Cyclic AMP-dependent phosphorylation of the inositol-1,4,5-trisphosphate receptor inhibits Ca2+ release from platelet membranes

doi:10.1016/0006-291X(92)90675-B

Biochemical and Biophysical Research Communications

Volume 184, Issue 2, 30 April 1992, Pages 893-899

https://doi.org/10.1016/0006-291X(92)90675-B Get rights and content

Abstract

Purified internal platelet membranes were treated with the catalytic subunit of protein kinase A to determine its effect on inositol-1,4,5-trisphosphate (IP3)-mediated Ca²⁺ release. Release kinetics were monitored using rhod-2, a Ca²⁺-specific fluorophore. Protein kinase A maximally inhibited the rate of IP₃-mediated Ca²⁺ release by approximately 30% at saturating IP₃ (10 μM). This inhibition was eliminated by pretreatment with a specific kinase inhibitor peptide. Partial purification of the platelet IP3 receptor showed that both endogenous kinases and added A kinase directly phosphorylate the receptor. Since the IP3 receptor is phosphorylated in the absence of added kinase, the observed inhibition (30%) by protein kinase A does not represent the maximal effect of phosphorylation.

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Cyclic AMP-dependent phosphorylation of the inositol-1,4,5-trisphosphate receptor inhibits Ca2+ release from platelet membranes

Abstract

Trends Biochem. Sci

Throm. Res

Biochim. Biophys. Acta

Biochim. Biophys. Acta

Biochim. Biophys. Acta

J. Biol. Chem

J. Biol. Chem

Meth. Enzymol

J. Biol. Chem

Biochem. Biophys. Res. Comm

Biochem. J

Cyclic AMP-dependent phosphorylation of the inositol-1,4,5-trisphosphate receptor inhibits Ca²⁺ release from platelet membranes