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

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

Content Provider	Semantic Scholar
Author	Steer, Sarah A. Wirsig, Karin C. Creer, Michael H. Ford, David McHowat, Jane
Copyright Year	2002
Abstract	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.
Starting Page	390
Ending Page	393
Page Count	4
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://ajpcell.physiology.org/content/ajpcell/283/6/C1621.full.pdf
PubMed reference number	12419708v1
Volume Number	283
Issue Number	6
Journal	American journal of physiology. Cell physiology
Language	English
Access Restriction	Open
Subject Keyword	Arachidonic Acid Buffers GF 109203X Muscle Cells Phorbols Phospholipase Phospholipids Plasmalogens Protein Kinase C Protein Kinase C-epsilon Signal Transduction Pathways Tissue membrane lysoplasmenylcholine
Content Type	Text
Resource Type	Article

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