Apigenin and LY294002 prolong EGF‐stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation

FEBS Letters

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