Feb 1, 1976

Properties of a toxin from the sea anemone Stoichacis helianthus, including specific binding to sphingomyelin

Proceedings of the National Academy of Sciences of the United States of America
A W Bernheimer, L S Avigad

Abstract

Stoichactis helianthus toxin, a protein derived presumably from the nematocysts, was purified to homogeneity. It has a molecular weight of about 16,000, an isoelectric pH of 9.8, and it contains approximately 3.7% carbohydrate. It is powerfully hemolytic for erythrocytes derived from a variety of animal species, those of the cat being the most sensitive and those of the guinea pig the most resistant. The toxin is lytic also for rabbit blood platelets, and it destroys cultured fibroblasts but is inactive for several kinds of bacterial protoplasts and spheroplasts. The hemolytic activity is specifically inhibited by sphingomyelin, and it is proposed that this phospholipid is the constituent of the membrane which functions as receptor for the toxin. Supporting evidence includes the findings that enzymes known to destroy sphingomyelin (a) prevent erythrocyte membranes from inhibiting hemolysis, and (b) render erythrocytes resistant to lysis by the toxin. The mechanism underlying hemolysis may involve translocation of membrane sphingomyelin by virtue of a specific affinity of the coelenterate protein for this phospholipid.

  • References12
  • Citations96

References

  • References12
  • Citations96

Citations

Mentioned in this Paper

SDS-PAGE
Cnidaria
Sea Anemones
Isoelectric Focusing
Fibroblasts
Phospholipase
Sphingomyelins
Erythrocytes
Hemolysis
Marine Toxins

About this Paper

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