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

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Oliva, MLV
Carmona, A. K.
Andrade, S. S.
Cotrin, S. S.
Soares-Costa, A.
Henrique-Silva, F.
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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.
Biochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 320, n. 4, p. 1082-1086, 2004.