FEBS Letters | |
Apigenin and LY294002 prolong EGF‐stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation | |
Itarte, Emilio1  Garcia, Lourdes1  Gómez, Néstor1  Llorens, Franc1  | |
[1] Departament de Bioquı́mica i Biologia Molecular, Unitats de Bioquı́mica de Ciències i de Veterinària, Universitat Autònoma de Barcelona, 08193-Bellaterra, Barcelona, Spain | |
关键词: Extracellular signal-regulated protein kinases 1/2; p90 ribosomal S6 kinase; Protein kinase B; Raf; Epidermal growth factor; Nerve growth factor; EGF; epidermal growth factor; ERK1/2; extracellular signal-regulated protein kinases 1/2; MAPK; mitogen-activated protein kinase; MEK; MAPK/ERK kinase; MBP; myelin basic protein; NGF; nerve growth factor; p90rsk; p90 ribosomal S6 kinase; PC12; rat pheochromocytoma cell line; PI3K; phosphoinositide 3-kinase; PKB; protein kinase B; RBD; Ras-binding domain of Raf-1; | |
DOI : 10.1016/S0014-5793(01)03252-5 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
In rat pheochromocytoma cell line (PC12) cells, initial epidermal growth factor (EGF)-stimulated extracellular signal-regulated protein kinases 1/2 (ERK1/2) phosphorylation was similar to that promoted by nerve growth factor (NGF), but declined rapidly. Pre-treatment with apigenin or LY294002 sustained EGF-stimulated ERK1/2 phosphorylation whereas wortmannin partially blocked initial ERK1/2 phosphorylation. Changes in ERK1/2 phosphorylation correlated with alterations in p90 ribosomal S6 kinase activity. Wortmannin, LY294002 and apigenin totally blocked growth factor-induced protein kinase B phosphorylation. However, none of them potentiated Raf activation, which was in fact decreased by LY290042 and wortmannin. The sustained EGF-induced ERK1/2 activation promoted by apigenin was not sufficient to commit PC12 cells to differentiate, which was achieved by stimulation with NGF, either alone or in the presence of apigenin.
【 授权许可】
Unknown
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