Cysteine proteinase activity regulation - A possible role of heparin and heparin-like glycosaminoglycans

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dc.contributor.authorAlmeida, P. C.
dc.contributor.authorNantes, I. L.
dc.contributor.authorRizzi, CCA
dc.contributor.authorJudice, Wagner Alves de Souza [UNIFESP]
dc.contributor.authorChagas, Jair Ribeiro [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorNader, Helena Bonciani [UNIFESP]
dc.contributor.authorTersariol, Ivarne Luis dos Santos [UNIFESP]
dc.contributor.institutionUniv Mogi Cruzes
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T12:30:54Z
dc.date.available2016-01-24T12:30:54Z
dc.date.issued1999-10-22
dc.description.abstractPapain is considered to be the archetype of cysteine proteinases. the interaction of heparin and other glycosaminoglycans with papain may be representative of many mammalian cysteine proteinase-glycosaminoglycan interactions that can regulate the function of this class of proteinases in vivo. the conformational changes in papain structure due to glycosaminoglycan interaction were studied by circular dichroism spectroscopy, and the changes in enzyme behavior were studied by kinetic analysis, monitored with fluorogenic substrate. the presence of heparin significantly increases the a-helix content of papain. Heparin binding to papain was demonstrated by affinity chromatography and shown to be mediated by electrostatic interactions. the incubation of papain with heparin promoted a powerful increase in the affinity of the enzyme for the substrate. in order to probe the glycosaminoglycan structure requirements for the papain interaction, the effects of two other glycosaminoglycans were tested. Like heparin, heparan sulfate, to a lesser degree, was able to decrease the papain substrate affinity, and it simultaneously induced a-helix structure in papain. On the other hand, dermatan sulfate was not able to decrease the substrate affinity and did not induce a-helix structure in papain. Heparin stabilizes the papain structure and thereby its activity at alkaline pH.en
dc.description.affiliationUniv Mogi Cruzes, Ctr Interdisciplinar Invest Bioquim, Ctr Ciencias Biomed, BR-08780911 Mogi Das Cruzes, SP, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Inst Nacl Farmacol, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Inst Nacl Farmacol, Disciplina Biol Mol, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Inst Nacl Farmacol, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Inst Nacl Farmacol, Disciplina Biol Mol, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.format.extent30433-30438
dc.identifierhttp://dx.doi.org/10.1074/jbc.274.43.30433
dc.identifier.citationJournal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 274, n. 43, p. 30433-30438, 1999.
dc.identifier.doi10.1074/jbc.274.43.30433
dc.identifier.issn0021-9258
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/26162
dc.identifier.wosWOS:000083276700017
dc.language.isoeng
dc.publisherAmer Soc Biochemistry Molecular Biology Inc
dc.relation.ispartofJournal of Biological Chemistry
dc.rightsinfo:eu-repo/semantics/openAccess
dc.titleCysteine proteinase activity regulation - A possible role of heparin and heparin-like glycosaminoglycansen
dc.typeinfo:eu-repo/semantics/article
unifesp.campusEscola Paulista de Medicina
unifesp.departamentoFarmacologia
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