Inhibitory selectivity of canecystatin: a recombinant cysteine peptidase inhibitor from sugarcane

Inhibitory selectivity of canecystatin: a recombinant cysteine peptidase inhibitor from sugarcane

Autor Oliva, MLV Google Scholar
Carmona, A. K. Google Scholar
Andrade, S. S. Google Scholar
Cotrin, S. S. Google Scholar
Soares-Costa, A. Google Scholar
Henrique-Silva, F. Google Scholar
Instituição Universidade Federal de São Paulo (UNIFESP)
Universidade Federal de São Carlos (UFSCar)
Resumo The cDNA of a cystein peptidase inhibitor was isolated from sugarcane and expressed in Escherichia coli. the protein, named canecystatin, has previously been shown to exert antifungal activity on the filamentous fungus Trichoderma reesei. Herein, the inhibitory specificity of canecystatin was further characterized. It inhibits the cysteine peptidases from plant source papain (K-i = 3.3 nM) and baupain (K-i = 2.1 x 10(-8) M), but no inhibitory effect was observed on ficin or bromelain. Canecystatin also inhibits lysosomal cysteine peptidases such as human cathepsin B (K-i = 125 nM), cathepsin K (K-i = 0.76 nM), cathepsin L (K-i = 0.6 nM), and cathepsin V (K-i = 1.0 nM), but not the aspartyl peptidase cathepsin D. the activity of serine peptidases such as trypsin, chymotrypsin, pancreatic, and neutrophil elastases, and human plasma kallikrein is not affected by the inhibitor, nor is the activity of the metallopeptidases angiotensin converting enzyme and neutral endopeptidase. This is the first report of inhibitory activity of a sugarcane cystatin on cysteine peptidases. (C) 2004 Elsevier Inc. All rights reserved.
Palavra-chave cysteine peptidase
cystatin
plant inhibitor
sugarcane
Idioma Inglês
Data de publicação 2004-08-06
Publicado em Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 320, n. 4, p. 1082-1086, 2004.
ISSN 0006-291X (Sherpa/Romeo, fator de impacto)
Publicador Elsevier B.V.
Extensão 1082-1086
Fonte http://dx.doi.org/10.1016/j.bbrc.2004.06.053
Direito de acesso Acesso restrito
Tipo Artigo
Web of Science WOS:000222923400006
Endereço permanente http://repositorio.unifesp.br/handle/11600/27882

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