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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 conclusion 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.
D K Kim, and
I Kudo, and
K Inoue
May 1993,
Biochimica et biophysica acta,
D K Kim, and
I Kudo, and
K Inoue
September 1986,
Biochimica et biophysica acta,
D K Kim, and
I Kudo, and
K Inoue
September 1983,
Proceedings of the National Academy of Sciences of the United States of America,
D K Kim, and
I Kudo, and
K Inoue
January 1979,
Biochimie,
D K Kim, and
I Kudo, and
K Inoue
December 1981,
Agents and actions,
D K Kim, and
I Kudo, and
K Inoue
June 1985,
The Journal of biological chemistry,
D K Kim, and
I Kudo, and
K Inoue
December 1987,
Seikagaku. The Journal of Japanese Biochemical Society,
D K Kim, and
I Kudo, and
K Inoue
January 1991,
Archives of biochemistry and biophysics,
D K Kim, and
I Kudo, and
K Inoue
February 1991,
Biokhimiia (Moscow, Russia),
D K Kim, and
I Kudo, and
K Inoue
November 2002,
Platelets,
