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

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

Autor Almeida, P. C. Google Scholar
Nantes, I. L. Google Scholar
Rizzi, CCA Google Scholar
Judice, Wagner Alves de Souza Autor UNIFESP Google Scholar
Chagas, Jair Ribeiro Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Nader, Helena Bonciani Autor UNIFESP Google Scholar
Tersariol, Ivarne Luis dos Santos Autor UNIFESP Google Scholar
Instituição Univ Mogi Cruzes
Universidade Federal de São Paulo (UNIFESP)
Resumo Papain 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.
Idioma Inglês
Data 1999-10-22
Publicado em Journal of Biological Chemistry. Bethesda: Amer Soc Biochemistry Molecular Biology Inc, v. 274, n. 43, p. 30433-30438, 1999.
ISSN 0021-9258 (Sherpa/Romeo, fator de impacto)
Editor Amer Soc Biochemistry Molecular Biology Inc
Extensão 30433-30438
Direito de acesso Acesso aberto Open Access
Tipo Artigo
Web of Science WOS:000083276700017

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