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Am J Physiol Lung Cell Mol Physiol 273: L1007-L1012, 1997;
1040-0605/97 $5.00
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AJP - Lung Cellular and Molecular Physiology, Vol 273, Issue 5 1007-L1012, Copyright © 1997 by American Physiological Society

ARTICLES

Stimulation of protein kinase C activity by tumor necrosis factor-alpha in bovine bronchial epithelial cells

T. A. Wyatt, H. Ito, T. J. Veys and J. R. Spurzem
Research Service, Department of Veterans Affairs Medical Center, Omaha, Nebraska 68105, USA.

Bronchial epithelial cell migration, attachment, and proliferation are important processes in response to airway injury. We have shown that tumor necrosis factor (TNF)-alpha stimulates the migration of bovine bronchial epithelial cells (BBEC) in vitro. We hypothesized that protein kinase C (PKC) may be one of the intracellular signaling mediators of TNF-alpha in BBEC. In this study, we have identified multiple PKC isoforms in BBEC and measured total cellular PKC activity. Polyclonal antibodies to the PKC-alpha, -beta 2, -delta, and -epsilon isoforms recognized protein bands around 80-90 kDa. BBEC primary cultures treated with either 500 U/ml TNF-alpha for 2-4 h or 100 ng/ml 12-O-tetradecanoylphorbol 13-acetate for 15 min resulted in three-to fivefold increases in PKC activity in the particulate fractions of crude cell lysates. This activity was inhibited by 1 microM calphostin C or 10 microM H-7. Similarly, TNF-alpha-stimulated BBEC migration was reduced at least twofold in the presence of H-7 or calphostin C. These studies suggest that the activation of PKC is necessary for TNF-alpha-stimulated BBEC migration.


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