Inibição da angiogênese inflamatória e da agregação plaquetária pela enzima BmooMPα-I, uma metaloprotease da peçonhada serpente Bothrops moojeni

• Ano de defesa: 2012
• Autor(a) principal: Gomes Filho, Saulo Antônio
• Tipo de documento: Dissertação
• Tipo de acesso: Acesso aberto
• Idioma: por
• Instituição de defesa: Universidade Federal de Uberlândia; BR; Programa de Pós-graduação em Genética e Bioquímica; Ciências Biológicas; UFU
• Palavras-chave em Português: Proteínas; Serpente peçonhenta - Peçonha; Bothrops moojeni; Metaloproteases; Agregação plaquetária; Angiogênese; Metalloproteinase; Platelet aggregation; Angiogenesis; CNPQ::CIENCIAS BIOLOGICAS::GENETICA
• Link de acesso: https://repositorio.ufu.br/handle/123456789/15862; https://doi.org/10.14393/ufu.di.2012.350

The venom of snakes from genus Bothrops contain toxin composed of several pharmacologically active substances, especially protein constituents, which act to induce local and systemic physiological changes in the body in which it is inoculated. Among the enzymatic component of the venoms are metalloproteinases, which are proteolytic enzymes zinc-dependents involved in the effects of ofidic envenoming. BmooMPα-I is a fibrin(ogen)olytic non-hemorrhagic enzyme isolated from B. moojeni snake venom. It shows a molecular mass of about 24.5 kDa, and belongs to the P-I class. In order to investigate its activity in relation to physiological processes, this work had as objective evaluated the BmooMPα-I influence in platelet aggregation and in inflammatory angiogenesis. The enzyme inhibited specifically the epinephrine-induced platelet aggregation when previously incubated with platelet rich plasma, not showing inhibition with ADP, collagen and ristocetin. Its activity is suppressed by denaturation, showing the dependence of the enzymatic action in the inhibition mechanism. About the inflammatory angiogenesis, our results showed that BmooMPα-I is an angiogenesis inhibitor.