15.1). Phosphorylation of peptides that are degraded by these enzymes leads to reduced degradation, whereas phosphorylation of peptides that interacted as competitive inhibitors of these enzymes alters only the K-i's. These data suggest that substrate phosphorylation could be one of the mechanisms whereby some intracellular peptides would escape degradation and could be regulating protein interactions within cells. (c) 2005 Elsevier Inc. All rights reserved.
Palavra-chave neurolysin
thimet oligopeptidase
intracellular peptide metabolism
phosphorylation
proteasome
peptidase
Idioma Inglês
Data de publicação 2006-01-13
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 339, n. 2, p. 520-525, 2006.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 520-525
Fonte http://dx.doi.org/10.1016/j.bbrc.2005.11.041
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000234329800010
Endereço permanente http://repositorio.unifesp.br/handle/11600/28693

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