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J Biol Chem, Vol. 274, Issue 39, 27562-27566, September 24, 1999

Galpha 13 Stimulates Rho-dependent Activation of the Cyclooxygenase-2 Promoter

Lee W. Slice, John H. Walsh, and Enrique Rozengurt

From the Division of Digestive Diseases, Department of Medicine, CURE, Digestive Diseases Research Center, and Molecular Biology Institute, University of California, Los Angeles, California 90095

Cyclooxygenase-2 (COX-2) gene expression is rapidly increased by cytokines, tumor promoters, and growth factors and is markedly enhanced in various cancer cells. Here, we examine the regulation of COX-2 promoter activity by alpha  subunits of heterotrimeric G proteins in NIH 3T3 cells. Using a transient transfection assay with a reporter vector in which the murine COX-2 promoter drives the production of luciferase and expression vectors encoding for alpha  subunits of G-proteins, we show that overexpression of wild type and constitutively active Galpha 13 and Galpha q induced transcription from the COX-2 promoter. The highest level of induced luciferase activity (5.8-fold) occurred in cells expressing the constitutively active Galpha 13(Q226L). We also show that expression of a constitutively active mutant of Rho (RhoQ63L) also induced transcription from the COX-2 promoter. Co-expression of Clostridium botulinum C3 toxin specifically blocked induction of the COX-2 promoter by either Galpha 13Q226L or RhoQ63L but did not prevent the activation of this promoter by Ras, Rac, v-src, or forskolin. We conclude that Galpha 13 signals through a Rho-dependent pathway leading to activation of the COX-2 promoter. This pathway is not inhibited by either cytochalasin D, which disrupts actin filament organization, or genistein, a broad spectrum tyrosine kinase inhibitor, indicating a bifurcation of the signaling pathway used by Galpha 13/Rho to induce COX-2 expression from that used to induce stress fiber formation and tyrosine phosphorylation of focal adhesion proteins.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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