Release of Ca2+ by Inositol 1,4,5-trisphosphate in Platelet Membrane Vesicles is Not Dependent on Cyclic AMP-dependent Protein Kinase

Overview

Journal Biochem J

Specialty Biochemistry

Date 1989 Feb 1

PMID 2784669

Citations 11

Authors

F ORourke

G B Zavoico

M B Feinstein

Affiliations

Soon will be listed here.

Abstract

In contrast with previous reports, it was found that membrane-protein phosphorylation by the catalytic subunit (CS) of cyclic AMP-dependent protein kinase had no effect on Ca2+ uptake into platelet membrane vesicles or on subsequent Ca2+ release by inositol 1,4,5-trisphosphate (IP3). Furthermore, IP-20, a highly potent synthetic peptide inhibitor of CS, which totally abolished membrane protein phosphorylation by endogenous or exogenous CS, also had no effect on either Ca2+ uptake or release by IP3. Commercial preparations of protein kinase inhibitor protein (PKI) usually had no effect, but one preparation partially inhibited Ca2+ uptake, which is attributable to the gross impurity of the commercial PKI preparation. IP3-induced release of Ca2+ was also unaffected by the absence of ATP from the medium, supporting the conclusion that Ca2+ release by IP3 does not require the phosphorylation of membrane protein.

Citing Articles

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Inhibition of inositol 1,4,5-trisphosphate-induced Ca2+ release by cAMP-dependent protein kinase in a living cell.

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Purification and characterization of the human type 1 Ins(1,4,5)P3 receptor from platelets and comparison with receptor subtypes in other normal and transformed blood cells.

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Ca2+ release by inositol 1,4,5-trisphosphate is blocked by the K(+)-channel blockers apamin and tetrapentylammonium ion, and a monoclonal antibody to a 63 kDa membrane protein: reversal of blockade by K+ ionophores nigericin and valinomycin and....

ORourke F, Soons K, Flaumenhauft R, WATRAS J, Matthews E, Feinstein M Biochem J. 1994; 300 ( Pt 3):673-83.

PMID: 8010949 PMC: 1138220. DOI: 10.1042/bj3000673.

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