M. R. Panara

TL;DR: A model of human prostaglandin endoperoxide synthase-2 expression allowing the assessment of pharmacological inhibition in vitro and ex vivo was characterized and cyclooxygenase activity increased in parallel with the mass of a monocyte protein doublet analyzed by Western blot using antibodies directed against the carboxyl-terminal portion of human PGHS-2.

TL;DR: In this paper, the selectivity in vitro of various conventional nonsteroidal anti-inflammatory drugs (NSAIDs) and new anti inflammatory compounds (NS-398, L-745,337 and SC58125) in inhibiting the cyclooxygenase activity of platelet prostaglandin endoperoxide synthase (PGHS)-1 and monocyte PGHS-2 in a human whole blood assay was evaluated by measuring the levels of PGE2 produced in plasma.

TL;DR: In unstable angina, episodes of aspirin-insensitive TXA2 biosynthesis may reflect extraplatelet sources, possibly expressing the inducible PGHS in response to a local inflammatory milieu, and a selective PGHS-2 inhibitor would be an ideal tool to test the clinical relevance of this novel pathway of arachidonic acid metabolism in this setting.

TL;DR: Findings are consistent with the hypothesis that the basal rate of lipid peroxidation is a major determinant of the response to vitamin E supplementation and have implications for the use of vitamin E in healthy subjects as well as for the design and interpretation of clinical trials of antioxidant intervention.

TL;DR: It is concluded that L‐745, 337 and NS‐398 are selective inhibitors of the cyclo‐oxygenase activity of human monocyte PGHS‐2 and these compounds may provide adequate tools to test the contribution of this novel pathway of arachidonate metabolism to human inflammatory disease.