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J. Biol. Chem., Vol. 261, Issue 16, 7184-7190, 06, 1986
YA Hannun, CR Loomis and RM Bell
The phospholipid, sn-1,2-diacylglycerol, and calcium dependencies of rat
brain protein kinase C were investigated with a mixed micellar assay
(Hannun, Y., Loomis, C., and Bell, R.M. (1985) J. Biol. Chem. 260,
10039-10043). Protein kinase C activity was independent of the number of
Triton X-100, phosphatidylserine (PS), and sn-1,2- dioleoylglycerol
(diC18:1) mixed micelles. Activation was strongly dependent on the mole per
cent of PS and diC18:1. Activity of protein kinase C was dependent on PS,
diC18:1, and calcium in mixed micelles prepared from detergents other than
Triton X-100. This is consistent with the micelle providing an inert
surface into which the lipid cofactors partition. Molecular sieve
chromatography provided direct evidence for the homogeneity of Triton
X-100, PS, and diC18:1 mixed micelles. Mixing studies and surface dilution
studies indicated that PS and diC18:1 rapidly equilibrate among the mixed
micelles. At saturating calcium, the diC18:1 dependence was strongly
dependent on the mole per cent PS present. At 10 mol % PS, 0.25 mol %
diC18:1 gave maximal activity whereas 6 mol % PS and 6 mol % diC18:1 did
not give maximal activity. diC18:1 dependencies were hyperbolic at all PS
levels tested. The data support the conclusion that a single molecule of
diC18:1/micelle is sufficient to activate monomeric protein kinase C. The
mole per cent PS required for maximal activation was reduced markedly as
the mole per cent diC18:1 increased. Under all conditions tested, the PS
dependence of protein kinase C activation lagged until greater than 3 mol %
PS was present. Then activation occurred in a cooperative manner with Hill
numbers near 4. These data indicate that 4 or more molecules of PS are
required to activate monomeric protein kinase C. PS was the most effective
of all the phospholipids tested in the mixed micelle assay. diC18:1 was
found to modulate the amount of calcium required for maximal activity. As
the level of Ca2+ increased, the mole per cent PS required reached a
limiting value of 3 mol %. A number of sn-1,2-diacylglycerols containing
short chain fatty acids activated protein kinase C in a saturable manner in
mixed micelles. The data are discussed in relation to a model for protein
kinase activation.
Protein kinase C activation in mixed micelles. Mechanistic implications of phospholipid, diacylglycerol, and calcium interdependencies
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