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  • Title: The myristoylated alanine-rich C-kinase substrate (MARCKS) is not required for mitogenic signalling via protein kinase C in cultured rat intestinal epithelial (RIE-1) cells.
    Author: Smith RD.
    Journal: Biochem Mol Biol Int; 1995 Apr; 35(5):1029-35. PubMed ID: 7549920.
    Abstract:
    Activation of protein kinase C (PKC) by angiotensin II or 12-O-tetradecanoylphorbol-13-acetate (TPA) was associated with a mitogenic response in RIE-1 rat intestinal epithelial cells. However, whereas in control experiments using Swiss 3T3 cells TPA stimulated phosphorylation of the major PKC substrate, MARCKS, the agent did not induce the phosphorylation of any protein with the electrophoretic mobility pattern of MARCKS in RIE-1 cells. However, TPA was able to activate PKC in RIE-1 cells since the agent reduced ('transmodulated') 125I-EGF binding to the cells. The failure of TPA to induce phosphorylation of MARCKS in RIE-1 cells was due to the lack of expression of MARCKS protein and mRNA by these cells. MARCKS is not therefore required for mitogenic signalling via PKC in RIE-1 cells.
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