Angiotensin converting enzymes from human urine of mild hypertensive untreated patients resemble the N-terminal fragment of human angiotensin I-converting enzyme

Angiotensin converting enzymes from human urine of mild hypertensive untreated patients resemble the N-terminal fragment of human angiotensin I-converting enzyme

Autor Casarini, D. E. Google Scholar
Plavinik, F. L. Google Scholar
Zanella, M. T. Google Scholar
Marson, O. Google Scholar
Krieger, J. E. Google Scholar
Hirata, I. Y. Google Scholar
Stella, RCR Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade de São Paulo (USP)
Resumo Angiotensin I-converting enzyme (ACE) activity was analyzed in human urine collected from mild hypertensive untreated patients. DEAE-cellulose chromatography using linear gradient elution revealed two forms of angiotensin I-converting enzyme, eluted in the conductivity of 0.75 and 1.25 mS. the fractions of each conductivity were pooled and submitted to direct eel filtration in an AcA-34 column, and the apparent molecular weights of urinary ACEs were estimated as 90 kDa (for ACE eluted in 0.75 mS) and 65 kDa (for ACE eluted in 1.25 mS). Both enzymes have a K-i of the order of 10(-7) M for the specific inhibitors studied, and are able to hydrolyze luteinizing hormone-releasing hormone and N-acetyl-Ser-Asp-Lys-Pro as described for N-domain ACE. By Western blot analysis, both peaks were recognized by ACE-specific antibody Y4, confirming the molecular weight already described. A plate precipitation assay using monoclonal antibodies to the N-domain of ACE showed that both forms of ACE binds with all monoclonal antibodies to the active N-domain ACE, suggesting that these forms of human urine ACEs resemble the N-fragment of ACE. the HP2 ACE (65 kDa) is similar to low molecular weight (LMW) ACE from normal subjects, and the HP2 ACE (90 kDa) is different from high molecular weight (190 kDa) and LMW (65 kDa) normal ACEs. the 90 kDa ACE could have an important role in development of hypertension. It will be fundamental to elucidate the molecular mechanism responsible for the genesis of this isoform. (C) 2001 Elsevier B.V. All rights reserved.
Palavra-chave human urine
angiotensin I-converting enzyme
N-domain
Idioma Inglês
Data de publicação 2001-01-01
Publicado em International Journal of Biochemistry & Cell Biology. Oxford: Pergamon-Elsevier B.V., v. 33, n. 1, p. 75-85, 2001.
ISSN 1357-2725 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 75-85
Fonte http://dx.doi.org/10.1016/S1357-2725(00)00072-8
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000167094200008
Endereço permanente http://repositorio.unifesp.br/handle/11600/26448

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