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Originally published In Press as doi:10.1074/jbc.M206949200 on July 26, 2002

J. Biol. Chem., Vol. 277, Issue 39, 36897-36903, September 27, 2002
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Cytoplasmic Prostaglandin E2 Synthase Is Dominantly Expressed in Cultured KAT-50 Thyrocytes, Cells That Express Constitutive Prostaglandin-endoperoxide H Synthase-2
BASIS FOR LOW PROSTAGLANDIN E2 PRODUCTION*

Rui Han and Terry J. SmithDagger

From the Division of Molecular Medicine, Department of Medicine, Harbor-UCLA Medical Center, Torrance, California 90502 and the David Geffen School of Medicine at the University of California, Los Angeles, California 90095

The recent identification and cloning of two glutathione-dependent prostaglandin E2 synthase (PGES) genes has yielded important insights into the terminal step of PGE2 synthesis. These enzymes form efficient functional pairs with specific members of the prostaglandin-endoperoxide H synthase (PGHS) family. Microsomal PGES (mPGES) is inducible and works more efficiently with PGHS-2, the inflammatory cyclooxygenase, while the cytoplasmic isoform (cPGES) pairs functionally with PGHS-1, the cyclooxygenase that ordinarily exhibits constitutive expression. KAT-50, a well differentiated thyroid epithelial cell line, expresses high levels of PGHS-2 but surprisingly low levels of PGE2 when compared with human orbital fibroblasts. Moreover, PGHS-1 protein cannot be detected in KAT-50. We report here that KAT-50 cells express high basal levels of cPGES but mPGES mRNA and protein are undetectable. Thus, KAT-50 cells express the inefficient PGHS-2/cPGES pair, and this results in modest PGE2 production. The high levels of cPGES and the absence of mPGES expression result from dramatic differences in the activities of their respective gene promoters. When mPGES is expressed in KAT-50 by transiently transfecting the cells, PGE2 production is up-regulated substantially. These observations indicate that naturally occurring cells can express a suboptimal profile of PGHS and PGES isoforms, resulting in diminished levels of PGE2 generation.

* This work was supported in part by National Institutes of Health Grants EY08976 and EY11708.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom all correspondence should be addressed: Division of Molecular Medicine, Bldg. C-2, Harbor-UCLA Medical Center, 1124 West Carson St., Torrance, CA 90502. E-mail: tjsmith@ucla.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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