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Apigenin and LY294002 prolong EGF‐stimulated ERK1/2 activation in PC12 cells but are unable to induce full differentiation
Author(s) -
Llorens Franc,
Garcia Lourdes,
Itarte Emilio,
Gómez Néstor
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)03252-5
Subject(s) - wortmannin , phosphorylation , apigenin , ly294002 , epidermal growth factor , kinase , microbiology and biotechnology , chemistry , nerve growth factor , cancer research , endocrinology , biology , phosphatidylinositol , biochemistry , receptor , antioxidant , flavonoid
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.