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J. Biochem, 1988, Vol. 104, No. 4 492-494
© 1988 Japanese Biochemical Society

other

Detection in Human Platelets of Phospholipase A2 Activity Which Preferentially Hydrolyzes an Arachidonoyl Residue1

Dae Kyong Kim, Ichiro Kudo2 and Keizo Inoue

Facultyl of Pharmaceutical Sciences, The University of Tokyo Bunkyo-ku, Tokyo 113

2 To whom all correspondence should be addressed

It has been generally considered that highly specific liberation of arachidonic acid is induced upon the stimulation of the platelets, although the molecular mechanism of the regulation of its action has not been well understood. An aim of the present study is to clarify the role of phospholipase A2 in the arachidonic acid metabolism within human platelets. Phosphatidylcholine or phosphatidylethanolamine with arachidonate at the sn-2 position of glycerol was cleaved efficiently by phospholipase A2 activity in homogenates as well as in the cytoplasmic fraction of human platelets, leading to the selective liberation of free arachidonate, whereas phospholipids with linoleate were hardly hydrolyzed under the same conditions. Double-reciprocal plots of kinetic data further strengthened the conclu sion that human platelet phospholipase A2 showed high selectivity for arachidonoyl residue. This enzyme may play a crucial role in the intracellular metabolism of the arachidonate of phospholipids.

1 This work was supported in part by Grants-in-Aid (Nos. 62222002, 62624504, 62870093) for Scientific Research from the Ministry of Education, Science and Culture of Japan.


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