Molecular Identification of Cytosolic Prostaglandin E2 Synthase That Is Functionally Coupled with Cyclooxygenase-1 in Immediate Prostaglandin E2Biosynthesis*
- T. Tanioka, Yoshihito Nakatani, Natsuki Semmyo, M. Murakami, I. Kudo
- BiologyJournal of Biological Chemistry
- 20 October 2000
The molecular identification of cytosolic glutathione (GSH)-dependent prostaglandin (PG) E2 synthase (cPGES), a terminal enzyme of the cyclooxygenase (COX)-1-mediated PGE2 biosynthetic pathway, showed similarity to p23, which is reportedly the weakly bound component of the steroid hormone receptor/hsp90 complex.
Regulation of Prostaglandin E2 Biosynthesis by Inducible Membrane-associated Prostaglandin E2 Synthase That Acts in Concert with Cyclooxygenase-2*
COX-2 and mPGES are essential components for delayed PGE2 biosynthesis, which may be linked to inflammation, fever, osteogenesis, and even cancer.
Phospholipase A2 enzymes.
Recent progress in phospholipase A₂ research: from cells to animals to humans.
Cellular Prostaglandin E2 Production by Membrane-bound Prostaglandin E Synthase-2 via Both Cyclooxygenases-1 and -2*
Current evidence suggests that two forms of prostaglandin (PG) E synthase (PGES), cytosolic PGES and membrane-bound PGES (mPGES) -1, preferentially lie downstream of cyclooxygenase (COX) -1 and -2,…
Prostaglandin E synthase.
The Lipid Mediator Protectin D1 Inhibits Influenza Virus Replication and Improves Severe Influenza
Prostaglandin E synthase, a terminal enzyme for prostaglandin E2 biosynthesis.
This review highlights the latest understanding of the expression, regulation and functions of these three PGES enzymes.
Recent advances in molecular biology and physiology of the prostaglandin E2-biosynthetic pathway.
Fas-induced Arachidonic Acid Release Is Mediated by Ca2+-independent Phospholipase A2 but Not Cytosolic Phospholipase A2, Which Undergoes Proteolytic Inactivation*
- G. Atsumi, Masae Tajima, Atsuyoshi Hadano, Yoshihito Nakatani, M. Murakami, I. Kudo
- Biology, ChemistryJournal of Biological Chemistry
- 29 May 1998
iPLA2-mediated fatty acid release is facilitated in Fas-stimulated cells and plays a modifying although not essential role in the apoptotic cell death process, concluding that caspase-3-mediated c PLA2 cleavage eventually leads to destruction of a catalytic triad essential for cPLA2 activity, thereby terminating its AA-releasing function.