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Synergistic activation by cis -fatty acid and diacylglycerol of protein kinase C and protein phosphorylation in hippocampal slices

Neuroscience, ISSN: 0306-4522, Vol: 68, Issue: 4, Page: 1017-1026
1995
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cis -Unsaturated fatty acid, which activates protein kinase C in vitro, stimulates protein phosphorylation in intact hippocampal slices. Two protein bands (44,000 and 47,000 mol. wt) are particularly sensitive to cis -fatty acid and are phosphorylated in a dose- and time-dependent manner. The cis -fatty acid-stimulated protein phosphorylation can be further potentiated with diacylglycerol or 12- O -tetradecanoylphorbol 13-acetate. Several lines of evidence indicate that the cis -fatty acid-stimulated phosphorylation of these proteins is mediated by protein kinase C. First, the cis -fatty acid effect is mimicked by other protein kinase C activators such as diacylglycerol. Second, the stimulation of the phosphorylation by these activators can be blocked by staurosporine, which potently inhibits protein kinase C. Third, a concomitant application of cis -fatty acid and diacylglycerol or 12- O -tetradecanoylphorbol 13-acetate enhances the 44,000 and 47,000 mol. wt phosphorylation in a synergistic manner, which is a novel activation mode for protein kinase C. Fourth, they can be phosphorylated by purified protein kinase C (type III: α). Moreover, the synergistic activation of purified protein kinase C by cis -fatty acid and diacylglycerol leads to a drastic increase in the phosphorylation of these two protein bands. Two-dimensional gel electrophoresis and immunoblot analysis revealed that they are both acidic proteins. The 47,000 mol. wt band consists of two protein components; one is found to be F1/growth-associated protein-43 (pI = 4.5), and the other 47,000 mol. wt protein has broad pI ranging from 4.6 to 4.9. The 44,000 mol. wt component is a major phosphoprotein with pI of 4.8–5.1.

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