Expression, Purification and Characterization of Recombinant Human Microsomal PGE2 Synthase-1 View Full Text


Ontology type: schema:Chapter     


Chapter Info

DATE

2003

AUTHORS

Marc Ouellet , Ally Pen , Po-Hien Ear , Jean-Pierre Falgueyret , Tammy G. LeRiche , Joseph A. Mancini , Denis Riendeau , M. David Percival

ABSTRACT

Prostaglandin E synthases (PGES) comprise a number of structurally different enzymes that convert the product of the cyclooxygenase enzymes, PGH2, into the physiologically important PGE2. An inducible microsomal PGES (mPGES-1) couples preferentially with COX-2 [1], whereas a constitutively and widely expressed cytosolic PGES (cPGES or p23) is believed to couple with Cox-1 [2]. Both of these enzyme activities are dependent on GSH. Most recently, a second, membrane-associated PGES (mPGES-2) that has a wide tissue distribution and is activated by a number of thio1-containing reagents was identified and purified [3]. Two cytosolic glutathione transferases (μ2 and μ3) also have some PGES activity. As the expression of mPGES-1 is strongly induced by pro-inflammatory stimuli and is down-regulated by glucocorticoids, mPGES-1 is a potential drug target for anti-inflammatory therapy. A solubilization and partial purification of a microsomal PGES activity from bovine vesicular glands has been reported [4]. It appears that this enzyme is the same as mPGES-1. Here we report the baculovirus over-expression of recombinant human mPGES-1 in Sf9 insect cells, its purification to apparent homogeneity and the characterization of its enzymatic properties. More... »

PAGES

113-116

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/978-1-4419-9194-2_22

DOI

http://dx.doi.org/10.1007/978-1-4419-9194-2_22

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1051259895

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/12751747


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