Results 141 to 150 of about 2,860 (168)
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Prostaglandin endoperoxide synthase isozymes
1997Abstract PGH synthases catalyze the initial reaction common to the formation of prostanoids and are the target sites for most nonsteroidal anti-inflammatory drugs (NSAIDs). Until the recent discovery of a second PGH synthase isozyme (PGH synthase-2; PGHS-2), it was thought that NSAIDs acted by inhibiting a single enzyme, now referred to as PGH ...
William L. Smith, David L. DeWitt
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Inhibition of lipoxygenase and prostaglandin endoperoxide synthase by anacardic acids
Biochemical and Biophysical Research Communications, 1991C22:1 omega 5-anacardic acid was found to be a good inhibitor of both potato lipoxygenase and ovine prostaglandin endoperoxide synthase with approximate IC50's of 6 and 27 microM, respectively. Very similar inhibition was seen with the crude exudate, rich in omega 5-anacardic acids, from glandular trichomes of an arthropod-resistant strain of geranium,
Ellen Heininger+8 more
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Immunocytochemical localization of prostaglandin endoperoxide synthase in the bovine intestine
Histochemistry, 1993The localization of prostaglandin (PG) endoperoxide synthase in bovine intestine was examined immunocytochemically with polyclonal antibody raised against PG endoperoxide synthase purified from bovine seminal glands. The most intense positive staining reaction for the enzyme was present in mast cells.
T. Suzuki+6 more
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Expression of prostaglandin endoperoxide synthase-1 in a baculovirus system
Biochemical and Biophysical Research Communications, 1992A cDNA coding for ovine prostaglandin endoperoxide (PGH) synthase-1 was used to construct a recombinant baculovirus which was expressed in Spodoptera frugiperda (Sf9) insect cells. Two proteins reactive with anti-PGH synthase antibody were produced. A larger protein (Mr = 72,000) coelectrophoresed with native enzyme; a smaller, more abundant protein ...
William L. Smith, Teruhiko Shimokawa
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Localization of prostaglandin endoperoxide synthase in the human corpus luteum
Human Reproduction, 1990Prostaglandins have been implicated in both maintenance and luteolysis of the primate corpus luteum. Central to the production of prostaglandins is the enzyme prostaglandin endoperoxide synthase (PGHS). In the present study, we identified the cell types which contain PGHS in 44 human corpora lutea, using immunoperoxidase staining techniques.
Martin R. Clark+3 more
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Inactivation of prostaglandin endoperoxide synthase by acylating derivatives of indomethacin
Biochemistry, 1993Derivatives of the potent antiinflammatory agent and cyclooxygenase inhibitor indomethacin were synthesized in which the carboxylic acid moiety was converted into reactive acylating agents. Indomethacin imidazole (indomethacin-IM) and indomethacin N-hydroxysuccinimide (indomethacin-NHS) inactivated both the cyclooxygenase and peroxidase activities when
Isabelle Wells, Lawrence J. Marnett
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The structures of prostaglandin endoperoxide H synthases-1 and -2
Prostaglandins & 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.
David L. DeWitt+2 more
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Prostaglandins, 1986
Prostaglandin endoperoxide synthase (i.e. cyclooxygenase; PGH synthase) and prostacyclin synthase (PGI synthase) were quantitated with specific immunoradiometric assays in microsomes from human placentae (n = 20) obtained from 7 up to 17 weeks of gestation.
G. Klok+2 more
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Prostaglandin endoperoxide synthase (i.e. cyclooxygenase; PGH synthase) and prostacyclin synthase (PGI synthase) were quantitated with specific immunoradiometric assays in microsomes from human placentae (n = 20) obtained from 7 up to 17 weeks of gestation.
G. Klok+2 more
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Characterization of a novel prostaglandin endoperoxide H synthase-1 transcript and examination of prostaglandin endoperoxide H synthase-1 expression. [PDF]
The prostaglandin endoperoxide H synthase (PGHS) enzyme plays a pivotal role in the prostanoid biosynthetic pathway because it catalyzes the formation of prostaglandin H2 (PGH2), the common precursor for prostanoids. The object of my research is to characterize a novel PGHS transcript and to examine the mechanisms that regulate PGHS-1 gene expression ...
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BJOG: An International Journal of Obstetrics & Gynaecology, 1986
Summary. Prostacyclin (PGI2) synthase and prostaglandin endoperoxide synthase (cyclo‐oxygenase; PGH synthase) were measured with specific immunoradiometric assays in myometrial microsomes from different areas of a primigravid uterus at 34 weeks gestation. PGH synthase concentrations increased significantly from fundus toward lower segment (P <0·005)
P. Moonen, Marc J. N. C. Keirse, G. Klok
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Summary. Prostacyclin (PGI2) synthase and prostaglandin endoperoxide synthase (cyclo‐oxygenase; PGH synthase) were measured with specific immunoradiometric assays in myometrial microsomes from different areas of a primigravid uterus at 34 weeks gestation. PGH synthase concentrations increased significantly from fundus toward lower segment (P <0·005)
P. Moonen, Marc J. N. C. Keirse, G. Klok
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