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Am J Physiol Cell Physiol 283: C1621-C1626, 2002; doi:10.1152/ajpcell.00109.2002
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Vol. 283, Issue 6, C1621-C1626, December 2002

Regulation of membrane-associated iPLA2 activity by a novel PKC isoform in ventricular myocytes

Sarah A. Steer1, Karin C. Wirsig2, Michael H. Creer2, David A. Ford1, and Jane McHowat2

Departments of 1 Biochemistry and 2 Pathology, St. Louis University School of Medicine, St. Louis, Missouri 63104

Thrombin stimulation of rabbit ventricular myocytes increases membrane-associated, Ca2+-independent phospholipase A2 (iPLA2) activity, resulting in accelerated hydrolysis of membrane plasmalogen phospholipids and increased production of arachidonic acid and lysoplasmenylcholine. This study was designed to investigate the signal transduction pathways involved in activation of membrane-associated iPLA2. Incubation of isolated membrane fractions suspended in Ca2+-free buffer with thrombin or phorbol 12-myristate 13-acetate resulted in a two- to threefold increase in iPLA2 activity. Prior treatment with the PKC inhibitor GF-109203X blocked iPLA2 activation by thrombin. These data suggest that a novel PKC isoform present in the membrane fraction modulates iPLA2 activity. Immunoblot analysis revealed a significant portion of PKC-epsilon present in the membrane fraction, but no other membrane-associated novel PKC isoform was detected by this method. These data indicate that activation of membrane-associated iPLA2 is mediated by a membrane-associated novel PKC isoform in thrombin-stimulated rabbit ventricular myocytes.

signal transduction; ventricular myocytes; calcium-independent phospholipase A2; protein kinase C


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