Activation of protein kinase C by oxidized diacylglycerols.
The effects of 1,2-diacylglycerol hydroperoxide (DAG-OOH), its alcohol (DAG-OH), "unoxidized" 1,2-diacylglycerol (DAG), 1,2-dioleoylglycerol (DOG), and phorbol 12-myristate acetate (PMA) on the activity of protein kinase C (PKC) isolated from rat brain were examined in the presence and absence of phosphatidylserine (PS) and calcium ion. Both DAG-OOH and DAG-OH stimulated the activity of PKC dose- and time-dependently. The ability of additives for PKC activation increased in the order of DOG, DAG << DAG-OOH, DAG-OH < PMA. DAG-OOH and DAG-OH activated PKC even in the absence of PS and calcium ion as PMA does. If DAG-OOH and DAG-OH are released from the oxidized biomembranes by the action of phospholipase C, these components may act like PMA and serve to activate the PKC-dependent signal transduction system.
Takekoshi
S
S
Department of Pathology, Tokai University School of Medicine, Isehara, Japan.
Kambayashi
Y
Y
Nagata
H
H
Takagi
T
T
Yamamoto
Y
Y
Watanabe
K
K
D000818:Animals; D001921:Brain / Q000201:enzymology; D002118:Calcium / Q000502:physiology; D004075:Diglycerides / Q000737:chemistry / Q000494:pharmacology*; D004789:Enzyme Activation; D066246:ErbB Receptors / Q000378:metabolism; D007700:Kinetics; D008054:Lipid Peroxides / Q000494:pharmacology*; D010084:Oxidation-Reduction; D010718:Phosphatidylserines / Q000502:physiology; D011493:Protein Kinase C / Q000378:metabolism*; D051381:Rats; D017382:Reactive Oxygen Species / Q000737:chemistry; D015398:Signal Transduction; D013329:Structure-Activity Relationship
D004075:Diglycerides; D008054:Lipid Peroxides; D010718:Phosphatidylserines; D017382:Reactive Oxygen Species; D066246:ErbB Receptors; D011493:Protein Kinase C; D002118:Calcium