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Toxins (Basel) ; 8(7)2016 07 20.
Artigo em Inglês | MEDLINE | ID: mdl-27447669

RESUMO

Tumor necrosis factor (TNF) is a major cytokine in inflammatory processes and its deregulation plays a pivotal role in several diseases. Here, we report that a zinc metalloprotease extracted from Bothrops moojeni venom (BmooMP-alpha-I) inhibits TNF directly by promoting its degradation. This inhibition was demonstrated by both in vitro and in vivo assays, using known TLR ligands. These findings are supported by molecular docking results, which reveal interaction between BmooMP-alpha-I and TNF. The major cluster of interaction between BmooMP-alpha-I and TNF was confirmed by the structural alignment presenting Ligand Root Mean Square Deviation LRMS = 1.05 Å and Interactive Root Mean Square Deviation IRMS = 1.01 Å, this result being compatible with an accurate complex. Additionally, we demonstrated that the effect of this metalloprotease on TNF is independent of cell cytotoxicity and it does not affect other TLR-triggered cytokines, such as IL-12. Together, these results indicate that this zinc metalloprotease is a potential tool to be further investigated for the treatment of inflammatory disorders involving TNF deregulation.


Assuntos
Bothrops , Venenos de Crotalídeos/metabolismo , Metaloendopeptidases/metabolismo , Simulação de Acoplamento Molecular , Proteínas de Répteis/metabolismo , Fator de Necrose Tumoral alfa/metabolismo , Zinco/metabolismo , Animais , Células Cultivadas , Venenos de Crotalídeos/química , Venenos de Crotalídeos/farmacologia , Macrófagos/efeitos dos fármacos , Macrófagos/metabolismo , Masculino , Metaloendopeptidases/química , Metaloendopeptidases/farmacologia , Camundongos Endogâmicos C57BL , Ligação Proteica , Conformação Proteica , Proteólise , Proteínas de Répteis/química , Proteínas de Répteis/farmacologia , Relação Estrutura-Atividade , Especificidade por Substrato , Receptores Toll-Like/agonistas , Receptores Toll-Like/metabolismo , Fator de Necrose Tumoral alfa/química , Zinco/química
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