PMID- 16336776
OWN - NLM
STAT- MEDLINE
DCOM- 20091019
LR  - 20220321
IS  - 1225-8687 (Print)
IS  - 1225-8687 (Linking)
VI  - 38
IP  - 6
DP  - 2005 Nov 30
TI  - Prostaglandin E synthase, a terminal enzyme for prostaglandin E2 biosynthesis.
PG  - 633-8
AB  - Biosynthesis of prostanoids is regulated by three sequential enzymatic steps, 
      namely phospholipase A2 enzymes, cyclooxygenase (COX) enzymes, and various 
      lineagespecific terminal prostanoid synthases. Prostaglandin E synthase (PGES), 
      which isomerizes COX-derived PGH2 specifically to PGE2, occurs in multiple forms 
      with distinct enzymatic properties, expressions, localizations and functions. Two 
      of them are membrane-bound enzymes and have been designated as mPGES-1 and 
      mPGES-2. mPGES-1 is a perinuclear protein that is markedly induced by 
      proinflammatory stimuli, is down-regulated by antiinflammatory glucocorticoids, 
      and is functionally coupled with COX-2 in marked preference to COX-1. Recent gene 
      targeting studies of mPGES-1 have revealed that this enzyme represents a novel 
      target for anti-inflammatory and anti-cancer drugs. mPGES-2 is synthesized as a 
      Golgi membrane-associated protein, and the proteolytic removal of the N-terminal 
      hydrophobic domain leads to the formation of a mature cytosolic enzyme. This 
      enzyme is rather constitutively expressed in various cells and tissues and is 
      functionally coupled with both COX-1 and COX-2. Cytosolic PGES (cPGES) is 
      constitutively expressed in a wide variety of cells and is functionally linked to 
      COX-1 to promote immediate PGE2 production. This review highlights the latest 
      understanding of the expression, regulation and functions of these three PGES 
      enzymes.
FAU - Kudo, Ichiro
AU  - Kudo I
AD  - Department of Health Chemistry, School of Pharmaceutical Sciences, Showa 
      University, 1-5-8 Hatanodai, Shinagawa-ku, Tokyo 142-8555, Japan.
FAU - Murakami, Makoto
AU  - Murakami M
LA  - eng
PT  - Journal Article
PT  - Review
PL  - Korea (South)
TA  - J Biochem Mol Biol
JT  - Journal of biochemistry and molecular biology
JID - 9702084
RN  - 0 (Anti-Inflammatory Agents)
RN  - 0 (Anti-Inflammatory Agents, Non-Steroidal)
RN  - 0 (Glucocorticoids)
RN  - EC 5.3.- (Intramolecular Oxidoreductases)
RN  - EC 5.3.99.3 (PTGES protein, human)
RN  - EC 5.3.99.3 (PTGES2 protein, human)
RN  - EC 5.3.99.3 (Prostaglandin-E Synthases)
RN  - EC 5.3.99.3 (Ptges protein, mouse)
RN  - EC 5.3.99.3 (Ptges2 protein, mouse)
RN  - K7Q1JQR04M (Dinoprostone)
SB  - IM
MH  - Animals
MH  - Anti-Inflammatory Agents/pharmacology
MH  - Anti-Inflammatory Agents, Non-Steroidal/pharmacology
MH  - Cytosol/metabolism
MH  - Dinoprostone/*biosynthesis/metabolism
MH  - *Gene Expression Regulation, Enzymologic
MH  - Glucocorticoids/metabolism
MH  - Golgi Apparatus/metabolism
MH  - Humans
MH  - Inflammation
MH  - Intramolecular Oxidoreductases/*physiology
MH  - Mice
MH  - Models, Biological
MH  - Prostaglandin-E Synthases
MH  - Protein Structure, Tertiary
RF  - 45
EDAT- 2005/12/13 09:00
MHDA- 2009/10/20 06:00
CRDT- 2005/12/13 09:00
PHST- 2005/12/13 09:00 [pubmed]
PHST- 2009/10/20 06:00 [medline]
PHST- 2005/12/13 09:00 [entrez]
AID - 10.5483/bmbrep.2005.38.6.633 [doi]
PST - ppublish
SO  - J Biochem Mol Biol. 2005 Nov 30;38(6):633-8. doi: 10.5483/bmbrep.2005.38.6.633.