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pubmed-article:11380624pubmed:abstractTextTreatment of many cell types with phorbol esters stimulates phospholipase D (PLD) activity implying regulation of the enzyme by protein kinase C. Studies of the effects of several protein-tyrosine kinase (PTK) inhibitors have suggested that PTK(s) play some roles in the phorbol ester-induced PLD activation, but it remains unclear how and which PTK(s) is involved in this pathway. In this study, we investigated the roles of Syk and other PTKs for the phorbol esters, 12-O-tetradecanoylphorbol 13-acetate (TPA)-induced PLD activation in K562 and DT40 cells.lld:pubmed
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pubmed-article:11380624pubmed:articleTitleRequirement of Syk-phospholipase C-gamma2 pathway for phorbol ester-induced phospholipase D activation in DT40 cells.lld:pubmed
pubmed-article:11380624pubmed:affiliationDepartment of Biochemistry Kobe University School of Medicine, Chuo-ku, Kobe 650-0017, Japan.lld:pubmed
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pubmed-article:11380624pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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