ISOLATION AND CHARACTERIZATION OF TWO NEW LECTIN TYPE C ISOLATED FROM THE Bothrops erythromelas VENOM.

TOYAMA, D.O.(1); ANTUNES, E.(2), CAMARGO, E.A. (2), MARANGONI, S.(3), CARNEIRO, E.M.(4) AND TOYAMA, M.H.(5)

(1) Universidade Mackenzie, São Paulo, (2) Departamento de Farmacologia, FMC, UNICAMP, (3) Departamento de Bioquímica, IB, UNICAMP, (4) Departamento de Fisiologia e Biofísica, IB, UNCAMP;  (5) UNESP, CELP, São Vicente.

In this article we isolated two new lectin type C isoform from the venom of Bothrops erythromelas venom.  Both proteins in the PAGE showed the presence of one electrophoretic band with molecular mass of 28kDa and in the presence of DTT we observed both proteins the presence of only 14kDa spot.  Both proteins did not showed significative activity on the platelet aggregation but induce significative edema.  The hamaglutination activity for both protein were inhibited by D-galactose, D-Lactose, that inhibited the edematogenic activity.  Both lectin also induce strong increasing of the insulin secretion in the isolated -cells by activation of PKC and PKA kinases and IP3 mobilization.  These insulin secretion potencializations were inhibited by pre incubation of both proteins with lactose.  Thus we conclude that both C-type lectin isolated from the Botrhops erythromelas venom was bind with specific membrane receptor mediated by specific recognition of D-galactose sugar residues.

KEY WORDS: lectin type C, Bothrops erythromelas, isulin secretion.

FINANCIAL SUPPORT: FAPESP, CNPq.