Inhibition of PDGF-induced phospholipase C activation by herbimycin A

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Inhibition of PDGF-induced phospholipase C activation by herbimycin A
Bo Yeon Kim; Soon Cheol Ahn; Dae Ook Kang; Hack Ryong Ko; Won Keun Oh; Hyun Sun Lee; Tae Ick Mheen; Hyune Mo Rho; Jong Seog Ahn
Bibliographic Citation
Biochimica et Biophysica Acta-Molecular Cell Research, vol. 1311, no. 1, pp. 33-36
Publication Year
Herbimycin A, an inhibitor of protein tyrosine kinases, dose-dependently reduced PDGF-induced inositol phosphates (IF,) accumulation without effect on phosphatidylethanol (PEt) formation in PLC-γ-overexpressing NIH 3T3 (NIH 3T3γ1) cells. The compound also reduced tyrosine phosphorylations of some proteins including PLC-γ1 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-γ1 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 3T3γ1 cells.
herbimycin Aphospholipase Cγ1phospholipase Dplate-derived growth factor
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Ochang Branch Institute > Chemical Biology Research Center > 1. Journal Articles
Ochang Branch Institute > Natural Product Research Center > 1. Journal Articles
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