Abstract
Prostaglandin H synthase (PGHS) catalyzes the conversion of arachidonate to PGG2, a key control step in prostanoid biosynthesis. Two isoforms of PGHS are known (Herschman, 1996). PGHS-1 is present at more or less constitutive levels in many cells, and has been assigned a housekeeping role. PGHS-2 is strongly induced by cytokines and mitogens in some cells, and is believed to play an important role in inflammatory processes. Induction of PGHS-2 in fibroblasts and macrophages is accompanied by large increases in arachidonate release and prostanoid synthesis (Reddy and Herschman, 1994). Inhibition of PGHS-2 expression blocked the mitogen-dependent increase in prostaglandin synthesis, but not the arachidonate release; the constitutive PGHS-1 remained in a latent form, unable to utilize the released arachidonate (Reddy and Herschman, 1994). Thus, cyclooxygenase catalysis by PGHS-1 and PGHS-2 is differentially controlled in these cells which have both isoforms.
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© 1996 Springer Science+Business Media New York
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Kulmacz, R.J., Chen, W., Wang, LH. (1996). Differential Control of Cyclooxygenase Catalysis in PGH Synthase Isoforms: Role of Hydroperoxide Initiator. In: Vanderhoek, J.Y. (eds) Frontiers in Bioactive Lipids. GWUMC Department of Biochemistry and Molecular Biology Annual Spring Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5875-0_14
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DOI: https://doi.org/10.1007/978-1-4615-5875-0_14
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