Glycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitors

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dc.contributor.authorGozzo, Andrezza Justino [UNIFESP]
dc.contributor.authorNunes, V.a. [UNIFESP]
dc.contributor.authorNader, Helena Bonciani [UNIFESP]
dc.contributor.authorDietrich, Carl Peter [UNIFESP]
dc.contributor.authorCarmona, Adriana Karaoglanovic [UNIFESP]
dc.contributor.authorSampaio, Misako Uemura [UNIFESP]
dc.contributor.authorSampaio, C.a.m. [UNIFESP]
dc.contributor.authorAraujo, Mariana da Silva [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2015-06-14T13:30:05Z
dc.date.available2015-06-14T13:30:05Z
dc.date.issued2003-08-01
dc.description.abstractHuman plasma kallikrein, a serine proteinase, plays a key role in intrinsic blood clotting, in the kallikrein-kinin system, and in fibrinolysis. The proteolytic enzymes involved in these processes are usually controlled by specific inhibitors and may be influenced by several factors including glycosaminoglycans, as recently demonstrated by our group. The aim of the present study was to investigate the effect of glycosaminoglycans (30 to 250 µg/ml) on kallikrein activity on plasminogen and factor XII and on the inhibition of kallikrein by the plasma proteins C1-inhibitor and antithrombin. Almost all available glycosaminoglycans (heparin, heparan sulfate, bovine and tuna dermatan sulfate, chondroitin 4- and 6-sulfates) reduced (1.2 to 3.0 times) the catalytic efficiency of kallikrein (in a nanomolar range) on the hydrolysis of plasminogen (0.3 to 1.8 µM) and increased (1.9 to 7.7 times) the enzyme efficiency in factor XII (0.1 to 10 µM) activation. On the other hand, heparin, heparan sulfate, and bovine and tuna dermatan sulfate improved (1.2 to 3.4 times) kallikrein inhibition by antithrombin (1.4 µM), while chondroitin 4- and 6-sulfates reduced it (1.3 times). Heparin and heparan sulfate increased (1.4 times) the enzyme inhibition by the C1-inhibitor (150 nM).en
dc.description.affiliationUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de Bioquímica
dc.description.affiliationUniversidade Federal de São Paulo (UNIFESP) Escola Paulista de Medicina Departamento de Biofísica
dc.description.affiliationUnifespUNIFESP, EPM, Depto. de Bioquímica
dc.description.affiliationUnifespUNIFESP, EPM, Depto. de Biofísica
dc.description.sourceSciELO
dc.format.extent1055-1059
dc.identifierhttp://dx.doi.org/10.1590/S0100-879X2003000800011
dc.identifier.citationBrazilian Journal of Medical and Biological Research. Associação Brasileira de Divulgação Científica, v. 36, n. 8, p. 1055-1059, 2003.
dc.identifier.doi10.1590/S0100-879X2003000800011
dc.identifier.fileS0100-879X2003000800011.pdf
dc.identifier.issn0100-879X
dc.identifier.scieloS0100-879X2003000800011
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/1794
dc.identifier.wosWOS:000185012900012
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.subjectGlycosaminoglycansen
dc.subjectHuman plasma kallikreinen
dc.subjectPlasminogenen
dc.subjectFactor XIIen
dc.subjectC1-inhibitoren
dc.subjectAntithrombinen
dc.titleGlycosaminoglycans affect the interaction of human plasma kallikrein with plasminogen, factor XII and inhibitorsen
dc.typeinfo:eu-repo/semantics/article
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