Abstract
Cyclooxygenase (Cox) (E.C. 1.14.99.1) is a rate-limiting enzyme in the biosynthesis of prostaglandins and thromboxanes, collectively known as prostanoids (PG) (1). PG synthesis may be regulated by irreversible self-inactivation of Cox, whereby the enzyme only forms a limited amount of product, estimated to be 1500 moles product/mole enzyme (2). The self-inactivated Cox is rapidly degraded by proteases (3). Thus, the half-life of Cox is short, estimated to be in the order of a few minutes in vitro as well as in vivo Furthermore, cyclooxygenase enzyme levels are modulated by pro-and anti-inflammatory mediators. Many growth factors and cytokines induce PG synthesis by inducing the de novo synthesis of Cox protein (4,5,6,7). In contrast, the anti-inflammatory glucocorticoids such as dexamethasone (dex) inhibit the synthesis of Cox activity (8) and protein synthesis (9).
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Hla, T. (1991). Regulation of Cyclooxygenase Gene Expression in Vascular Endothelial Cells. In: Bailey, J.M. (eds) Prostaglandins, Leukotrienes, Lipoxins, and PAF. GWUMC Department of Biochemistry Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4899-0727-1_6
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