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The effect of a reduction in protein kinase C activity on the metabolism of exogenous [3H]diC8 by freshly isolated smooth muscle cells from rabbit aorta and cultured A10 smooth muscle cells was determined. The metabolism of [3H]diC8 by both smooth muscle cell preparations was predominantly by hydrolysis to yield monoC8 and glycerol (lipase pathway); very little radioactivity was incorporated into phospholipids. Diacylglycerol lipase activity measured in vitro with A10 cell homogenates was much greater than diacylglycerol kinase activity. The addition of the protein kinase C inhibitor H-7 to incubations of isolated aortic smooth muscle cells and cultured A10 cells had no significant effect on the metabolism of [3H]diC8. Protein kinase C activity in cultured A10 cells preincubated for 20 h with a phorbol ester was reduced to 14% of control as a consequence of down-regulation, but diC8 metabolism was not changed. Therefore, protein kinase C does not regulate the metabolism of diacylglycerols in aortic smooth muscle cells.
M Chuang, and
K R Dell, and
D L Severson
January 1989,
The American journal of physiology,
M Chuang, and
K R Dell, and
D L Severson
May 1998,
Journal of vascular surgery,
M Chuang, and
K R Dell, and
D L Severson
July 1989,
Biochemical and biophysical research communications,
M Chuang, and
K R Dell, and
D L Severson
October 1991,
Biochemical and biophysical research communications,
M Chuang, and
K R Dell, and
D L Severson
September 1988,
Biochemical and biophysical research communications,
M Chuang, and
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D L Severson
May 1989,
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M Chuang, and
K R Dell, and
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M Chuang, and
K R Dell, and
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M Chuang, and
K R Dell, and
D L Severson
August 1995,
Biochemical and biophysical research communications,
M Chuang, and
K R Dell, and
D L Severson
December 1987,
Experimental cell research,
