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

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dc.contributor.authorOliva, MLV
dc.contributor.authorCarmona, A. K.
dc.contributor.authorAndrade, S. S.
dc.contributor.authorCotrin, S. S.
dc.contributor.authorSoares-Costa, A.
dc.contributor.authorHenrique-Silva, F.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionUniversidade Federal de São Carlos (UFSCar)
dc.date.accessioned2016-01-24T12:37:19Z
dc.date.available2016-01-24T12:37:19Z
dc.date.issued2004-08-06
dc.description.abstractThe 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.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biochem, BR-04044020 São Paulo, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, SP, Brazil
dc.description.affiliationUniv Fed Sao Carlos, Lab Biol Mol, DGE, Sao Carlos, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biochem, BR-04044020 São Paulo, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biophys, BR-04044020 São Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.format.extent1082-1086
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2004.06.053
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 320, n. 4, p. 1082-1086, 2004.
dc.identifier.doi10.1016/j.bbrc.2004.06.053
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27882
dc.identifier.wosWOS:000222923400006
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectcysteine peptidaseen
dc.subjectcystatinen
dc.subjectplant inhibitoren
dc.subjectsugarcaneen
dc.titleInhibitory selectivity of canecystatin: a recombinant cysteine peptidase inhibitor from sugarcaneen
dc.typeinfo:eu-repo/semantics/article
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