Direct activation of purified protein kinase C by unsaturated fatty acids (oleate and arachidonate) in the absence of phospholipids and Ca2+

K Murakami, A Routtenberg - FEBS letters, 1985 - Elsevier
K Murakami, A Routtenberg
FEBS letters, 1985Elsevier
Unsaturated fatty acids (oleic acid and arachidonic acid) activate purified protein kinase C
independently of phospholipid and Ca 2+. Oleic acid activation of protein kinase C is as
effective as phosphatidylserine and Ca 2+. K a, values for oleic acid and arachidonic acid
are 50 and 53 μM, respectively. In contrast to the cis fatty acids, a trans form (elaidic acid) or
a saturated fatty acid (stearic acid) has little or no effect on protein kinase C activation. If cis
fatty acid liberation is physiologically important, this suggests that another mechanism may …
Abstract
Unsaturated fatty acids (oleic acid and arachidonic acid) activate purified protein kinase C independently of phospholipid and Ca2+. Oleic acid activation of protein kinase C is as effective as phosphatidylserine and Ca2+. Ka, values for oleic acid and arachidonic acid are 50 and 53 μM, respectively. In contrast to the cis fatty acids, a trans form (elaidic acid) or a saturated fatty acid (stearic acid) has little or no effect on protein kinase C activation. If cis fatty acid liberation is physiologically important, this suggests that another mechanism may exist for protein kinase C activation, in addition to phospholipase C/phosphatidylinositol turnover signaling, possibly via the liberation of cis fatty acids by the Ca2+-dependent phospholipase A2 system.
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