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- W2014569811 abstract "Early signalling events between protein kinase C (PKC) activation and lymphokine transcription were compared between phorbol ester-sensitive and -resistant EL4 cell lines which do or do not respond with interleukin 2 (IL2) production, respectively. The earliest event detected in the sensitive cell line was a dramatic increase in the tyrosine phosphorylation of an 85,000 Mr protein (p85; 30 s), followed by mobility shifts of raf-1, mitogen-activated protein kinase kinase (MEK), mitogen-activated protein (MAP) kinase, lck and ZAP-70 (within 5 min). In contrast, p85 was not detected in the resistant cell line and lck and raf-1 mobility shifts exhibited delayed kinetics. Both vanadate and okadaic acid blocked the phorbol ester-stimulated p85 tyrosine phosphorylation in the sensitive cell line, suggesting that a phosphatase activity downstream of PKC activation may be required for p85 tyrosine phosphorylation. Characterization of p85 and its regulation should help elucidate some of the earliest events in this PKC pathway." @default.
- W2014569811 created "2016-06-24" @default.
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- W2014569811 date "1995-01-01" @default.
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- W2014569811 title "Rapid tyrosine phosphorylation of an 85,000 Mr protein after phorbol ester stimulation of EL4 thymoma cells" @default.
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- W2014569811 doi "https://doi.org/10.1016/0898-6568(94)00068-m" @default.
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