PGDS

HPGDS
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1IYH, 1IYI, 1V40, 2CVD, 2VCQ, 2VCW, 2VCX, 2VCZ, 2VD0, 2VD1, 3EE2, 3KXO, 3VI5, 3VI7, 4EC0, 4EDY, 4EDZ, 4EE0, 5AIS, 5AIV, 5AIX Contents See also ; References ; Further reading ;
Identifiers
Aliases	HPGDS , GSTS, GSTS1-1, PGD2, PGDS, GSTS1, hematopoietic prostaglandin D synthase
External IDs	OMIM: 602598 MGI: 1859384 HomoloGene: 113741 GeneCards: HPGDS
EC number	2.5.1.18
Gene location (Human)
Chr.	Chromosome 4 (human)
End	94,342,876 bp
Gene location (Mouse)
Chr.	Chromosome 6 (mouse)
End	65,121,892 bp
RNA expression pattern
	Top expressed in
	placenta; ; Achilles tendon; ; gallbladder; ; synovial membrane; ; amniotic fluid; ; rectum; ; synovial joint; ; upper lobe of left lung; ; optic nerve; ; right coronary artery;
	Top expressed in
	calvaria; ; Sertoli cell; ; yolk sac; ; ooblast; ; cornea; ; uterus; ; thyroid gland; ; superior frontal gyrus; ; neural tube; ; thymus;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	transferase activity ; calcium ion binding ; protein homodimerization activity ; isomerase activity ; metal ion binding ; prostaglandin-D synthase activity ; protein binding ; magnesium ion binding ; glutathione transferase activity ;
Cellular component	cytoplasm ; cytosol ;
Biological process	prostaglandin metabolic process ; locomotory behavior ; lipid metabolism ; cyclooxygenase pathway ; fatty acid metabolic process ; fatty acid biosynthetic process ; prostaglandin biosynthetic process ; glutathione derivative biosynthetic process ; signal transduction ; negative regulation of male germ cell proliferation ; glutathione metabolic process ;
	Sources:Amigo / QuickGO
Orthologs
	27306
	54486
	ENSG00000163106
	ENSMUSG00000029919
	O60760
	Q9JHF7
	NM_014485
	NM_019455
	NP_055300
	NP_062328
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated May 22, 2024

PGDS protein is a protein that in humans is encoded by the HPGDS gene.^[5]^[6]^[7]^[8]

Prostaglandin-D synthase is a sigma class glutathione-S-transferase family member. The enzyme catalyzes the conversion of PGH2 to PGD2 and plays a role in the production of prostanoids in the immune system and mast cells. The presence of this enzyme can be used to identify the differentiation stage of human megakaryocytes.^[8]

Related Research Articles

Prostaglandin D₂ (or PGD₂) is a prostaglandin that binds to the receptor PTGDR (DP₁), as well as CRTH2 (DP₂). It is a major prostaglandin produced by mast cells – recruits Th2 cells, eosinophils, and basophils. In mammalian organs, large amounts of PGD₂ are found only in the brain and in mast cells. It is critical to development of allergic diseases such as asthma. Research carried out in 1989 found PGD₂ is the primary mediator of vasodilation (the "niacin flush") after ingestion of niacin (nicotinic acid).

The prostaglandin D₂ receptor 1 (DP₁), a G protein-coupled receptor encoded by the PTGDR1 gene (also termed PTGDR), is primarily a receptor for prostaglandin D₂ (PGD₂). The receptor is a member of the prostaglandin receptors belonging to the subfamily A14 of rhodopsin-like receptors. Activation of DP1 by PGD2 or other cognate receptor ligands is associated with a variety of physiological and pathological responses in animal models.

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

Prostaglandin-H2 D-isomerase (PTGDS) is an enzyme that in humans is encoded by the PTGDS gene.

Glutathione S-transferase P is an enzyme that in humans is encoded by the GSTP1 gene.

<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.

In enzymology, a prostaglandin-D synthase is an enzyme that catalyzes the chemical reaction

Prostaglandin F receptor (FP) is a receptor belonging to the prostaglandin (PG) group of receptors. FP binds to and mediates the biological actions of Prostaglandin F_2α (PGF_2α). It is encoded in humans by the PTGFR gene.

Glutathione S-transferase A2 is an enzyme that in humans is encoded by the GSTA2 gene.

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

Glutathione S-transferase M3 (brain), also known as GSTM2, is an enzyme which in humans is encoded by the GSTM99 gene.

Glutathione S-transferase A4, also known as GSTA4, is an enzyme which in humans is encoded by the GSTA4 gene.

Serine/threonine-protein kinase D2 or PKD2 is an enzyme that in humans is encoded by the PRKD2 gene.

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

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

Glutathione S-transferase omega-1 is an enzyme that in humans is encoded by the GSTO1 gene.

Beta-1,4 N-acetylgalactosaminyltransferase 1 is an enzyme that in humans is encoded by the B4GALNT1 gene.

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

Microsomal prostaglandin E synthase-1 (mPGES-1) or Prostaglandin E synthase is an enzyme that in humans is encoded by the PTGES gene.

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

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000163106 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029919 – 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.
↑ Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O (Oct 1997). "Cloning and crystal structure of hematopoietic prostaglandin D synthase". Cell. 90 (6): 1085–95. doi: 10.1016/S0092-8674(00)80374-8 . PMID 9323136. S2CID 933875.
↑ Mahmud I, Ueda N, Yamaguchi H, Yamashita R, Yamamoto S, Kanaoka Y, Urade Y, Hayaishi O (Dec 1997). "Prostaglandin D synthase in human megakaryoblastic cells". J Biol Chem. 272 (45): 28263–6. doi: 10.1074/jbc.272.45.28263 . PMID 9353279.
↑ Jowsey IR, Thomson AM, Flanagan JU, Murdock PR, Moore GB, Meyer DJ, Murphy GJ, Smith SA, Hayes JD (Oct 2001). "Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases". Biochem J. 359 (Pt 3): 507–16. doi:10.1042/0264-6021:3590507. PMC 1222171 . PMID 11672424.
1 2 "Entrez Gene: PGDS prostaglandin D2 synthase, hematopoietic".

Kanaoka Y, Urade Y (2004). "Hematopoietic prostaglandin D synthase". Prostaglandins Leukot. Essent. Fatty Acids. 69 (2–3): 163–7. doi:10.1016/S0952-3278(03)00077-2. PMID 12895599.
Suzuki T, Watanabe K, Kanaoka Y, et al. (1998). "Induction of hematopoietic prostaglandin D synthase in human megakaryocytic cells by phorbol ester". Biochem. Biophys. Res. Commun. 241 (2): 288–93. doi:10.1006/bbrc.1997.7803. PMID 9425264.
Tokugawa Y, Kunishige I, Kubota Y, et al. (1998). "Lipocalin-type prostaglandin D synthase in human male reproductive organs and seminal plasma". Biol. Reprod. 58 (2): 600–7. doi: 10.1095/biolreprod58.2.600 . PMID 9475419.
Pinzar E, Kanaoka Y, Inui T, et al. (2000). "Prostaglandin D synthase gene is involved in the regulation of non-rapid eye movement sleep". Proc. Natl. Acad. Sci. U.S.A. 97 (9): 4903–7. Bibcode:2000PNAS...97.4903P. doi: 10.1073/pnas.090093997 . PMC 18330 . PMID 10781097.
Kanaoka Y, Fujimori K, Kikuno R, et al. (2000). "Structure and chromosomal localization of human and mouse genes for hematopoietic prostaglandin D synthase. Conservation of the ancestral genomic structure of sigma-class glutathione S-transferase". Eur. J. Biochem. 267 (11): 3315–22. doi: 10.1046/j.1432-1327.2000.01362.x . PMID 10824118.
Fujimori K, Kanaoka Y, Sakaguchi Y, Urade Y (2001). "Transcriptional activation of the human hematopoietic prostaglandin D synthase gene in megakaryoblastic cells. Roles of the oct-1 element in the 5'-flanking region and the AP-2 element in the untranslated exon 1". J. Biol. Chem. 275 (51): 40511–6. doi: 10.1074/jbc.M007688200 . PMID 10998423.
Sui D, Wilson JE (2000). "Interaction of insulin-like growth factor binding protein-4, Miz-1, leptin, lipocalin-type prostaglandin D synthase, and granulin precursor with the N-terminal half of type III hexokinase". Arch. Biochem. Biophys. 382 (2): 262–74. doi:10.1006/abbi.2000.2019. PMID 11068878.
Noguchi E, Shibasaki M, Kamioka M, et al. (2002). "New polymorphisms of haematopoietic prostaglandin D synthase and human prostanoid DP receptor genes". Clin. Exp. Allergy. 32 (1): 93–6. doi:10.1046/j.0022-0477.2001.01261.x. PMID 12002745. S2CID 24779233.
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.
Inoue T, Irikura D, Okazaki N, et al. (2003). "Mechanism of metal activation of human hematopoietic prostaglandin D synthase". Nat. Struct. Biol. 10 (4): 291–6. doi:10.1038/nsb907. PMID 12627223. S2CID 25214344.
Ando M, Murakami Y, Kojima F, et al. (2003). "Retrovirally introduced prostaglandin D2 synthase suppresses lung injury induced by bleomycin". Am. J. Respir. Cell Mol. Biol. 28 (5): 582–91. doi:10.1165/rcmb.2002-0162OC. PMID 12707014.
Inoue T, Okano Y, Kado Y, et al. (2005). "First determination of the inhibitor complex structure of human hematopoietic prostaglandin D synthase". J. Biochem. 135 (3): 279–83. doi:10.1093/jb/mvh033. PMID 15113825.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928 . PMID 15489334.

This article on a gene on human chromosome 4 is a stub. You can help Wikipedia by expanding it.

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.

[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000163106 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000029919 – 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.

[pmid9323136-5] Kanaoka Y, Ago H, Inagaki E, Nanayama T, Miyano M, Kikuno R, Fujii Y, Eguchi N, Toh H, Urade Y, Hayaishi O (Oct 1997). "Cloning and crystal structure of hematopoietic prostaglandin D synthase". Cell. 90 (6): 1085–95. doi: 10.1016/S0092-8674(00)80374-8 . PMID 9323136. S2CID 933875.

[pmid9353279-6] Mahmud I, Ueda N, Yamaguchi H, Yamashita R, Yamamoto S, Kanaoka Y, Urade Y, Hayaishi O (Dec 1997). "Prostaglandin D synthase in human megakaryoblastic cells". J Biol Chem. 272 (45): 28263–6. doi: 10.1074/jbc.272.45.28263 . PMID 9353279.

[pmid11672424-7] Jowsey IR, Thomson AM, Flanagan JU, Murdock PR, Moore GB, Meyer DJ, Murphy GJ, Smith SA, Hayes JD (Oct 2001). "Mammalian class Sigma glutathione S-transferases: catalytic properties and tissue-specific expression of human and rat GSH-dependent prostaglandin D2 synthases". Biochem J. 359 (Pt 3): 507–16. doi:10.1042/0264-6021:3590507. PMC 1222171 . PMID 11672424.

[entrez-8] 1 2 "Entrez Gene: PGDS prostaglandin D2 synthase, hematopoietic".

[1]

[2]

[3]

[4]

[5]

[6]

[7]

[8]

PGDS

Contents

See also

Related Research Articles

References

Further reading