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J. Biol. Chem., Vol. 268, Issue 31, 23059-23065, 11, 1993
SK Joseph and SV Ryan
The inositol trisphosphate receptor (IP3R) in brain has been shown to be a
substrate for several different protein kinases in vitro. We have studied
the phosphorylation of the IP3R in intact cells by using isolated
hepatocytes and an antibody to immunoprecipitate the receptor protein from
detergent extracts. Stimulation of 32P-labeled hepatocytes with glucagon or
N6,2'-O-dibutyryladenosine 3',5'-cyclic monophosphate (db-cAMP) markedly
increased phosphorylation of the IP3R. However, no increase was observed in
response to angiotensin II, vasopressin, 12-O-
tetradecanoyl-phorbol-13-acetate, or epidermal growth factor. The kinetics
of phosphorylation in response to glucagon was both rapid and transient. In
agreement with previous studies, physiological concentrations of Ca2+
stimulated D-myo-inositol 1,4,5-trisphosphate (IP3) binding to
permeabilized hepatocytes (Pietri, F., Hilly, M., and Mauger, J.-P. (1990)
J. Biol. Chem. 265, 17478-17485). Pretreatment of cells with db-cAMP had no
effect on binding in the absence of added Ca2+ but enhanced binding
measured in the presence of basal low concentrations (0.16-0.25 microM) of
Ca2+ and decreased the concentration of Ca2+ required for half-maximal
stimulation. The effect of db-cAMP was associated with an increase in
affinity of the IP3 binding site without a change in maximum number of
binding sites. Preincubation of intact hepatocytes with okadaic acid alone
produced an increase in basal phosphorylation of the IP3R, and maximal
phosphorylation of the receptor was observed in the presence of both
okadaic acid and db-cAMP. However, okadaic acid blocked the effect of
db-cAMP and inhibited the effect of Ca2+ on IP3 binding. Detergent-
solubilized binding sites were already fully activated and insensitive to
modulation by Ca2+ or cAMP-dependent protein kinase. It is proposed that
the receptor in native membranes is inhibited and that Ca2+ and
cAMP-dependent protein kinase may act to relieve this inhibition.
Phosphorylation of the inositol trisphosphate receptor in isolated rat hepatocytes
Department of Pathology and Cell Biology, Thomas Jefferson University School of Medicine, Philadelphia, Pennsylvania 19107.
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