Selective prostaglandin G/H synthase (PGHS)-2 inhibitors show greater inhibitory activities on human PGHS-2 than on murine PGHS-2 in intact cells

J Berg; H Fellier; A Bodenteich; T Christoph; R Towart

doi:10.1007/s10787-997-0020-y

Selective prostaglandin G/H synthase (PGHS)-2 inhibitors show greater inhibitory activities on human PGHS-2 than on murine PGHS-2 in intact cells

Inflammopharmacology. 1997;5(2):119-26. doi: 10.1007/s10787-997-0020-y.

Authors

J Berg¹, H Fellier, A Bodenteich, T Christoph, R Towart

Affiliation

¹ Department of Pharmacology, TopCro Pharma Research GmbH, Linz, Austria.

PMID: 17694360
DOI: 10.1007/s10787-997-0020-y

Abstract

Excess eicosanoid formation during inflammation has been attributed to the expression of the gene coding for the inducible isoform of prostaglandin G/H synthase (PGHS-2). Human and murine PGHS-2 proteins differ in 73 out of the 604 amino acids. When comparing the inhibitory effects of a panel of PGHS-inhibitors in a whole cell human and murine PGHS-2 assay carried out under identical conditions, classical NSAIDs with the exception of aspirin and tenoxicam showed similar inhibitory effects on both human and murine PGHS-2 enzymes. However, the PGHS-2 selective inhibitors nimesulide, flosulide and NS398 showed a much greater inhibition of human PGHS-2. We suggest that these differences could be due to the genetic differences of human and murine PGHS-2.