PMID: 8603100Mar 27, 1996Paper

Inhibition of PDGF-induced phospholipase C activation by herbimycin A

Biochimica Et Biophysica Acta
B Y KimJ S Ahn

Abstract

Herbimycin A, an inhibitor of protein tyrosine kinases, dose-dependently reduced PDGF-induced inositol phosphates (IPt) accumulation without effect on phosphatidylethanol (PEt) formation in PLC-gamma 1-overexpressing NIH 3T3 (NIH 3T3 gamma 1) cells. The compound also reduced tyrosine phosphorylations of some proteins including PLC-gamma 1 in response to PDGF. On the other hand, phorbol 12-myristate 13-acetate (PMA)-induced phospholipase D (PLD) activation was reduced by herbimycin A in the cells, indicating that the pathways for PLD activation by PDGF and PMA are different from each other. Also, these results suggest that PLC-gamma 1 activation is not always an upstream event for PLD activation and that tyrosine phosphorylation of one or more proteins not affected by herbimycin A should be indispensable for PLD activation in PDGF-stimulated NIH 3T3 gamma 1 cells.

References

Sep 28, 1990·Biochemical and Biophysical Research Communications·Y Z CaoA M Mastro
Mar 15, 1994·Biochemical and Biophysical Research Communications·T KumadaY Nozawa
May 1, 1993·Molecular Biology of the Cell·G L SchievenJ A Ledbetter
Apr 1, 1993·Proceedings of the National Academy of Sciences of the United States of America·D Mangoura, G Dawson

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