Edematogenic Activity Of The Protein With Disintegrin-Like/Cysteine-Rich Domains Isolated From Bothrops moojeni Snake Venom (Viperidae, Crotalinae).

¹Magrin, R.A.; ^1,2Vitorino, A.F.C.; ²Ribeiro, J.U.; ²Selistre-de-Araújo, H.S.; ¹Hamaguchi, A. and ¹Homsi-Brandeburgo, M.I.

1 Instituto de Genética e Bioquímica (INGEB), Universidade Federal de Uberlândia (UFU), Uberlândia-MG; 2 Departamento de Ciências Fisiológicas (DCF), Universidade Federal de São Carlos (UFSCar), São Carlos-SP, Brasil.

Several studies has shown that the non-protease domains of the class snake venom metalloproteinases (SVMPs) are able to inhibit the platelet aggregation by blocking essential procoagulant integrins on platelet surface. In this work we report on the partial isolation and characterization of a protein (BmjED) from the venom of the snake Bothrops moojeni, using chromatographies on DEAE-Sephacel and Sephadex G-75 columns. The protein have molecular mass by SDS-PAGE under reducing (~32 kDa) and nonreducing (~40 kDa) conditions. Its amino acid sequence from Edman analysis of the first 20 residues amino-terminal region (LGNDIVSPDVVGNELLEVGE) showned high similarities with others disintegrin-like proteins from various snake venoms. BmjED did not show proteolytic activity and did not inhibit collagen- and ADP-induced platelet aggregation. When injected in different doses (50, 100 and 200 g) into the posterior paw of Swiss mice (n = 5), BmjED induced the development of a dose-dependent edema. After 1, 2 and 3 hours the thickness of each paw was measured, using a low pressure caliper and edema expressed as the percent increment. This protein possibly is a proteic fragment containing the disintegrin-like/cysteine-rich domains of metalloproteinase.The ability of BmjED to induce an edematogenic process, suggesting the existence of a still unknown nonenzymatic mechanism of vascular permeability increase, caused by protein with disintegrin-like/cysteine-rich domains.

Financial Support: CNPq, FAPEMIG and FAPESP.

Correspondence to: ramagrin@hotmail.com