Efeito de ions metalicos divalentes sobre a atividade de metaloproteases da matriz secretadas por celulas do tecido gengival

AUTOR(ES)
DATA DE PUBLICAÇÃO

2000

RESUMO

Matrix Metalloproteinases (MMPs) are a family of proteolytic enzymes that mediates the degradation of extracellular matrix. They are secreted as inactive proenzymes (zymogen), and they are thought to be activated in the tissue by cleavage of the propeptide. All members of this family have zinc and calcium binding to the active site. The MMPs take part in physiologic and pathologic events, as developmental of salivary glands and teeth and periodontal disease, respectively. Several divalent metal íons, as zinc and copper, are contained in dental materiaIs, as dental amalgam, and the interaction between metal íons and the oral environrnent is a major subject in dental research. The aim of this work was to study the effect of several of divalent metaIs on the activity of MMPs secreted by gingival tissue .cells. Gingival explants were cultured at 37° C for 24 h in DMEM and the secreted enzymes were characterized as MMP-2 and MMP-9 by immunoprecipitation. After, the effect of metaIs on the activity of the MMPs was tested using gelatin zymography and also against denatured collagen type I degradation in vitro. Divalente metaIs, as zinc and cupper, inhibited active and zimogen forms of MNrP-2 and MMP-9.

ASSUNTO(S)

metais zinco enzimas

ACESSO AO ARTIGO

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