[HTML][HTML] Molecular identification of cytosolic prostaglandin E2 synthase that is functionally coupled with cyclooxygenase-1 in immediate prostaglandin E2biosynthesis
T Tanioka, Y Nakatani, N Semmyo, M Murakami… - Journal of Biological …, 2000 - ASBMB
Here we report the molecular identification of cytosolic glutathione (GSH)-dependent
prostaglandin (PG) E 2 synthase (cPGES), a terminal enzyme of the cyclooxygenase (COX)-
1-mediated PGE 2 biosynthetic pathway. GSH-dependent PGES activity in the cytosol of rat
brains, but not of other tissues, increased 3-fold after lipopolysaccharide (LPS) challenge.
Peptide microsequencing of purified enzyme revealed that it was identical to p23, which is
reportedly the weakly bound component of the steroid hormone receptor/hsp90 complex …
prostaglandin (PG) E 2 synthase (cPGES), a terminal enzyme of the cyclooxygenase (COX)-
1-mediated PGE 2 biosynthetic pathway. GSH-dependent PGES activity in the cytosol of rat
brains, but not of other tissues, increased 3-fold after lipopolysaccharide (LPS) challenge.
Peptide microsequencing of purified enzyme revealed that it was identical to p23, which is
reportedly the weakly bound component of the steroid hormone receptor/hsp90 complex …