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Protein kinase C does not regulate diacylglycerol metabolism in aortic smooth muscle cells

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Summary

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.

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Abbreviations

IP3 :

inositol 1,4,5-trisphosphate

DG:

diacylglycerol

MG:

monoacylglycerol

PL:

phospholipid(s)

diC8:

dioctanoylglycerol

H-7:

1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride

monoC8:

monooctanoylglycerol

PS:

phosphatidylserine

PDBu:

phorbol 12,13-dibutyrate

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Chuang, M., Dell, K.R. & Severson, D.L. Protein kinase C does not regulate diacylglycerol metabolism in aortic smooth muscle cells. Mol Cell Biochem 96, 69–77 (1990). https://doi.org/10.1007/BF00228454

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