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Am J Physiol Cell Physiol 280: C701-C708, 2001;
0363-6143/01 $5.00
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Vol. 280, Issue 3, C701-C708, March 2001

Prostaglandin endoperoxide H synthase expression in human thyroid epithelial cells

Andrew G. Gianoukakis1,2, H. James Cao2, Timothy A. Jennings3, and Terry J. Smith1,2,4

Divisions of 1 Endocrinology and Metabolism and 2 Molecular and Cellular Medicine, Departments of Medicine, 3 Pathology, and 4 Biochemistry and Molecular Biology, Albany Medical College and Samuel S. Stratton Veterans Affairs Medical Center, Albany, New York 12208

KAT-50, an established human thyrocyte cell line, expresses constitutively high levels of prostaglandin endoperoxide H synthase-2 (PGHS-2), the inflammatory cyclooxygenase. Here, we examine primary human thyrocytes. We find that they, too, express PGHS-2 mRNA and protein under control culture conditions. A substantial fraction of the basal prostaglandin E2 (PGE2) produced by these cells can be inhibited by SC-58125 (5 µM), a PGHS-2-selective inhibitor. Interleukin (IL)-1beta (10 ng/ml) induces PGHS-2 expression and PGE2 production in primary thyrocytes. The induction of PGHS-2 and PGE2 synthesis by IL-1beta could be blocked by glucocorticoid treatment. Unlike KAT-50, most of the culture strains also express PGHS-1 protein. Our observations suggest that both cyclooxygenase isoforms may have functional roles in primary human thyroid epithelial cells, and PGHS-2 might predominate under basal and cytokine-activated culture conditions.

prostanoid; inflammation; cyclooxygenase


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R. Han and T. J. Smith
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
J. Biol. Chem., September 20, 2002; 277(39): 36897 - 36903.
[Abstract] [Full Text] [PDF]


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