Imb. Francischetti et al., BOTHROPS SP. SNAKE-VENOMS - COMPARISON OF SOME BIOCHEMICAL AND PHYSICOCHEMICAL PROPERTIES AND INTERFERENCE IN PLATELET FUNCTIONS, Comparative biochemistry and physiology. C. Comparative pharmacologyand toxicology, 119(1), 1998, pp. 21-29
Procoagulant, proteolytic, phospholipase and platelet pro-aggregating
and inhibiting activities were screened for pooled venoms of seven Bot
hrops species as well as Crotalus durissus terrificus and Lachesis mut
a snakes typical of the Brazilian territory. As reported by other auth
ors, we also found that examination of the electrophoretic and gel fil
tration patterns of Bothrops snakes venoms could not be used for ident
ification of the species of a given venom because of the lack of marke
d interspecific differences within the same genus. Our data indicated
that B. cotiara, B. alternatus and B. atrox possess no platelet pro-ag
gregating activity, low inhibitory effect on platelet aggregation and
very low or intermediate levels for the other activities. B. moojeni,
B. neuwiedi and B. jararacussu whose venoms possess high procoagulant,
platelet pro-aggregating and phospholipase activities are low in both
proteolytic and platelet inhibitory activities. B, jararaca venom sho
wed the highest inhibitory effect on platelet aggregation and very low
platelet pro-aggregating activity. Compared with the Bothrops venoms
studied, L. muta venom showed that highest proteolytic activity while
C. d. terrificus venom presented remarkable high platelet pro-aggregat
ing and phospholipase activities. In all venoms, proteolytic activity
could be completely inhibited by EDTA (2 mM) alone. In contrast, the p
resence of phenylmethylsulfonyl fluoride (5 mM) inhibited partially th
e caseinolytic activity of all venoms, except that L. muta venom, whic
h was almost completely blocked by this reagent. Altogether, these dat
a confirm the presence of high levels of metalloproteinases in the ven
oms of Crotalinae snakes. Most of these enzymes are dependent of the a
vailability of Ca2+, being much less the same concerning the presence
of serine residues in their active sites. The data indicated that the
presence and levels of procoagulant, azocaseinolytic and phospholipase
A(2) activities alone could not differentiated the species of the Bot
hrops venoms studied, particularly in the cases of B. jararaca, B. moo
jeni and B. atrox. However, the platelet inhibiting property of low do
ses of B, jararaca venom can be useful to differentiate it from B. moo
jeni venom. In the same way, the platelet pro-aggregating activity of
high doses of B. jararaca venom may be used to distinguish it from B.
atl ox crude venom, otherwise very similar but incapable to activate p
latelets. In conclusion, our comparative screening of biological prope
rties has indicated that platelet studies may serve as a tool to disti
nguish among venoms that otherwise behave biochemically in a very simi
lar way. Although promising, the general applicability of platelet act
ivation studies by snake venoms for classification or taxanomical purp
oses has yet to be extended to other family of snakes to be proven use
ful. (C) 1998 Elsevier Science Inc.