Abstract
Prostaglandins play critical roles in a number of physiological and pathophysiological processes. These molecules are involved in regulating blood flow to organs, initiating platelet aggregation in blood clotting, and mainly mediating the classical symptoms of inflammation. Biosynthesis of prostaglandins is initiated by prostaglandin endoperoxide H synthases (PGHS) −1 and −2, which catalyze the conversion of arachidonic acid to PGH2. PGHSs are homodimers comprised of ∼72 kDa monomers of identical primary sequence and recently have been investigated in the respect of allosteric communications between two subunits during ligand binding. The nonsteroidal anti-inflammatory drugs show multiple inhibition modalities against PGHSs. Their time-dependent and subunit-preferential bindings to PGHSs complicate the interactions of PGHSs with the cognate substrates and their regulations by natural and synthetic ligands. Accordingly, a paradigm shift in the analysis of PGHS-ligand complex during PGHS catalysis is required and their theoretical revaluation and biological functioning in vivo are described in this paper.
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