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Cyclooxygenases: structural, cellular, and molecular biology.
This review examines how the structures of these enzymes relate mechanistically to cyclooxygenase and peroxidase catalysis, and how differences in the structure of PGHS-2 confer on this isozyme differential sensitivity to COX-2 inhibitors.
Prostaglandin Endoperoxide H Synthases (Cyclooxygenases)-1 and −2*
This review compares and contrast PGHS-1 and -2 in the context of the regulation of expression of the two enzymes, the mechanisms of enzyme catalysis, and the biological significance of having two PGHSs.
Differential inhibition of prostaglandin endoperoxide synthase (cyclooxygenase) isozymes by aspirin and other non-steroidal anti-inflammatory drugs.
Prostaglandin endoperoxide H synthases-1 and -2.
Prostaglandin endoperoxide synthase: regulation of enzyme expression.
- D. Dewitt
- BiologyBiochimica et biophysica acta
- 8 May 1991
Prostaglandin and thromboxane biosynthesis.
Characterization of inducible cyclooxygenase in rat brain
This study used Western blot analysis and immunohistochemistry to describe the biochemical characterization and anatomical distribution of the second, mitogen‐inducible form of this enzyme, COX 2 in the rat brain.
Primary structure of prostaglandin G/H synthase from sheep vesicular gland determined from the complementary DNA sequence.
The availability of a full-length cDNA clone coding for prostaglandin G/H synthase should facilitate studies of the regulation of expression of this enzyme and the structural features important for catalysis and for interaction with anti-inflammatory drugs.
Intravenous lipopolysaccharide induces cyclooxygenase 2‐like immunoreactivity in rat brain perivascular microglia and meningeal macrophages
It is reported that intravenous lipopolysaccharide (LPS or endotoxin) induces cyclooxygenase 2‐like immunoreactivity in cells closely associated with brain blood vessels and in cells in the meninges, suggesting that perivascular microglia and meningeal macrophages throughout the brain may be the cellular source of prostaglandins following systemic immune challenge.
Differential inhibition of human prostaglandin endoperoxide H synthases-1 and -2 by nonsteroidal anti-inflammatory drugs.
- O. Laneuville, D. Breuer, D. Dewitt, T. Hla, C. Funk, W. Smith
- Biology, MedicineThe Journal of pharmacology and experimental…
- 1 November 1994
An in vitro expression system for accurate kinetic analyses of the inhibition of the human prostaglandin H synthase isozymes by nonsteroidal anti-inflammatory drugs (NSAIDs) indicates that neither measurements of affinities of NSAIDs for hPGHS-2 conducted in vitro with 10 microM arachidonate nor measurements of time-dependent inhibition of hPG HS-2 always predict whether a compound has anti- inflammatory activity in vivo.