Amidolytic activity of prostatic acid phosphatase on human semenogelins and semenogelin-derived synthetic substrates

Amidolytic activity of prostatic acid phosphatase on human semenogelins and semenogelin-derived synthetic substrates

Autor Brillard-Bourdet, M. Google Scholar
Rehault, S. Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Ferrer, M. Google Scholar
Moreau, T. Google Scholar
Gauthier, F. Google Scholar
Instituição Univ Tours
Universidade Federal de São Paulo (UNIFESP)
Resumo In addition to kallikrein hK3, a serine protease generafly reported as PSA (prostate-specific antigen). at least two other enzymes in human seminal plasma also cleave synthetic peptidyl substrates derived from the sequence of human semenogelins. We have identified one of these as prostatic acid phosphatase (PAP), a major component of prostatic fluid whose physiological function is unclear. the other is a high M-r basic protein present at low concentrations in seminal plasma and that remains to be characterized. PAP was purified to homogeneity from freshly ejaculated seminal plasma. Its N-terminal sequence and its phosphatase properties (hydrolysis of para-nitrophenylphosphate at low pH) were determined, and its inhibition by sodium fluoride measured. Both purified and commercial PAP also had amidolytic activity on peptide substrates derived from the semenogelin sequence at neutral and slightly basic pH. the k(cat)/K-m values were in the 10(2)-10(3) M-1.s(-1) range using fluorogenic semenogelin-derived substrates whose peptidyl moiety included cleavage sites that had been identified ex PAP cleavage sites differed from those of hK3 and were mainly at P1=Gln residues or between residues bearing hydroxyl groups, PAP amidolytic activity was poorly inhibited by all currently used Aide spectrum proteinase inhibitors. Only 3-4 dichloroisocoumarin and benzamidine inhibited purified PAP, Purified human semenogelin was cleaned by purified and commercial PAP at neutral PH: the two main cleavage sites were at Tyr292 and Ser170 (semenogelin I sequence). only the former has been identified ex vivo by analysis of seminal plasma.
Assunto amidolytic activity
fluorogenic substrates
human kallikrein
Idioma Inglês
Data 2002-01-01
Publicado em European Journal of Biochemistry. Oxford: Blackwell Publishing Ltd, v. 269, n. 1, p. 390-395, 2002.
ISSN 0014-2956 (Sherpa/Romeo, fator de impacto)
Editor Blackwell Publishing Ltd
Extensão 390-395
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000173398100043

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