PMID: 9194574May 27, 1997Paper

Dissociation of tyrosine phosphorylation and activation of phosphoinositide phospholipase C induced by the protein kinase C inhibitor Ro-31-8220 in Swiss 3T3 cells treated with platelet-derived growth factor

Biochimica Et Biophysica Acta
E J YeoJ H Exton

Abstract

Platelet-derived growth factor (PDGF) stimulates the hydrolysis of phosphatidylinositol 4,5-bisphosphate (Ptd InsP2) via phospholipase C-gamma1 (PLC-gamma1) in Swiss 3T3 cells. Treatment of cells with the protein kinase C (PKC) inhibitor Ro-31-8220 greatly decreased PDGF-induced tyrosine phosphorylation of PLC-gamma1, but paradoxically enhanced the production of inositol phosphates (InsPs). The inhibitor also caused an increase of PDGF receptor tyrosine phosphorylation at later times. The changes in phosphorylation of the receptor were correlated with alterations in PLC-gamma1 translocation to the particulate fraction. Thus, although activation of PLC-gamma1 was associated with phosphorylation of the receptor and translocation of the enzyme to the particulate fraction, it was dissociated from its tyrosine phosphorylation. A non-receptor-associated, cytosolic tyrosine kinase also was found to phosphorylate PLC-gamma1 in a PDGF-dependent manner, but was not inhibited by Ro-31-8220 in vitro. PKC depletion by phorbol ester treatment decreased the tyrosine phosphorylation of PLC-gamma1 induced by PDGF and slowed the translocation of PLC-gamma1, but Ro-31-8220 produced further effects. The effect of Ro-31-8220 to enhance the producti...Continue Reading

References

Dec 18, 1989·FEBS Letters·P D DavisS E Wilkinson
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Citations

Sep 18, 1998·Biochimica Et Biophysica Acta·C H HeldinL Rönnstrand
Aug 11, 2011·PloS One·Marta Vázquez-CedeiraPedro A Lazo
Sep 18, 2007·Cellular Signalling·Edith Browaeys-PolyKatia Cailliau

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