MPGES-1

PTGES
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	3DWW, 4WAB, 4AL1, 4BPM, 4YL1, 4YL3, 4YK5, 4AL0, 4YL0, 5BQI, 5BQG, 5BQH Contents See also ; References ; Further reading ;
Identifiers
Aliases	PTGES , MGST-IV, MGST1-L1, MGST1L1, MPGES, PGES, PIG12, PP102, PP1294, TP53I12, mPGES-1, prostaglandin E synthase
External IDs	OMIM: 605172 MGI: 1927593 HomoloGene: 3587 GeneCards: PTGES
Gene location (Human)
Chr.	Chromosome 9 (human)
End	129,753,042 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	30,819,875 bp
RNA expression pattern
	Top expressed in
	palpebral conjunctiva; ; gastric mucosa; ; seminal vesicula; ; mucosa of urinary bladder; ; skin of abdomen; ; nipple; ; minor salivary gland; ; canal of the cervix; ; pancreatic ductal cell; ; placenta;
	Top expressed in
	blastocyst; ; morula; ; cumulus cell; ; white adipose tissue; ; lip; ; ankle joint; ; urethra; ; esophagus; ; urinary bladder; ; calvaria;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	glutathione binding ; isomerase activity ; prostaglandin-E synthase activity ; glutathione transferase activity ;
Cellular component	cytoplasm ; integral component of membrane ; endoplasmic reticulum membrane ; intracellular membrane-bounded organelle ; membrane ; nuclear envelope lumen ; perinuclear region of cytoplasm ; mitochondrion ;
Biological process	prostaglandin metabolic process ; response to cytokine ; response to organic cyclic compound ; response to retinoic acid ; lipid metabolism ; cyclooxygenase pathway ; fatty acid metabolic process ; response to calcium ion ; response to lipopolysaccharide ; fatty acid biosynthetic process ; acute inflammatory response ; prostaglandin biosynthetic process ; chronic inflammatory response ; negative regulation of cell population proliferation ; signal transduction ; glutathione metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	9536
	64292
	ENSG00000148344
	ENSMUSG00000050737
	O14684
	Q9JM51
	NM_004878 ; NM_198797
	NM_022415
	NP_004869
	NP_071860
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated August 19, 2023

Microsomal prostaglandin E synthase-1 (mPGES-1)^[5]^[6] or Prostaglandin E synthase is an enzyme that in humans is encoded by the PTGES gene.^[7]^[8]^[9]

The protein encoded by this gene is a glutathione-dependent prostaglandin E synthase. The expression of this gene has been shown to be induced by proinflammatory cytokine interleukin 1 beta (IL1B). Its expression can also be induced by tumor suppressor protein TP53, and may be involved in TP53-induced apoptosis.

Knockout studies in mice suggest that this gene may contribute to the pathogenesis of collagen-induced arthritis and mediate acute pain during inflammatory responses.^[9]

Related Research Articles

Leukotriene C₄ (LTC₄) is a leukotriene. LTC₄ has been extensively studied in the context of allergy and asthma. In cells of myeloid origin such as mast cells, its biosynthesis is orchestrated by translocation to the nuclear envelope along with co-localization of cytosolic phospholipase A2 (cPLA2), Arachidonate 5-lipoxygenase (5-LO), 5-lipoxygenase-activating protein (FLAP) and LTC₄ synthase (LTC₄S), which couples glutathione to an LTA₄ intermediate. The MRP1 transporter then secretes cytosolic LTC₄ and cell surface proteases further metabolize it by sequential cleavage of the γ-glutamyl and glycine residues off its glutathione segment, generating the more stable products LTD₄ and LTE₄. All three leukotrienes then bind at different affinities to two G-protein coupled receptors: CYSLTR1 and CYSLTR2, triggering pulmonary vasoconstriction and bronchoconstriction.

<span class="mw-page-title-main">Prostaglandin E synthase</span>

Prostaglandin E synthase is an enzyme involved in eicosanoid and glutathione metabolism, a member of MAPEG family. It generates prostaglandin E (PGE) from prostaglandin H2.

Leukotriene C4 synthase is an enzyme that in humans is encoded by the LTC4S gene.

<span class="mw-page-title-main">Prostaglandin-endoperoxide synthase 2</span> Human enzyme involved in inflammation

Prostaglandin-endoperoxide synthase 2, also known as cyclooxygenase-2 or COX-2, is an enzyme that in humans is encoded by the PTGS2 gene. In humans it is one of two cyclooxygenases. It is involved in the conversion of arachidonic acid to prostaglandin H2, an important precursor of prostacyclin, which is expressed in inflammation.

<span class="mw-page-title-main">Glutathione S-transferase A1</span> Protein-coding gene in the species Homo sapiens

Glutathione S-transferase A1 is an enzyme that in humans is encoded by the GSTA1 gene.

Glutathione S-transferase Mu 2 is an enzyme that in humans is encoded by the GSTM2 gene.

Hyaluronan synthase 2 is an enzyme that in humans is encoded by the HAS2 gene.

Glutathione peroxidase 2 is an enzyme that in humans is encoded by the GPX2 gene.

Alpha-N-acetylneuraminide alpha-2,8-sialyltransferase is an enzyme that in humans is encoded by the ST8SIA1 gene.

Glutathione S-transferase Mu 4 is an enzyme that in humans is encoded by the GSTM4 gene.

Hyaluronan synthase 1 is an enzyme that in humans is encoded by the HAS1 gene.

Microsomal glutathione S-transferase 1 is an enzyme that in humans is encoded by the MGST1 gene.

Ceramide glucosyltransferase is an enzyme that in humans is encoded by the UGCG gene.

PGDS protein is a protein that in humans is encoded by the HPGDS gene.

In molecular biology the MAPEG family of proteins are a group of membrane associated proteins with highly divergent functions. Included are the 5-lipoxygenase-activating protein, leukotriene C4 synthase, which catalyzes the production of leukotriene C4 (LTC4) from leukotriene A4 (LTA4), and microsomal glutathione S-transferase II (GST-II), which also produces LTC4 from LTA4.

Hyaluronan synthase 3 is an enzyme that in humans is encoded by the HAS3 gene.

Microsomal glutathione S-transferase 2 is an enzyme that in humans is encoded by the MGST2 gene.

Microsomal glutathione S-transferase 3 is an enzyme that in humans is encoded by the MGST3 gene.

Microsomal prostaglandin E synthase-2 (mPGES-2) or Prostaglandin E synthase 2 is an enzyme that in humans encoded by the PTGES2 gene located on chromosome 9. The protein encoded by this gene is a membrane-associated prostaglandin E synthase, which catalyzes the conversion of prostaglandin H2 to prostaglandin E2. This protein also has been shown to activate the transcription regulated by a gamma-interferon-activated transcription element (GATE). Multiple transcript variants have been found for this gene.

Glutathione peroxidase 6 (GPx-6) is an enzyme that in humans is encoded by the GPX6 gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000148344 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050737 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Jakobsson PJ, Thorén S, Morgenstern R, et al. (1989). "Identification of human prostaglandin E synthase: a microsomal glutathione-dependent, inducible enzyme, constituting a potential novel drug target". Proc Natl Acad Sci USA. 96 (13): 7220–7225. Bibcode:1999PNAS...96.7220J. doi: 10.1073/pnas.96.13.7220 . PMC 22058 . PMID 10377395.
↑ Hui-Hua Chang; Emmanuelle J Meuillet (2011). "Identification and development of mPGES-1 inhibitors: where we are at?". Future Med Chem. 3 (15): 1909–1934. doi:10.4155/fmc.11.136. PMC 3232027 . PMID 22023034.
↑ Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B (Sep 1997). "A model for p53-induced apoptosis". Nature. 389 (6648): 300–5. Bibcode:1997Natur.389..300P. doi:10.1038/38525. PMID 9305847. S2CID 4429638.
↑ Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A, Persson B (May 1999). "Common structural features of MAPEG -- a widespread superfamily of membrane-associated proteins with highly divergent functions in eicosanoid and glutathione metabolism". Protein Sci. 8 (3): 689–92. doi:10.1110/ps.8.3.689. PMC 2144274 . PMID 10091672.
1 2 "Entrez Gene: PTGES prostaglandin E synthase".

Bastien L, Sawyer N, Grygorczyk R, et al. (1994). "Cloning, functional expression, and characterization of the human prostaglandin E2 receptor EP2 subtype". J. Biol. Chem. 269 (16): 11873–7. doi: 10.1016/S0021-9258(17)32654-6 . PMID 8163486.
Wu T, Wu H, Wang J, Wang J (2011). "Expression and cellular localization of cyclooxygenases and prostaglandin E synthases in the hemorrhagic brain". J Neuroinflammation. 8: 22. doi:10.1186/1742-2094-8-22. PMC 3062590 . PMID 21385433.
Funk CD, Furci L, FitzGerald GA, et al. (1994). "Cloning and expression of a cDNA for the human prostaglandin E receptor EP1 subtype". J. Biol. Chem. 268 (35): 26767–72. doi: 10.1016/S0021-9258(19)74379-8 . PMID 8253813.
Giacomini E, Giordani L, di Modugno F, et al. (1998). "Increased PGE2 production mediates the in vitro inhibitory effect of the human immunodeficiency virus P24 immunosuppressive heptapeptide Ch7". Scand. J. Immunol. 48 (3): 248–53. doi:10.1046/j.1365-3083.1998.00389.x. PMID 9743208. S2CID 20332912.
Jakobsson PJ, Thorén S, Morgenstern R, Samuelsson B (1999). "Identification of human prostaglandin E synthase: a microsomal, glutathione-dependent, inducible enzyme, constituting a potential novel drug target". Proc. Natl. Acad. Sci. U.S.A. 96 (13): 7220–5. Bibcode:1999PNAS...96.7220J. doi: 10.1073/pnas.96.13.7220 . PMC 22058 . PMID 10377395.
Forsberg L, Leeb L, Thorén S, et al. (2000). "Human glutathione dependent prostaglandin E synthase: gene structure and regulation". FEBS Lett. 471 (1): 78–82. doi:10.1016/S0014-5793(00)01367-3. PMID 10760517. S2CID 10901322.
Han R, Smith TJ (2002). "Cytoplasmic prostaglandin E2 synthase is dominantly expressed in cultured KAT-50 thyrocytes, cells that express constitutive prostaglandin-endoperoxide H synthase-2. Basis for low protaglandin E2 production". J. Biol. Chem. 277 (39): 36897–903. doi: 10.1074/jbc.M206949200 . PMID 12145315.
Giannoulias D, Alfaidy N, Holloway AC, et al. (2002). "Expression of prostaglandin I(2) synthase, but not prostaglandin E synthase, changes in myometrium of women at term pregnancy". J. Clin. Endocrinol. Metab. 87 (11): 5274–82. doi: 10.1210/jc.2002-020521 . PMID 12414902.
Ouellet M, Falgueyret JP, Ear PH, et al. (2003). "Purification and characterization of recombinant microsomal prostaglandin E synthase-1". Protein Expr. Purif. 26 (3): 489–95. doi:10.1016/S1046-5928(02)00566-1. PMID 12460774.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi: 10.1073/pnas.242603899 . PMC 139241 . PMID 12477932.
Uracz W, Uracz D, Olszanecki R, Gryglewski RJ (2003). "Interleukin 1beta induces functional prostaglandin E synthase in cultured human umbilical vein endothelial cells". J. Physiol. Pharmacol. 53 (4 Pt 1): 643–54. PMID 12512699.
Meadows JW, Eis AL, Brockman DE, Myatt L (2003). "Expression and localization of prostaglandin E synthase isoforms in human fetal membranes in term and preterm labor". J. Clin. Endocrinol. Metab. 88 (1): 433–9. doi: 10.1210/jc.2002-021061 . PMID 12519887.
Kamei D, Murakami M, Nakatani Y, et al. (2003). "Potential role of microsomal prostaglandin E synthase-1 in tumorigenesis". J. Biol. Chem. 278 (21): 19396–405. doi: 10.1074/jbc.M213290200 . PMID 12626523.
Jakobsson PJ, Thorén S, Morgenstern R, Samuelsson B (2003). "Characterization of microsomal, glutathione dependent prostaglandin E synthase". Adv. Exp. Med. Biol. Advances in Experimental Medicine and Biology. 507: 287–91. doi:10.1007/978-1-4615-0193-0_44. ISBN 978-0-306-47283-1. PMID 12664599.
Thorén S, Weinander R, Saha S, et al. (2003). "Human microsomal prostaglandin E synthase-1: purification, functional characterization, and projection structure determination". J. Biol. Chem. 278 (25): 22199–209. doi: 10.1074/jbc.M303227200 . PMID 12672824.
Alfaidy N, Sun M, Challis JR, Gibb W (2003). "Expression of membrane prostaglandin E synthase in human placenta and fetal membranes and effect of labor". Endocrine. 20 (3): 219–25. doi:10.1385/ENDO:20:3:219. PMID 12721500. S2CID 9590845.
Ekström L, Lyrenäs L, Jakobsson PJ, et al. (2003). "Basal expression of the human MAPEG members microsomal glutathione transferase 1 and prostaglandin E synthase genes is mediated by Sp1 and Sp3". Biochim. Biophys. Acta. 1627 (2–3): 79–84. doi:10.1016/S0167-4781(03)00077-0. PMID 12818425.
Murakami M, Nakashima K, Kamei D, et al. (2003). "Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2". J. Biol. Chem. 278 (39): 37937–47. doi: 10.1074/jbc.M305108200 . PMID 12835322.
Trebino CE, Stock JL, Gibbons CP, et al. (2003). "Impaired inflammatory and pain responses in mice lacking an inducible prostaglandin E synthase". Proc. Natl. Acad. Sci. U.S.A. 100 (15): 9044–9. Bibcode:2003PNAS..100.9044T. doi: 10.1073/pnas.1332766100 . PMC 166435 . PMID 12835414.

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000148344 - Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000050737 - Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid10377395-5] Jakobsson PJ, Thorén S, Morgenstern R, et al. (1989). "Identification of human prostaglandin E synthase: a microsomal glutathione-dependent, inducible enzyme, constituting a potential novel drug target". Proc Natl Acad Sci USA. 96 (13): 7220–7225. Bibcode:1999PNAS...96.7220J. doi: 10.1073/pnas.96.13.7220 . PMC 22058 . PMID 10377395.

[PMC3232027-6] Hui-Hua Chang; Emmanuelle J Meuillet (2011). "Identification and development of mPGES-1 inhibitors: where we are at?". Future Med Chem. 3 (15): 1909–1934. doi:10.4155/fmc.11.136. PMC 3232027 . PMID 22023034.

[pmid9305847-7] Polyak K, Xia Y, Zweier JL, Kinzler KW, Vogelstein B (Sep 1997). "A model for p53-induced apoptosis". Nature. 389 (6648): 300–5. Bibcode:1997Natur.389..300P. doi:10.1038/38525. PMID 9305847. S2CID 4429638.

[pmid10091672-8] Jakobsson PJ, Morgenstern R, Mancini J, Ford-Hutchinson A, Persson B (May 1999). "Common structural features of MAPEG -- a widespread superfamily of membrane-associated proteins with highly divergent functions in eicosanoid and glutathione metabolism". Protein Sci. 8 (3): 689–92. doi:10.1110/ps.8.3.689. PMC 2144274 . PMID 10091672.

[entrez-9] 1 2 "Entrez Gene: PTGES prostaglandin E synthase".

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MPGES-1

Contents

See also

Related Research Articles

References

Further reading