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1 Department of Medicine, School of Medicine, University of California, CURE: Digestive Diseases Research Center and Molecular Biology Institute, Los Angeles, CA, USA
* To whom correspondence should be addressed. E-mail: erozengurt{at}mednet.ucla.edu.
Protein kinase C (PKC), a major target for the tumor promoting phorbol esters, has been implicated in the signal transduction pathways that mediate important functions in intestinal epithelial cells including proliferation and carcinogenesis. Using IEC-18 cells arrested in G0/G1, addition of phorbol esters resulted in a modest increase in [3H]-thymidine incorporation as well as a slight shift towards S and G2/M phase of the cell cycle, whereas the combination of EGF and PDB synergistically stimulated DNA synthesis. To investigate the effects of receptor-mediated PKC activation on mitogenesis, we demonstrated that Ang II induced ERK activation, a response completely blocked by pretreatment with MEK inhibitors or specific PKC inhibitors. Furthermore, Ang II stimulated an over 3-fold increase in [3H]-thymidine incorporation, which was corroborated by flow cytometric analysis of the cell cycle to levels comparable to that achieved by combination of EGF and PDB. Taken together, our results indicate that receptor-mediated PKC activation, as induced by Ang II, transduces mitogenic signals leading to DNA synthesis and cell proliferation in IEC-18 cells.
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