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- W2029056385 abstract "Phorbol myristate acetate (PM A) increased the formation of |32P | PI 4,5-P, in 32P-prelabeled human platelet. In saponin-permeabilized platelets, in which 32P from exogenous |γ-32P| ATP was incorporated into PI 4-P and PI 4,5-P2, addition of 10 nM PMA resulted in increased formation of |32P|PI 4,5-P2 and |32P|PI 4-P. In order to distinguish whether increased [32P]PI 4,5-P2 formation by PMA reflected merely an increase of [32P]PI 4-P, the substrate for PI 4-P 5-kinase, or activation of PI 4-P Skinase, we examined the membrane fraction in which most of the kinase activity was located. Although PMA itself did not affect the PI 4-P 5-kinase activity in the control membranes, the kinase activity was increased nearly 2-fold in membranes pretreated with 10 nM PMA but not 4α-phorbol didecanoate which does not activate protein kinase C (PKC). These results suggested that membrane PI 4-P 5-kinase activity was stimulated by the activation of PKC.However, 100 nM PMA did not stimulate [32P]PI 4,s-P2 formation in saponin-permeabilized platelets, and the PI 4-P 5-kinase activity in membranes from platelets pretreated with 100 nM PMA was almost the same as that in control membranes. This can be explained by product inhibition, since PI 4,5-P2 inhibited concentration-dependently the membrane PI 4-P 5-kinase activity. The Ca2+ -dependent PKC fraction partially purified from the platelet cytosol stimulated the membrane PI 4-P 5-kinase activity, whereas the Ca2'-independent PKC fraction inhibited the kinase activity. Taken together, the present results suggest that the platelet membrane PI 4-P 5-kinase activity is stimulated by Ca2+ -dependent PKC (cPKC) and is negatively regulated by PI 4,s-p2 and Ca2+ -independent PKC(nPKC)." @default.
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- W2029056385 date "1994-01-01" @default.
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- W2029056385 title "Regulation of Phosphatidylinositol 4-phosphate 5-kinase by Protein Kinase C in Human Platelet Membranes" @default.
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- W2029056385 doi "https://doi.org/10.3109/09537109409006443" @default.
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