Protein kinase C is differentially regulated by thrombin, insulin, and epidermal growth factor in human mammary tumor cells

The exposure of serum-deprived mammary tumor cells MCF-7 and T-47D to insulin, thrombin, and epidermal growth factor (EGF) resulted in dramatic modifications in the activity and in the translocation capacity of protein kinase C from cytosol to membrane fractions. Insulin induces a 600% activation of...

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Autores principales: Gomez, M.L., Medrano, E.E., Cafferatta, E.G.A., Tellez-Inon, M.T.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_00144827_v175_n1_p74_Gomez
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Sumario:The exposure of serum-deprived mammary tumor cells MCF-7 and T-47D to insulin, thrombin, and epidermal growth factor (EGF) resulted in dramatic modifications in the activity and in the translocation capacity of protein kinase C from cytosol to membrane fractions. Insulin induces a 600% activation of the enzyme after 5 h of exposure to the hormone in MCF-7 cells; thrombin either activates (200% in MCF-7) or down-regulates (in T-47D), and EGF exerts only a moderate effect. Thus, the growth factors studied modulate differentially the protein kinase C activity in human mammary tumor cells. The physiological significance of the results obtained are discussed in terms of the growth response elicited by insulin, thrombin, and EGF. © 1988.