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Prostaglandin endoperoxide synthases-1 and -2
Journal of Lipid Mediators and Cell Signalling, 1995Publisher Summary The chapter compares and contrasts the structural and kinetic properties of prostaglandin endoperoxide H synthase-1 (PGHS-1) and -2. It also discusses the description of the interactions of the two isozymes with nonsteroidal anti-inflammatory drugs (NSAIDs).
J C, Otto, W L, Smith
exaly +3 more sources
The enzymology of prostaglandin endoperoxide H synthases-1 and -2
Prostaglandins and Other Lipid Mediators, 2002We summarize the enzymological properties of prostaglandin endoperoxide H synthases (PGHs)-1 and -2, the enzymes that catalyze the committed step in prostaglandin biosynthesis. These isoenzymes are closely related structurally and mechanistically.
Inseok Song
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The structures of prostaglandin endoperoxide H synthases-1 and -2
Prostaglandins and Other Lipid Mediators, 2002Despite the marked differences in their physiological roles, the structures and catalytic functions of the prostaglandin H2 endoperoxide synthases-1 and -2 (PGHS-1 and -2) are almost completely identical. These integral membrane proteins catalyze the conversion of arachidonic acid to PGG2 and finally to PGH2.
Michael G Malkowski +2 more
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Prostaglandin endoperoxide synthase: why two isoforms?
American Journal of Physiology-Gastrointestinal and Liver Physiology, 1996 Prostaglandin endoperoxide synthase-1 [prostaglandin G/H synthase-1 (PGHS-1)] and PGHS-2 are key enzymes in the conversion of arachidonic acid to prostaglandins and other eicosanoids. We refer to these isoforms as cyclooxygenase-1 (COX-1) and COX-2 in this review.
C S, Williams, R N, DuBois
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European Journal of Pain, 2000 The analgesic drug tramadol has been shown to relieve pain in inflammatory conditions, to inhibit the development of experimental inflammation, and to reduce prostaglandin (PG)E 2 concentrations in the inflammatory exudate. In this
Angelo Sala
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Biochemical and Biophysical Research Communications, 1994
A Prostaglandin endoperoxide synthase isoenzyme was recently identified in several cell lines. Osteoblasts possess Prostaglandin endoperoxide synthase activity, but it is not known which isoenzymes are present in these cells. Our objective was to identify these isoenzymes in human osteoblasts. Resting cells in culture did not produce measurable amounts
A J, de Brum-Fernandes +7 more
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A Prostaglandin endoperoxide synthase isoenzyme was recently identified in several cell lines. Osteoblasts possess Prostaglandin endoperoxide synthase activity, but it is not known which isoenzymes are present in these cells. Our objective was to identify these isoenzymes in human osteoblasts. Resting cells in culture did not produce measurable amounts
A J, de Brum-Fernandes +7 more
openaire +2 more sources
Prostaglandin endoperoxide synthase: structure and catalysis
Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1991In this review, we describe the properties of PGH synthase, the enzyme which catalyzes the committed step in the synthesis of prostaglandins and thromboxane. We begin by presenting an overview of protanoid biosynthesis and the mechanism of action of these local hormones. We then describe the novel characteristics of the two distinct reactions catalyzed
W L, Smith, L J, Marnett
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Expression of prostaglandin endoperoxide synthase in rat brain
Molecular Brain Research, 1993Developmental and regional expression of prostaglandin endoperoxide synthase (PES) transcript was examined in the rat brain and in primary mixed cultures of neurons and glial cells from neonatal brain. Although the PES mRNA level in the brain was much lower than that in peripheral rat tissues such as lung, liver, spleen and kidney, a significant 3.0 kb
M, Kawasaki +3 more
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