Calcium free inositol (1,4,5)-trisphosphate stimulates protein kinase C dependent protein phosphorylation in nuclei isolated from mitogen-treated Swiss 3T3 cells

Biochemical and Biophysical Research Communications
A M MartelliL Cocco

Abstract

As a step towards the elucidation of the role played by nuclear polyphosphoinositides, we have investigated the effect of exogenous calcium free inositol (1,4,5)-trisphosphate on the in vitro phosphorylation of proteins in nuclei prepared from Swiss 3T3 cells treated with bombesin and insulin-like growth factor I. When present in combination with phosphatidylserine, inositol (1,4,5)-trisphosphate enhanced the phosphorylation of two nuclear proteins, Mr 21,000 and 31,000, as well as of exogenous histone H1, to the same extent as a combination of phosphatidylserine and diacylglycerol. Inositol (1,4,5)-trisphosphate alone had no effect. This stimulation could be abolished by the protein kinase C inhibitor sphingosine and by EGTA, while could be restored by a combination of phosphatidylserine and exogenous Ca+(+) ions. These results raise the possibility that inositol (1,4,5)-trisphosphate is capable of liberating Ca+(+) ions from a nuclear store thus stimulating protein kinase C activity.

References

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Citations

Jun 1, 1993·Journal of Cellular Biochemistry·A M SorensenD T Baran
Jan 1, 1992·Advances in Enzyme Regulation·N M MaraldiF A Manzoli
Jan 1, 1994·Advances in Enzyme Regulation·N M MaraldiF A Manzoli
Mar 1, 1993·Molecular and Cellular Endocrinology·R J KonradB A Wolf
Aug 14, 1992·Biochimica Et Biophysica Acta·O BachsE Carafoli
Apr 15, 2008·Trends in Endocrinology and Metabolism : TEM·A RevelliJ Tesarik
Nov 1, 1993·Journal of Dairy Science·N KatohA Yuasa
Aug 1, 1992·Seminars in Cell Biology·R F Irvine, N Divecha

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