Epidermal growth factor induces protein tyrosine phosphorylation and association of p190 with ras‐GTP‐ase activating protein in Caco‐2 cells

FEBS Letters

Migliaccio, Antimo²  Auricchio, Alberto¹  Castoria, Gabriella²  Bilancio, Antonio²  Domenico, Marina di² 

[1] Dipartimento di Pediatria, Facoltà di Medicina e Chirurgia, Università di Napoli Federico II, Via Pansini 5, 80131 Napoli, Italia;Istituto di Patologia Generale e Oncologia, Facoltà di Medicina e Chirurgia, II Università di Napoli, Largo S. Andrea delle Dame 2, 80138 Napoli, Italia

关键词: Signal transduction;    Tyrosine phosphorylation;    ras-GAP;    p190;    p62;    c-erb B2;    BIS;    N;    N′ methylene-bis-acrylamide;    EGF;    epidermal growth factor;    EGF-R;    EGF-Receptor;    SDS sodium dodecyl-sulphate;    PAGE;    polyacrylamide gel electrophoresis;    PBA;    phosphate-buffered saline;    PMSF phenyl-methyl-sulfonyl-fluoride;    ras-GAP;    ras-GTP-ase activating protein;    TEMED;    N;    N;    N′;    N′-tetramethyl-ethylene-diamine;    Tris;    Tris [hydroximethyl]-aminomethane;   

DOI  :  10.1016/0014-5793(94)00987-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Epidermal growth factor (EGF) modulates several functions of human enterocytes. We report that this growth factor induces strong tyrosine phosphorylation stimulation of its receptor and several putative substrates of the receptor intrinsic kinase including c-erb B2 in proliferating human colon carcinoma cells (Caco-2). In addition EGF induces stable association of the GTP-ase activating protein of p21^ras to the p190 protein and to a 62 mol.wt. tyrosine-phosphorylated protein. This association is probably consequent to EGF stimulation of protein tyrosine phosphorylation and could coordinate progression through cell cycle with polarity, cell—cell interactions and cell mobility.

【 授权许可】

Unknown