Laboratorio Of Venenos E Toxinas Animais Lvta

São Carlos, Brazil

Laboratorio Of Venenos E Toxinas Animais Lvta

São Carlos, Brazil
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Andrich F.,Laboratorio Of Venenos E Toxinas Animais Lvta | Andrich F.,Laboratorio Of Quimica Of Proteinas Lqp | Carnielli J.B.T.,Laboratorio Of Quimica Of Proteinas Lqp | Cassoli J.S.,Laboratorio Of Venenos E Toxinas Animais Lvta | And 6 more authors.
Toxicon | Year: 2010

A new vasoactive cytolytic toxin, referred to as Sp-CTx, has been purified from the venom of the scorpionfish Scorpaena plumieri by a combination of gel filtration and anion exchange chromatographies. An estimation of Sp-CTx native molecular mass, performed by size exclusion chromatography, demonstrated that it is a 121 kDa protein. Further physicochemical studies revealed its glycoproteic nature and dimeric constitution, comprising subunits of approximately 65 kDa (MALDI-TOF-MS). Such protein has proved to possess a potent hemolytic activity on washed rabbit erythrocytes (EC50 0.46 nM), whose effect was strongly reduced after treatment with antivenom raised against stonefish venom - Synanceja trachynis (SFAV). This cross-reactivity has been confirmed by western blotting. Like S. plumieri whole venom (100 μg/mL), Sp-CTx (1-50 nM) caused a biphasic response on phenylephrine pre-contracted rat aortic rings, characterized by an endothelium- and dose-dependent relaxation phase followed by a contractile phase. The vasorelaxant activity has been abolished by l-NAME, demonstrating the involvement of nitric oxide on the response. We report here the first isolation of a cytolytic/vasoactive protein from scorpionfish venom and the data provided suggest structural and functional similarities between Sp-CTx and previously published stonefish hemolytic toxins. © 2010 Elsevier Ltd.

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