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J. Biol. Chem., Vol. 260, Issue 27, 14477-14483, 11, 1985
PF Blackmore, SB Bocckino, LE Waynick and JH Exton
Treatment of isolated hepatocytes with NaF produced a concentration-
dependent activation of phosphorylase, inactivation of glycogen synthase,
efflux of Ca2+, rise in cytosolic free Ca2+ ([Ca2+]i), increase in
myo-inositol-1,4,5,-P3 levels, decrease in phosphatidylinositol-4,5-P2
levels, and increase in 1,2-diacylglycerol levels. These changes were
evident within 1 min and maximum at 2-5 min. Maximum effects on Ca2+
efflux, [Ca2+]i, glycogen synthase, and phosphorylase were observed with 15
mM NaF, whereas myo-inositol-1,4,5- P3 and 1,2-diacylglycerol levels were
maximally stimulated by 50 mM NaF. The levels of intracellular cAMP were
decreased by NaF (up to 10 mM) in the absence or presence of glucagon
(0.1-1 nM) or forskolin (2 microM). The effects of low doses of NaF (2-15
mM) to inhibit basal or glucagon-stimulated cAMP accumulation, mobilize
Ca2+, activate phosphorylase, and inactivate glycogen synthase were all
potentiated by AlCl3. This potentiation was abolished by the Al3+ chelator
deferoxamine. These results illustrate that AlF4- can mimic the effects of
Ca2+-mobilizing hormones in hepatocytes and suggest that the coupling of
the receptors for these hormones to the hydrolysis of
phosphatidylinositol-4,5-P2 to myo-inositol 1,4,5-P3 is through a guanine
nucleotide-binding regulatory protein. This is because AlF4- is known to
modulate the activity of other guanine nucleotide regulatory proteins (Ni,
Ns, and transducin).
Role of a guanine nucleotide-binding regulatory protein in the hydrolysis of hepatocyte phosphatidylinositol 4,5-bisphosphate by calcium-mobilizing hormones and the control of cell calcium. Studies utilizing aluminum fluoride
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