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 IPsR in intact cells by using isolated hepatocytes and an antibody to immunoprecipitate the receptor protein from detergent extracts.Stimulation of s2P-labeled hepatocytes with glucagon or N8,ZI-Odibutyryladenosine 3',5'-cyclic monophosphate (db-CAMP) markedly increased phosphorylation of the IPsR.However, no increase was observed in response to angiotensin 11, vasopressin, 12-0-tetradecanoylphorbol-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 (IPS) binding to permeabilized hepatocytes (Pietri, F., Hilly, M., and Mauger,
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Joseph et al. (1993) studied this question.
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