Dual regulation of phospholipase D1 by protein kinase C alpha in vivo.
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| Abstract |
The regulation of phospholipase D1 (PLD1), which has been shown to be activated by protein kinase C (PKC) alpha, was investigated in the human melanoma cell lines. In G361 cell line, which lacks PKCalpha, 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced PLD activation was potentiated by introducing PKCalpha by the adenovirus vector. The kinase-negative PKCalpha elevated TPA-induced PLD activity less significantly than the wild type. A PKC specific inhibitor GF109203X lowered PLD activation in the cells expressing PKCalpha, but did not prevent PLD potentiation induced by the kinase-negative PKCalpha. Expression of PKCbetaII and the kinase-negative PKCbetaII enhanced TPA-stimulated PLD activity moderately in MeWo cell line, in which PKCbetaII is absent. Furthermore, the TPA treatment increased the association of PKCalpha, PKCbetaII, and their kinase-negative mutants with PLD1 in melanoma cells. These results indicate that PLD1 is dually regulated through phosphorylation as well as through the protein-protein interaction by PKCalpha, and probably by PKCbetaII, in vivo.
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| Authors | Masahiro Oka, Tomohiro Hitomi, Taro Okada, Shun-ichi Nakamura Si, Hiroshi Nagai, Motoi Ohba, Toshio Kuroki, Ushio Kikkawa, Masamitsu Ichihashi |
| Journal | Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 294 Issue 5 Pg. 1109-13 (Jun 28 2002) ISSN: 0006-291X [Print] United States |
| PMID | 12074591 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't) |
| Chemical References |
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