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J. Biol. Chem., Vol. 269, Issue 7, 4866-4871, 02, 1994
SJ Slater, MB Kelly, FJ Taddeo, C Ho, E Rubin and CD Stubbs
The hypothesis that protein kinase C (PKC) activity is sensitive to
phospholipid head group interactions was tested using lipid bilayers of
defined composition with PKC purified from rat brain. The head group
interactions were modulated by varying phosphatidylcholine cis-
unsaturation, vesicle curvature, and by the addition of
phosphatidylethanolamine and cholesterol. With unilamellar vesicles
(including 20 mol% brain phosphatidylserine), increased phosphatidylcholine
unsaturation potentiated basal and phorbol ester stimulated PKC activity.
By contrast, in the presence of phosphatidylethanolamine, the activity
decreased with increasing phosphatidylcholine unsaturation. Weakening
phospholipid head group interactions spaces the head group region and
increases interstitial water, and this effect was assessed from its effect
on the fluorescence intensity of the phospholipid-labeled fluorophore
1-palmitoyl-2-N-(4- nitrobenzo-2-oxa-1,3-diazole)aminohexanoylphosphat
idylcholin e (C6-NBD- PC). When the PKC activities with vesicles of varying
phosphatidylcholine unsaturation, with and without
phosphatidylethanolamine, were plotted as a function of the fluorescence
intensity of C6-NBD-PC-labeled vesicles, a biphasic profile was obtained,
which had an optimum value of intensity, relating to head group spacing,
that corresponded to a maximal enzyme activity. A similar biphasic curve
was also found when PKC activities were plotted as a function of published
bilayer intrinsic curvature x-ray diffraction data, a parameter closely
related to head group spacing. By contrast, no simple relationship was
evident between PKC activity and 1,6-diphenyl-1,3,5-hexatriene anisotropy,
taken as a measure of lipid order or fluidity. Therefore, increasing the
level of phosphatidylcholine unsaturation, phosphatidylethanolamine, or
cholesterol either potentiates or attenuates PKC activity, dependent on
whether the initial condition is above or below its optimum.
The modulation of protein kinase C activity by membrane lipid bilayer structure
Department of Pathology and Cell Biology, Thomas Jefferson University, Philadelphia, Pennsylvania 19107.
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