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The activity of protein kinase C (Ca2+/phospholipid-dependent enzyme) in the presence of phosphatidylserine and its physiological regulator, diacylglycerol, could be suppressed by a mixture of brain gangliosides. Half-maximal inhibition was observed at 30 microM and was nearly complete at 100 microM. Inhibition was observed at all concentrations of Ca2+ between 10(-8) and 10(-4) M. Inhibition of protein kinase C activity could not be reversed by increasing the concentration of diacylglycerol or the substrate, histone. Inhibition was also observed when myelin basic protein or a synthetic myelin basic protein peptide was used as substrate. Among the individual gangliosides, the rank order of potency was GT1b greater than GD1a = GD1b greater than GM3 = GM1. Our results suggest that gangliosides may regulate the responsiveness of protein kinase C to diacylglycerol.
D Kreutter, and
J Y Kim, and
J R Goldenring, and
H Rasmussen, and
C Ukomadu, and
R J DeLorenzo, and
R K Yu
May 1988,
FASEB journal : official publication of the Federation of American Societies for Experimental Biology,
D Kreutter, and
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J R Goldenring, and
H Rasmussen, and
C Ukomadu, and
R J DeLorenzo, and
R K Yu
June 1988,
Neurochemical research,
D Kreutter, and
J Y Kim, and
J R Goldenring, and
H Rasmussen, and
C Ukomadu, and
R J DeLorenzo, and
R K Yu
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January 2002,
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D Kreutter, and
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H Rasmussen, and
C Ukomadu, and
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The Journal of biological chemistry,
D Kreutter, and
J Y Kim, and
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H Rasmussen, and
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D Kreutter, and
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R J DeLorenzo, and
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May 2004,
The Journal of biological chemistry,
D Kreutter, and
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H Rasmussen, and
C Ukomadu, and
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R K Yu
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D Kreutter, and
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Journal of neurochemistry,
