Produção Nacional
Revisado por pares
Activation of αMβ2-mediated phagocytosis by HF3, a P-III class metalloproteinase isolated from the venom of Bothrops jararaca
2004; Elsevier BV; Volume: 322; Issue: 3 Linguagem: Inglês
10.1016/j.bbrc.2004.08.012
ISSN1090-2104
AutoresCarlos Alberto-Silva, Juliana P. Zuliani, Marina T. Assakura, Reinhard Mentele, Antônio Carlos Martins de Camargo, Catarina Teixeira, Solange M.T. Serrano,
Tópico(s)Blood Coagulation and Thrombosis Mechanisms
ResumoThe integrin αMβ2 regulates important cell functions in inflammation being the primary phagocytic receptor on macrophages. HF3, a metalloproteinase isolated from Bothrops jararaca venom, is a potent hemorrhagic toxin. A cDNA encoding HF3 indicated that it is a multidomain molecule composed of a pro-domain, a catalytic domain with a zinc binding sequence, followed by disintegrin-like and cysteine-rich domains. It is known that metalloproteinases play a relevant role in the pathogenesis of venom-induced local tissue damage including inflammation. In this study we evaluated the effects of native HF3 and its recombinant disintegrin-like/cysteine-rich domains (DC-HF3) on αMβ2-mediated phagocytosis of opsonized-zymosan particles by macrophages. HF3 and DC-HF3 significantly increased phagocytosis and this activity was inhibited by anti-αM and anti-β2 antibodies. The data show the ability of P-III metalloproteinases to activate macrophages for phagocytosis through integrin αMβ2 and suggest that the disintegrin-like/cysteine-rich domains are important for this effect. This is the first report on the activation of phagocytosis via αMβ2 integrin by a metalloproteinase containing disintegrin-like/cysteine-rich domains.
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