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Titolo:
Requirement of Syk-phospholipase C-gamma 2 pathway for phorbol ester-induced phospholipase D activation in DT40 cells
Autore:
Hitomi, T; Yanagi, S; Inatome, R; Ding, J; Takano, T; Yamamura, H;
Indirizzi:
Kobe Univ, Sch Med, Dept Biochem, Chuo Ku, Kobe, Hyogo 6500017, Japan KobeUniv Kobe Hyogo Japan 6500017 m, Chuo Ku, Kobe, Hyogo 6500017, Japan
Titolo Testata:
GENES TO CELLS
fascicolo: 5, volume: 6, anno: 2001,
pagine: 475 - 485
SICI:
1356-9597(200105)6:5<475:ROSC2P>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; TYROSINE-PHOSPHORYLATION; GROWTH-FACTOR; STIMULATION; MECHANISMS; CA2+; AUTOPHOSPHORYLATION; INVOLVEMENT; MEMBRANE; ISOFORMS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamura, H Kobe Univ, Sch Med, Dept Biochem, Chuo Ku, Kobe, Hyogo 6500017, Japan Kobe Univ Kobe Hyogo Japan 6500017 Kobe, Hyogo 6500017, Japan
Citazione:
T. Hitomi et al., "Requirement of Syk-phospholipase C-gamma 2 pathway for phorbol ester-induced phospholipase D activation in DT40 cells", GENES CELLS, 6(5), 2001, pp. 475-485

Abstract

Background: Treatment 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. Results: TPA-induced PLD activation was remarkably reduced in both Syk dominant negative mutant K562 cells and Syk deficient DT40 B cells. Mutationalanalysis further indicated that two major autophosphorylation sites (Tyr-518 and Tyr-519) of Syk are critical for PLD activation. Similarly, TPA-induced PLD activation was reduced in Btk deficient cells, but unaffected in Lyn deficient cells. Finally, in cells deficient in the PLC-gamma2, one of the phosphorylated substrates regulated by Syk and Btk, TPA-induced PLD activation, as well as phosphatidylinositol 4,5-bisphosphate (PIP2) hydrolysis was remarkably reduced. Conclusions: We demonstrated that the Syk, Btk and PLC-gamma2 pathways arerequired for TPA-induced PLD activation in DT40 cells.

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Documento generato il 28/03/20 alle ore 13:42:11