Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L

Comparative substrate specificity analysis of recombinant human cathepsin V and cathepsin L

Autor Puzer, L. Google Scholar
Cotrin, S. S. Google Scholar
Alves, MFM Google Scholar
Egborge, T. Google Scholar
Araujo, M. S. Google Scholar
Juliano, M. A. Google Scholar
Juliano, L. Google Scholar
Bromme, D. Google Scholar
Carmona, A. K. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Mt Sinai Sch Med
Resumo Cathepsins V and L have high identity and few structural differences. in this paper, we reported a comparative study of the hydrolytic activities of recombinant human cathepsins V and L using fluorescence resonance energy transfer peptides derived from Abz-KLRSSKQ-EDDnp (Abz = ortho-aminobenzoic acid and EDDnp = N-(2,4-dinitrophenyl)ethylenediamine). Five series of peptides were synthesized to map the S-3 to S'(2) subsites. the cathepsin V subsites S-1 and S-3 present a broad specificity while cathepsin L has preference for positively charged residues. the S-2 subsites of both enzymes require hydrophobic residues with preference for Phe and Leu. the S-1' and S-2' subsites of cathepsins V and L are less specific. Based on these data we designed substrates to explore the electrostatic potential differences of them. Finally, the kininogenase activities of these cathepsins were compared using synthetic human kininogen fragments. Cathepsin V preferentially released Lys-bradykinin while cathepsin L released bradykinin. This kininogenase activity by cathepsins V and L was also observed from human high and low molecular weight kininogens. (C) 2004 Elsevier Inc. All rights reserved.
Palavra-chave lysosomal proteases
cysteine proteases
cathepsin L
cathepsin V
Fluorogenic substrates
bradykinin
kininogen
Idioma Inglês
Data de publicação 2004-10-15
Publicado em Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 430, n. 2, p. 274-283, 2004.
ISSN 0003-9861 (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 274-283
Fonte http://dx.doi.org/10.1016/j.abb.2004.07.006
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000224104500019
Endereço permanente http://repositorio.unifesp.br/handle/11600/27980

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