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KMID : 0620920010330040303
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Experimental & Molecular Medicine
2001 Volume.33 No. 4 p.303 ~ p.309
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D609-sensitive tyrosine phosphorylation is involved in Fas-mediated phospholipase D activation
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Joong Soo Han/Jong Gon Kim
In Cheol Shin/Ki Sung Lee/Joong Soo Han
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Abstract
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Both Fas and PMA can activate phospholipase D via activation of protein kinase Cβ in A20 cells. Phospholipase D activity was increased 4 fold in the presence of Fas and 2.5 fold in the presence of PMA. The possible involvement of tyrosine phosphorylation in Fas-induced activation of phospholipase D was investigated. In five minute after Fas cross-linking, there was a prominent increase in tyrosine phosphorylated proteins, and it was completely inhibited by D609, a specific inhibitor of phosphatidylcholine-specific phospholipase C (PC-PLC). A tyrosine kinase inhibitor, genistein, can partially inhibit Fas-induced phospholipase D activation. There were no effects of genistein on Fas-induced activation of PC-PLC and protein kinase C. These results strongly indicate that tyrosine phosphorylation may in part account for the increase in phospholipase D activity by Fas cross-linking and D609 can block not only PC-PLC activity but also tyrosine phosphorylation involved in Fas-induced phospholipase D activation.
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