Mechanism of activation by ca2+ of hemolysis induced by lytic polypeptide equinatoxin ii
Keywords:
erythrocyte, hemolysis, divalent cations, equinatoxin IIAbstract
Equinatoxin II is a cytolytic polypeptide from the sea anemone Actinia equina L. which forms pores in
natural and artificial membranes. In the present study, we show that the mechanism by which Ca2+
activates toxin-induced hemolysis of human red blood cells consists of the ability of Ca2+ which enters
the cell presumably through preformed toxin-induced pores and acts inside the cell to increase the rate of
toxin binding to the membrane. As a result, a larger amount of pores is produced thus increasing the rate
of hemolysis. In addition, the data reveal that equinatoxin II induces hemolysis of RBC interacting with a
limited number of toxin-binding sites (receptors) with an upper estimate of (180 35) 103 sites per one
cell. The total number of toxin-binding sites does not depend on the presence of Ca2+. These data strongly
suggest that specific receptor must exist on the erythrocyte membrane to mediate the hemolytic action of
this toxin.
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