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Vol. 57, Issue 1, 36-43, January 2000

Involvement of Protein Kinase C-gamma in IL-1beta -Induced Cyclooxygenase-2 Expression in Human Pulmonary Epithelial Cells

Chien-Huang Lin, Sheng-Yuan Sheu, Horng-Mo Lee, Yuan-Soon Ho, Wen-Sen Lee, Wun-Chang Ko, and Joen-Rong Sheu

Graduate Institutes of Biomedical Technology (C.-H.L., H.-M.L., Y.-S.H.) and Medical Sciences (S.-Y.S., W.-S.L., W.-C.K., J.-R.S.), Taipei Medical College, Taipei, Taiwan

The signaling pathway of protein kinase C (PKC) is known to play a role in mediating the action of various cytokines. Here we examined the signal transduction pathway of PKC activation and the role of PKC isoforms in interleukin-1beta (IL-1beta )-mediated cyclooxygenase-2 (COX-2) expression in human pulmonary epithelial cell line (A549). The tyrosine kinase inhibitors (genistein and tyrphostin AG126) and phosphatidylcholine-phospholipase C inhibitor (D-609) prevented IL-1beta -induced prostaglandin E2 (PGE2) release and COX-2 expression, whereas U-73122 (a phosphatidylinositol-phospholipase C inhibitor) and propranolol (a phosphatidate phosphohydrolase inhibitor) had no effect. The PKC inhibitors (Go 6976 and Ro 31-8220) and NF-kappa B inhibitor, pyrrolidine dithiocarbamate, also attenuated IL-1beta -induced PGE2 release and COX-2 expression. Western blot analysis using PKC isoenzyme-specific antibodies indicated that A549 cells expressed PKC-alpha , -gamma , -iota , -lambda , -zeta , and -µ. IL-1beta caused the translocation of PKC-gamma but not other isoforms from cytosol to the membrane fraction. Moreover, the translocation of PKC-gamma was inhibited by genistein or D-609, but not by U-73122. IL-1beta caused the translocation of p65 NF-kappa B from cytosol to the nucleus as well as the degradation of Ikappa B-alpha in cytosol. Furthermore, the translocation of p65 NF-kappa B was inhibited by genistein, Go 6976, Ro 31-8220, or pyrrolidine dithiocarbamate. These results indicate that in human pulmonary epithelial cells, IL-1beta might activate phosphatidylcholine-phospholipase C through an upstream tyrosine phosphorylation to elicit PKC activation, which in turn initiates NF-kappa B activation, and finally induces COX-2 expression and PGE2 release. Of the PKC isoforms present in A549 cells, only activation of PKC-gamma is involved in regulating IL-1beta -induced responses.

Copyright © 2000 by The American Society for Pharmacology and Experimental Therapeutics


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