Results 141 to 150 of about 2,860 (168)
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Prostaglandin endoperoxide synthase isozymes

1997
Abstract 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
openaire   +2 more sources

Inhibition of lipoxygenase and prostaglandin endoperoxide synthase by anacardic acids

Biochemical and Biophysical Research Communications, 1991
C22:1 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
openaire   +3 more sources

Immunocytochemical localization of prostaglandin endoperoxide synthase in the bovine intestine

Histochemistry, 1993
The 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
openaire   +3 more sources

Expression of prostaglandin endoperoxide synthase-1 in a baculovirus system

Biochemical and Biophysical Research Communications, 1992
A 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
openaire   +3 more sources

Localization of prostaglandin endoperoxide synthase in the human corpus luteum

Human Reproduction, 1990
Prostaglandins 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
openaire   +3 more sources

Inactivation of prostaglandin endoperoxide synthase by acylating derivatives of indomethacin

Biochemistry, 1993
Derivatives 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
openaire   +3 more sources

The structures of prostaglandin endoperoxide H synthases-1 and -2

Prostaglandins & Other Lipid Mediators, 2002
Despite 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
openaire   +3 more sources

Not prostacyclin synthase but prostaglandin endoperoxide synthase increases with human placental development

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
openaire   +3 more sources

Characterization of a novel prostaglandin endoperoxide H synthase-1 transcript and examination of prostaglandin endoperoxide H synthase-1 expression. [PDF]

open access: possible, 1999
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 ...
openaire   +2 more sources

Distribution of prostaglandin endoperoxide synthase and prostacyclin synthase in the late pregnant uterus

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
openaire   +3 more sources

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