Poster 23 - Partial biochemical and pharmacological characterization of Scorpaena plumieri fish

Poster 23. Congresso da Sociedade Brasileira de Toxinologia, 8., Symposium of the Pan American Section of the International Society on Toxinology, 8., 2004, Angra dos Reis, Brasil. Abstracts... J. Venom. Anim. Toxins incl.Trop. Dis., 2004, 10, 3, p.382.

Partial Biochemical and Pharmacological Characterization of Scorpaena plumieri fish venom.

^1,2Andrich, F.; ¹Cassoli, J.S.; ¹Carrijo, L.C.; ²De Lima, M.E.; ¹Figueiredo, S.G.

1 Lab. de Toxinologia, Dept. de Ciências Fisiológicas, CBM - UFES, Vitória/ES; 2 LVTA, Dept. de Bioquímica e Imunologia, ICB – UFMG, Belo Horizonte/MG.

The venomous fish Scorpaenaplumieri is found along the Brazilian coast, where provokes a great number of accidents. In this work we describe a partial biochemical characterization of Scorpaenaplumieri whole venom, which is contained within the tissues that envelop the dorsal, pelvic and anal fin spines. Like other venomous fishes, scorpionfish venom is proteic in nature; SDS-PAGE showed many protein bands which ranged in size approximately from 15 to 300KDa. Venom obtained from fresh captured specimens of this fish was tested in vitro or in animal models for a better characterization of its toxics properties. The venom is toxic/lethal for mice (LD50=2.6mg/g mouse) and sub-lethal doses produced convulsions, respiratory distress, paralysis and increases in defecation and urination. In addition, the fresh venom induced decreases in blood pressure, heart rate and respiratory frequency (Biopac System) when it was injected in experimental rats (50mg i.v.) and produced hemorrhagic spots in mice dorsal skin (Minimum Hemorrhagic Dose » 30mg). Scorpaenaplumieri venom has also been found to be strong hemolytic to washed rabbit erythrocytes. These pharmacological activities were unstable even when the venom was frozen; this fact could be associated with the presence of proteolytic enzymes. The SDS-PAGE assays showed that the crude venom digests gelatin and hydrolyses a, and g chains of fibrinogen. Unlike other biological activities, the proteolytic activities were stable at 4°C. Fractionation of the Scorpaenaplumieri venom on a Sephacryl S-200 HR column was achieved and demonstrated that fibrinogen and gelatin were hydrolysed by distinct enzymes. Our results open prospects for the identification of new proteins that may prove useful either as research tools or as therapeutic agents.