Proteinase activity regulation by glycosaminoglycans

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dc.contributor.authorTersariol, Ivarne Luis dos Santos [UNIFESP]
dc.contributor.authorPimenta, D.c. [UNIFESP]
dc.contributor.authorChagas, Jair Ribeiro [UNIFESP]
dc.contributor.authorAlmeida, P.c.
dc.contributor.institutionUniversidade de Mogi das Cruzes Centro Interdisciplinar de Investigação Bioquímica
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2015-06-14T13:29:36Z
dc.date.available2015-06-14T13:29:36Z
dc.date.issued2002-02-01
dc.description.abstractThere are few reports concerning the biological role and the mechanisms of interaction between proteinases and carbohydrates other than those involved in clotting. It has been shown that the interplay of enzymes and glycosaminoglycans is able to modulate the activity of different proteases and also to affect their structures. From the large number of proteases belonging to the well-known protease families and also the variety of carbohydrates described as widely distributed, only few events have been analyzed more deeply. The term family is used to describe a group of proteases in which every member shows an evolutionary relationship to at least one other protease. This relationship may be evident throughout the entire sequence, or at least in that part of the sequence responsible for catalytic activity. The majority of proteases belong to the serine, cysteine, aspartic or metalloprotease families. By considering the existing limited proteolysis process, in addition to the initial idea that the proteinases participate only in digestive processes, it is possible to conclude that the function of the enzymes is strictly limited to the cleavage of intended substrates since the destruction of functional proteins would result in normal tissue damage. In addition, the location as well as the eventual regulation of protease activity promoted by glycosaminoglycans can play an essential role in the development of several physiopathological conditions.en
dc.description.affiliationUniversidade de Mogi das Cruzes Centro Interdisciplinar de Investigação Bioquímica
dc.description.affiliationUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de Biofísica
dc.description.affiliationUnifespUNIFESP, EPM, Depto. de Biofísica
dc.description.sourceSciELO
dc.format.extent135-144
dc.identifierhttp://dx.doi.org/10.1590/S0100-879X2002000200001
dc.identifier.citationBrazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 35, n. 2, p. 135-144, 2002.
dc.identifier.doi10.1590/S0100-879X2002000200001
dc.identifier.fileS0100-879X2002000200001.pdf
dc.identifier.issn0100-879X
dc.identifier.scieloS0100-879X2002000200001
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/1355
dc.identifier.wosWOS:000174281400001
dc.language.isoeng
dc.publisherAssociação Brasileira de Divulgação Científica
dc.relation.ispartofBrazilian Journal of Medical and Biological Research
dc.rightsinfo:eu-repo/semantics/openAccess
dc.subjectProteinasesen
dc.subjectHeparin bindingen
dc.subjectGlycosaminoglycanen
dc.subjectMacromoleculesen
dc.titleProteinase activity regulation by glycosaminoglycansen
dc.typeinfo:eu-repo/semantics/article
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