Results 151 to 160 of about 2,860 (168)

Pharmacology of Prostaglandin Endoperoxide Synthase Isozymes‐1 and‐2^a

Annals of the New York Academy of Sciences, 1994
It is now that there are two isozymes of prostaglandin endoperoxide (PGH) synthase (cyclooxygenase) called PGH synthase-1 and -2 or COX I and II. Both isozymes catalyze the conversion of arachidonate to PGH2, the committed step in the formation of both prostacyclin and thromboxane A2. PGH synthase-1 is present in platelets and endothelial cells whereas
William L. Smith, Elizabeth A. Meade, David L. Dwitt   +2 more
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Kinetic studies on the conversion of prostaglandin endoperoxide PGH2 by thromboxane synthase

Prostaglandins, 1978
We have investigated the time course of formation of thromboxane A2, thromboxane B2, and the C-17 hydroxy fatty acid, HHT, from arachidonic acid in a washed human platelet suspension. Our results indicate that HHT is not a breakdown product of thromboxane A2, but rather thromboxane A2 decomposes exclusively into thromboxane B2.
D.J. Crutchley, B.E. Tainer, Marshall W. Anderson, Thomas E. Eling   +3 more
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Rapid Inactivation of Prostaglandin Endoperoxide Synthases by N-(Carboxyalkyl)maleimides

Biochemistry, 1994
N-(Carboxyalkyl)maleimides were synthesized as potential inhibitors of prostaglandin endoperoxide synthase (PGHS). Inactivation of the cyclooxygenase and peroxidase activities of PGHS occurred in a biphasic manner with extremely rapid inactivation followed by slow, time-dependent inactivation.
Amit S. Kalgutkar, Lawrence J. Marnett
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Activation of 2-Aminofluorene by Prostaglandin Endoperoxide H Synthase 2

Biochemical and Biophysical Research Communications, 1995
Prostaglandin endoperoxide H synthase is the key enzyme in the conversion of arachidonic acid to tissue prostanoids. Two isoforms of prostaglandin endoperoxide H synthase have been identified: PHS-1 is constitutively expressed in most tissues under normal physiological conditions and PHS-2 is expressed in response to inflammatory agents, tumor ...
Gerald N. Levy, Wendell W. Weber, Ying Liu   +2 more
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Prostaglandin Endoperoxide Synthases: Structure, Function, and Synthesis of Novel Lipid Signaling Molecules

2010
Prostanoids are involved in a wide range of biological processes including vascular function, wound healing, and inflammation. Prostaglandin endoperoxide synthases (PGHSs) generate the central precursor molecule for all prostanoids. New insights into the regulation of PGHS activity and isoform-specific functions in cells and in vivo have been gained ...
Lawrence J. Marnett, Melissa V. Turman
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Localization of prostaglandin endoperoxide synthase in neurons and glia in monkey brain

Brain Research, 1991
The localization of prostaglandin endoperoxide synthase in monkey brain was investigated by the immunoperoxidase method using the monoclonal antibody (PES-7) raised against the enzyme purified from bovine seminal vesicle. The frozen sections with 30-microns thickness were employed after the brain was fixed with perfusion of 2% paraformaldehyde in ...
Yasuyoshi Watanabe, Shozo Yamamoto, Osamu Sugimoto, Hiroaki Ehara, Shogo Tsubokura, Hirovuki Kagamiyama, Osamu Hayaishi, Kazuvuki Imamura   +7 more
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Conversions of prostaglandin endoperoxides by prostacyclin synthase from pig aorta

Prostaglandins, 1980
Partially purified prostacyclin synthase from pig aorta converted the prostaglandin (PG) endoperoxide PGH2 to prostacyclin (PGI2), and PGH1 to 12-hydroxy-8,10-heptadecadienoic acid (HHD). Both reactions were inhibited by 15-hydroperoxy-5,8,11,13-eicosatetraenoic acid (15-HP) in a dose-dependent rashion.
Paulina Wlodawer, Sven Hammarström
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Characterization of prostaglandin endoperoxide synthase from a human cell line

Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, 1986
Prostaglandin endoperoxide synthase has been purified from the recently established human lung tumor cell line, Lu-65. By gel filtration, the purified enzyme migrated with a relative molecular weight of 115,000, unlike the ovine enzyme, which migrated at 155,000.
Noreen J. Hickok, Gladys Chin, Richard S. Bookman   +2 more
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Amino Acids Essential to Catalysis by Prostaglandin Endoperoxide Synthase

1991
The recent availability of cDNAs containing the entire coding region of prostaglandin endoperoxide (PGH) synthase (1–3) and the development of constructs which can be used for expressing the enzyme in vitro (4–6) permits the use of site-directed mutagenesis to characterize this enzyme (4–7).
Teruhiko Shimokawa, William L. Smith
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Inactivation of Prostaglandin Endoperoxide Synthase (PGHS) by N-(Substituted)Maleimides

1997
Prostaglandin endoperoxide synthase (PGHS, EC 1.14.99.1) catalyzes the first two steps of prostaglandin biosynthesis.1 Its cyclooxygenase activity oxygenates arachidonic acid to form PGG2; the peroxidase activity of the enzyme then reduces PGG2 in the presence of a reducing substrate to the corresponding alcohol PGH2.2,3 The cyclooxygenase activity is ...
Amit S. Kalgutkar, Brenda C. Crews, Lawrence J. Marnett   +2 more
openaire   +3 more sources