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HORMONES AND SIGNALING

ANG II stimulates PKC-dependent ERK activation, DNA synthesis, and cell division in intestinal epithelial cells

Department of Medicine, School of Medicine, CURE: Digestive Diseases Research Center and Molecular Biology Institute, University of California, Los Angeles, California 90095

Submitted 26 September 2002 ; accepted in final form 26 February 2003

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. With the use of IEC-18 cells arrested in G₀/G₁, addition of phorbol esters resulted in a modest increase in [³H]thymidine incorporation and a slight shift toward the S and G₂/M phases of the cell cycle, whereas the combination of EGF and phorbol 12,13-dibutyrate (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 mitogen/extracellular signal-regulated kinase inhibitors or specific PKC inhibitors. Furthermore, ANG II stimulated an over threefold increase in [³H]thymidine incorporation that was corroborated by flow cytometric analysis of the cell cycle to levels comparable to that achieved by the 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.

IEC-18 cells; mitogen-activated protein kinase; mitogen/extracellular signal-regulated kinase; phorbol ester; angiotensin II; protein kinase C; deoxyribonucleic acid

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