TY - JOUR
T1 - Mechanism of hemolysis induced by nematocyst venom
T2 - Roles of phospholipase A and direct lytic factor
AU - Hessinger, David A.
AU - Lenhoff, Howard M.
N1 - Funding Information:
The authors are grateful to Judy Hessinger for her expert and diligent culturing of Aiptasia and to Dr. James Clegg at the Laboratory for Quantitative Biology, University of Miami, Coral Gables, Fla., for access to his laboratory and for his stimulating ideas. This work was supported in part by NIH Training Grant No. HP 00187 to the Laboratory for Quantitative Biology, grants NSF No. GB5491 and NIH No. GM5011 to H.M.L., and the Division of Sponsored Research at the University of South Florida.
PY - 1976/4
Y1 - 1976/4
N2 - Pure venom from the acontial nematocysts of the sea anemone Aiptasia pallida exhibited phospholipase A (phosphatide acyl-hydrolase; EC 3.1.1.4) activity on a mixture of free phospholipids. Diethyl aminoethyl cellulose fractionation of the venom gave four distinct protein peaks with the phospholipase A activity being restricted to fractions III and IV. These two fractions tested separately also were able to lyse red blood cells weakly. Fractions I and II enhanced the hemolytic activity of fractions III and IV, with fractions I and III giving as much as ninefold enhancement over that of III alone. Fraction I appears analogous to the direct lytic factor of some snake and bee venoms. Fraction III, which could not appreciably hydrolyze the phospholipids of the intact red cell membrane, was able to do so in the presence of fraction I. The sequential interactions of these two nematocyst venom proteins with the red blood cell membrane to produce hemolysis is discussed.
AB - Pure venom from the acontial nematocysts of the sea anemone Aiptasia pallida exhibited phospholipase A (phosphatide acyl-hydrolase; EC 3.1.1.4) activity on a mixture of free phospholipids. Diethyl aminoethyl cellulose fractionation of the venom gave four distinct protein peaks with the phospholipase A activity being restricted to fractions III and IV. These two fractions tested separately also were able to lyse red blood cells weakly. Fractions I and II enhanced the hemolytic activity of fractions III and IV, with fractions I and III giving as much as ninefold enhancement over that of III alone. Fraction I appears analogous to the direct lytic factor of some snake and bee venoms. Fraction III, which could not appreciably hydrolyze the phospholipids of the intact red cell membrane, was able to do so in the presence of fraction I. The sequential interactions of these two nematocyst venom proteins with the red blood cell membrane to produce hemolysis is discussed.
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U2 - 10.1016/0003-9861(76)90297-6
DO - 10.1016/0003-9861(76)90297-6
M3 - Article
C2 - 5957
SN - 0003-9861
VL - 173
SP - 603
EP - 613
JO - Archives of Biochemistry and Biophysics
JF - Archives of Biochemistry and Biophysics
IS - 2
ER -