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

Abstract:

: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 (Ki =3.3nM) and baupain (Ki=2.1x10(-8)M), but no inhibitory effect was observed on ficin or bromelain. Canecystatin also inhibits lysosomal cysteine peptidases such as human cathepsin B (Ki=125nM), cathepsin K (Ki=0.76nM), cathepsin L (Ki=0.6nM), and cathepsin V (Ki=1.0nM), 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.

authors

Oliva ML,Carmona AK,Andrade SS,Cotrin SS,Soares-Costa A,Henrique-Silva F

doi

10.1016/j.bbrc.2004.06.053

subject

Has Abstract

pub_date

2004-08-06 00:00:00

pages

1082-6

issue

4

eissn

0006-291X

issn

1090-2104

pii

S0006291X04013361

journal_volume

320

pub_type

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