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Information on EC 5.3.99.4 - prostaglandin-I synthase and Organism(s) Homo sapiens and UniProt Accession Q16647
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5.3.99.4 prostaglandin-I synthaseIUBMB Comments
A cytochrome P-450 heme-thiolate enzyme. Converts prostaglandin H2 into prostaglandin I2 (prostacyclin).
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Word Map
- 5.3.99.4
-
thromboxane
-
cyclooxygenase
- endothelial
-
arachidonic
- artery
- platelet
- cox-2
-
vasodilator
- hypertension
-
prostanoids
-
endoperoxide
-
eicosanoids
- pulmonary
- vessel
- indomethacin
- aorta
-
6-keto-pgf1
- tranylcypromine
- peroxynitrite
-
vasoconstriction
-
endothelium-dependent
-
6-keto-prostaglandin
-
6-keto-pgf1alpha
-
phosphoglucose
-
iloprost
- tx
- mpges-1
- medicine
-
6-keto
-
antithrombotic
-
5-lipoxygenase
- dazoxiben
-
heme-thiolate
- ptges
- f1alpha
- synthase-1
-
beraprost
- 15-hpete
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
pgis, prostacyclin synthase, pgi2 synthase, ptgis, prostacyclin synthetase, pgi2 synthetase, cyp8a1, pgi synthase, prostaglandin i2 synthase, pgi2-s, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Aortic cytochrom P450
-
-
-
-
PGI2 synthase
PGI2 synthetase
-
-
-
-
PGIS
prostacyclin synthase
Prostacyclin synthetase
-
-
-
-
Prostacycline synthetase
-
-
-
-
Prostaglandin I2 synthase
Prostaglandin I2 synthetase
-
-
-
-
Synthetase, prostacyclin
-
-
-
-
PGI2 synthase
-
-
-
-
PGIS
-
-
-
-
PGIS
-
-
prostacyclin synthase
-
-
-
-
prostacyclin synthase
-
-
Prostaglandin I2 synthase
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E,15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate
mechanism
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
isomerization
intramolecular oxidoreduction
-
-
-
-
isomerization
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -, -
SYSTEMATIC NAME
IUBMB Comments
(5Z,13E)-(15S)-9alpha,11alpha-Epidioxy-15-hydroxyprosta-5,13-dienoate 6-isomerase
A cytochrome P-450 heme-thiolate enzyme. Converts prostaglandin H2 into prostaglandin I2 (prostacyclin).
CAS REGISTRY NUMBER
COMMENTARY
65802-86-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
15-hydroperoxyeicosatetraenoic acid
13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid + 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid
-
13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid and 15-ketoeicosatetraenoic acid result from homolytic cleavage of the O-O bond, whereas 13-hydroxy-14,15-epoxy-5,8,11-eicosatrienoic acid + 15-ketoeicosatetraenoic acid results from heterolytic cleavage. About 80% of substrate is cleaved homolytically, and maximal velocity of homolytic cleavage is about 1.4fold faster than heterolytic cleavage
-
?
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-6,9alpha-epoxy-11a,15-dihydroxyprosta-5,13-dienoate
-
i.e. prostaglandin H2
prostaglandin I2
?
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate
-
-
-
-
?
10-hydroperoxyoctadeca-8,12-dienoic acid
10-oxooctadeca-8,12-dienoic acid + 10-oxodec-8-enoic acid + 10-hydroxyoctadeca-8,12-dienoic acid
-
-
-
-
?
prostaglandin H1
12-hydroxy-8,10-heptadecadienoic acid + malondialdehyde
-
-
-
-
?
additional information
?
-
-
fusion protein linking cyclooxygenase COX-2 and prostacyclin synthase together, is able to convert arachidonic acid to prostaglandin G2, prostaglandin H2 and prostaglandin I2. Fusion protein may directly synthesize prostaglandin I2 from arachidonic acid with Km value of 0.0032 mM
-
-
?
Prostaglandin H2
?
-
produces prostaglandin I2 which has opposite actions on platelet aggregatory and vasoconstrictive properties
-
-
?
Prostaglandin H2
?
-
formation of prostaglandin I2 which is a powerful vasodilator and the most potent naturally occuring inhibitor of platlet aggregation. An imbalance in the ratio of prostaglandin I2 to thromboxane A2, a compound that has opposite biological properties may reflect some of the changes occuring in various pathological situations including thrombosis and ischemia
-
-
?
Prostaglandin H2
Prostaglandin I2
-
-
-
-
?
Prostaglandin H2
Prostaglandin I2
-
in vivo, this reaction is coupled to a previous one, where arachidonic acid is converted by cyclooxygenase and yields the substrate PGH2
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(5Z,13E)-(15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E)-(15S)-6,9alpha-epoxy-11a,15-dihydroxyprosta-5,13-dienoate
-
i.e. prostaglandin H2
prostaglandin I2
?
(5Z,13E,15S)-9alpha,11alpha-epidioxy-15-hydroxyprosta-5,13-dienoate
(5Z,13E,15S)-6,9alpha-epoxy-11alpha,15-dihydroxyprosta-5,13-dienoate
-
-
-
-
?
Prostaglandin H2
?
-
produces prostaglandin I2 which has opposite actions on platelet aggregatory and vasoconstrictive properties
-
-
?
Prostaglandin H2
?
-
formation of prostaglandin I2 which is a powerful vasodilator and the most potent naturally occuring inhibitor of platlet aggregation. An imbalance in the ratio of prostaglandin I2 to thromboxane A2, a compound that has opposite biological properties may reflect some of the changes occuring in various pathological situations including thrombosis and ischemia
-
-
?
Prostaglandin H2
Prostaglandin I2
-
-
-
-
?
Prostaglandin H2
Prostaglandin I2
-
in vivo, this reaction is coupled to a previous one, where arachidonic acid is converted by cyclooxygenase and yields the substrate PGH2
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
heme
-
heme conformation and heme protein matrix interactions for human and zebrafish enzymes in the presence and absence of ligands, overview. The heme group is in the ferric, six-coordinate, low-spin state for both resting and ligand-bound enzymes of boh species. Drastically different RR shifts with heme conformational changes in both hPGIS and zPGIS upon different ligand bindings, suggesting that PGIS exhibits a ligand-specific heme conformational change to accommodate the substrate binding
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
miconazole
-
i.e. 1-[2,4-dichloro-beta-[(2,4-dichlorobenzyl)oxy]phenyl]imidazole
additional information
-
the enzyme is deactivated by prostaglandin H2 and peroxides
-
rofecoxib
-
inhibitor of cyclooxygenase COX-2, additionally non-competitive inhibition of prostacyclin synthase
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13-cis-retinoic acid
-
induces prostaglandin-I synthase activity and expression of mRNA and protein, mediated by retinoic acid receptor. Actinomycin and cycloheximide both inhibit the retinoic acid-induced expression. 13-cis-Retinoic acid additionally increases the release of prostaglandin I2, both spontaneous and thrombin-induced. Co-incubation with 13-cis-retinoic acid and interleukin-1beta results in a synergic increase in the release of prostaglandin I2
additional information
-
the extent of prostaglandin I2 production is determined by an appropriate ratio of COX-1/COX-2 to PGIS. Human vascular endothelial cells transfected with a construct that contains COX-1 and prostaglandin-I synthase cDNAs have an equivalent increase in COX-1 and PGIS, and produce a large quantity of prostaglandin-I synthase which is more than 200fold over that produced by untransfected cells
-
additional information
-
constitutive expression of prostaglandin-I synthase and cyclooxygenase-1 in HK cells, while expression of cyclooxygenase-2 and prostaglandin-E synthase are up-regulated in response to tumor necrosis factor-alpha, tumor growth factor-beta, and lipopolysaccharide
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.059
15-hydroperoxyeicosatetraenoic acid
pH 7.5, 23°C, heterolytic cleavage
0.065
15-hydroperoxyeicosatetraenoic acid
pH 7.5, 23°C, homolytic cleavage
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.001
rofecoxib
Homo sapiens
-
22°C, 0.001 mM rofecoxib completely blocks cyclooxygenase COX-2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
46
-
CM column, assayed at 23°C using 30 microM prostaglandin H1 as the substrate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
study on involvement of enzyme polymorphism in adenomatous or hyperplastic colorectal polyps. The enzyme promoter polymorphism may affect risk of colorectal polyps and modify the effects of nonsteroidal anti-inflammatory drug use on polyp risk
-
normal aortic endothelium. Co-distribution of prostaglandin cyclase and cyclooxygenase COX-1, while expression of cyclooxygenase COX-2 is not detected in endothelium
-
constitutive expression of prostaglandin-I synthase and cyclooxygenase-1 in HK cells, while expression of cyclooxygenase-2 and prostaglandin-E synthase are up-regulated in response to tumor necrosis factor-alpha, tumor growth factor-beta, and lipopolysaccharide
-
normal aortic endothelium. Co-distribution of prostaglandin cyclase and cyclooxygenase COX-1, while expression of cyclooxygenase COX-2 is not detected in endothelium
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
one transmembrane segment in the NH2-terminal domain of the enzyme
-
anchors to the membrane with a single N-terminal transmembrane domain, the bulk of the enzyme is located at the cytosolic side of ER
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
PGIS over-expressed mesenchymal stem cells are more resistant to free radical stress-induced apoptosis, secrete paracrine factors to enhance immunemodulation and, thus, provide cardiac protection
malfunction
-
enzyme variant rs5602 is associated with a risk of spontaneous abortion
physiological function
-
the enzyme is critical for the regulation of platelet aggregation and vascular tone
additional information
-
structure-function relationship analysis by a combination of resonance Raman spectroscopy and molecular dynamics simulation approaches using prostaglandin H2 analogues U46619 or (Z)-7-[(1S,4R,5R,6S)-5-[(E,3S)-3-hydroxyoct-1-enyl]-3-oxabicyclo[2.2.1]heptan-6-yl]hept-5-enoic acid, U51605 or 9alpha,11alpha-azoprosta-5Z,13E-dien-1-oic acid, and U44069 or (Z)-7-[(1R,4S,5R,6S)-6-[(E,3S)-3-hydroxyoct-1-enyl]-3-oxabicyclo[2.2.1]heptan-5-yl]hept-5-enoic acid and inhibitors minoxidil, clotrimazole, miconazole, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). PTGIS_HUMAN
500
1
57104
Swiss-Prot
Secretory Pathway (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
48000
57000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
diabetes induces prostacyclin synthase nitration in carotid plaques
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
DELTA-20-PGIS
-
PGH2 presentation to the membrane-bound mutant has a 2 to 3fold delay compared to that of membrane-bound wild-type PGIS
PGIS/TXAS(8-27)
-
the first 20 membrane anchor residues of human PGIS are replaced by the corresponding membrane anchor region of human TXAS (thromboxane A2 synthase). Efficiency of the isomerization of PGH2 to PGI2 is slowed down with approximately 25, 65, and 85% at 30, 60, and 120 s reactions, compared to the wild-type PGIS, respectively
additional information
-
fusion protein linking cyclooxygenase COX-2 and prostacyclin synthase together, separated by a transmembrane domain of 10 or 22 residues. Expressed protein is able to convert arachidonic acid to prostaglandin G2, prostaglandin H2 and prostaglandin I2. Fusion protein may directly synthesize prostaglandin I2 from arachidonic acid with Km value of 0.0032 mM
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Triton X-100
-
within 30 s, about 75% of PGH2 is presented to the PGIS active side and isomerized to PGI2 by the membrane-bound PGIS. In contrast, only about 20% of the substrate is isomerized to the product by the detergent-solubilized (Triton X-100) PGIS. Replacement of the membrane with detergent does not alter the PGIS active side conformation, but affects the substrate presentation
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
human PGIS is significantly unstable when the heme cofactor appears in the reduction and/or reduction-CO binding state
-
662059
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His4-tagged modified enzyme from Escherichia coli strain BL21/(DE3)pLys by nickel affinity chromatography and carboxymethyl cation exchange chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression with C-terminal His-tag and hydrophilic aminoterminal segment MAKKTSS
fusion protein linking cyclooxygenase COX-2 and prostacyclin synthase together, separated by a transmembrane domain of 10 or 22 residues
-
recombinant expression of C-terminally His4-tagged enzyme with the first 17 amino acid residues in the N-terminal transmembrane domain replaced with a hydrophilic sequence, MAKKTSS, in Escherichia coli strain BL21/(DE3)pLys
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression, in terms of mRNA and protein, are lower in tumour samples than in non-tumoural mucosa
-
hyperglycemia and palmitate increase prostacyclin synthase nitration and reduce its activity
-
PGIS mRNA and protein expression is increased in response to mechanical cyclical stretch in both spinal ligament and uterine myometrial cells, up-regulation is observed in umbilical vein endothelial cell treated with a thromboxane analogue
-
the enzyme has enhanced expression mainly in endothelial cells of patients with immunglobulin A nephropathy
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
overexpression of PGIS is highly effective in controlling vascular diseases and ischemia-reperfusion tissue injury, gene transfer of bicistronic COX-1/PGIS has the potential for treatment of diverse clinical disorders including vascular diseases, pulmonary hypertension, and ischemia-reperfusion cerebral and cardiac injury
medicine
-
the enzyme acts as a regulator of thyroid papillary carcinoma proliferation, increased expression levels may play a role in the pathogenesis of these tumors
medicine
-
study on involvement of enzyme polymorphism in adenomatous or hyperplastic colorectal polyps. The enzyme promoter polymorphism may affect risk of colorectal polyps and modify the effects of nonsteroidal anti-inflammatory drug use on polyp risk
medicine
-
upregulation of prostaglandin I2 synthesis by expression of a fusion protein linking cyclooxygenase COX-2 and prostacyclin synthase shows strong activity in inhibiting platelet aggregation induced by arachidonic acid in vitro and may be used for therapeutic inventions for strokes and heart attacks
medicine
-
prostacyclin synthase overexpression apparently protects insulin-producing cells against cytokine toxicity via suppression of endoplasmic reticulum and mitochondrial stress-mediated cell death pathways
medicine
-
tyrosine nitration of prostacyclin synthase is correlated with an excessive inflammatory response in atherosclerotic carotid arteries from patients with type 2 diabetes
medicine
-
co-adjuvant therapy with enzyme enhancers, such as retinoids, has therapeutic value for head and neck squamous cell carcinoma treatment
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
McNamara, D.B.; Hussey, J.L.; Kerstein, M.D.; Rosenson, R.S.; Hyman, A.L.; Kadowitz, P.J.
Modulation of prostacyclin synthetase and unmasking of PGE2 isomerase in bovine coronary arterial microsomes
Biochem. Biophys. Res. Commun.
118
33-39
1984
Bos taurus, Canis lupus familiaris, Ovis aries, Homo sapiens
Lin, Y.Z.; Wu, K.K.; Ruan K.H.
Characterization of the secondary structure and membrane interaction of the putative membrane anchor domains of prostaglandin I2 synthase and cytochrome P450 2C1
Arch. Biochem. Biophys.
352
78-84
1988
Homo sapiens
Tanabe, T.; Ullrich, V.
Prostacyclin and thromboxane synthases
J. Lipid Mediat. Cell Signal.
12
243-255
1995
Homo sapiens, Sus scrofa
Zou, M.; Martin, C.; Ullrich, V.
Tyrosine nitration as a mechanism of selective inactivation of prostacyclin synthase by peroxynitrite
Biol. Chem.
378
707-713
1997
Homo sapiens
Deng, H.; Huang, A.; So, S.P.; Lin, Y.Z.; Ruan, K.H.
Substrate access channel topology in membrane-bound prostacyclin synthase
Biochem. J.
362
545-551
2002
Homo sapiens
Ruan, K.H.; Deng, H.; Wu, J.; So, S.P.
The N-terminal membrane anchor domain of the membrane-bound prostacyclin synthase involved in the substrate presentation of the coupling reaction with cyclooxygenase
Arch. Biochem. Biophys.
435
372-381
2005
Homo sapiens
Wu, K.K.; Liou, J.Y.
Cellular and molecular biology of prostacyclin synthase
Biochem. Biophys. Res. Commun.
338
45-52
2005
Bos taurus, Homo sapiens, Mus musculus
Yeh, H.C.; Hsu, P.Y.; Wang, J.S.; Tsai, A.L.; Wang, L.H.
Characterization of heme environment and mechanism of peroxide bond cleavage in human prostacyclin synthase
Biochim. Biophys. Acta
1738
121-132
2005
Homo sapiens
Wada, M.; Yokoyama, C.; Hatae, T.; Shimonishi, M.; Nakamura, M.; Imai, Y.; Ullrich, V.; Tanabe, T.
Purification and characterization of recombinant human prostacyclin synthase
J. Biochem.
135
455-463
2004
Homo sapiens
Kajita, S.; Ruebel, K.H.; Casey, M.B.; Nakamura, N.; Lloyd, R.V.
Role of COX-2, thromboxane A2 synthase, and prostaglandin I2 synthase in papillary thyroid carcinoma growth
Mod. Pathol.
18
221-227
2005
Homo sapiens
Yeh, H.C.; Tsai, A.L.; Wang, L.H.
Reaction mechanisms of 15-hydroperoxyeicosatetraenoic acid catalyzed by human prostacyclin and thromboxane synthases
Arch. Biochem. Biophys.
461
159-168
2007
Homo sapiens (Q16647), Homo sapiens
Ruan, K.H.; Deng, H.; So, S.P.
Engineering of a protein with cyclooxygenase and prostacyclin synthase activities that converts arachidonic acid to prostacyclin
Biochemistry
45
14003-14011
2006
Homo sapiens
Kawka, D.W.; Ouellet, M.; Hetu, P.; Singer, I.I.; Riendeau, D.
Double-label expression studies of prostacyclin synthase, thromboxane synthase and COX isoforms in normal aortic endothelium
Biochim. Biophys. Acta
1771
45-54
2007
Canis lupus familiaris, Homo sapiens, Rattus norvegicus
Poole, E.M.; Bigler, J.; Whitton, J.; Sibert, J.G.; Potter, J.D.; Ulrich, C.M.
Prostacyclin synthase and arachidonate 5-lipoxygenase polymorphisms and risk of colorectal polyps
Cancer Epidemiol. Biomarkers Prev.
15
502-508
2006
Homo sapiens
Griffoni, C.; Spisni, E.; Strillacci, A.; Toni, M.; Bachschmid, M.M.; Tomasi, V.
Selective inhibition of prostacyclin synthase activity by rofecoxib
J. Cell. Mol. Med.
11
327-338
2007
Bos taurus, Homo sapiens
Lee, I.Y.; Cho, W.; Kim, J.; Park, C.S.; Choe, J.
Human follicular dendritic cells interact with T cells via expression and regulation of cyclooxygenases and prostaglandin E and I synthases
J. Immunol.
180
1390-1397
2008
Homo sapiens
Camacho, M.; Rodriguez, C.; Salazar, J.; Martinez-Gonzalez, J.; Ribalta, J.; Escudero, J.R.; Masana, L.; Vila, L.
Retinoic acid induces PGI synthase expression in human endothelial cells
J. Lipid Res.
49
1707-1714
2008
Homo sapiens
He, C.; Choi, H.C.; Xie, Z.
Enhanced tyrosine nitration of prostacyclin synthase is associated with increased inflammation in atherosclerotic carotid arteries from type 2 diabetic patients
Am. J. Pathol.
176
2542-2549
2010
Homo sapiens
Yeh, H.C.; Gerfen, G.J.; Wang, J.S.; Tsai, A.L.; Wang, L.H.
Characterization of the peroxidase mechanism upon reaction of prostacyclin synthase with peracetic acid. Identification of a tyrosyl radical intermediate
Biochemistry
48
917-928
2009
Homo sapiens (Q16647)
Cathcart, M.C.; Reynolds, J.V.; OByrne, K.J.; Pidgeon, G.P.
The role of prostacyclin synthase and thromboxane synthase signaling in the development and progression of cancer
Biochim. Biophys. Acta
1805
153-166
2010
Homo sapiens
Gurgul-Convey, E.; Lenzen, S.
Protection against cytokine toxicity through endoplasmic reticulum and mitochondrial stress prevention by prostacyclin synthase overexpression in insulin-producing cells
J. Biol. Chem.
285
11121-11128
2010
Homo sapiens
Lian, W.S.; Cheng, W.T.; Cheng, C.C.; Hsiao, F.S.; Chen, J.J.; Cheng, C.F.; Wu, S.C.
In vivo therapy of myocardial infarction with mesenchymal stem cells modified with prostaglandin I synthase gene improves cardiac performance in mice
Life Sci.
88
455-464
2011
Homo sapiens (Q16647)
Chao, W.C.; Lu, J.F.; Wang, J.S.; Yang, H.C.; Chen, H.H.; Lan, Y.K.; Yu, Y.C.; Chou, P.T.; Wang, L.H.
Probing the interaction between prostacyclin synthase and prostaglandin H2 analogues or inhibitors via a combination of resonance Raman spectroscopy and molecular dynamics simulation approaches
J. Am. Chem. Soc.
133
18870-18879
2011
Danio rerio, Homo sapiens
Camacho, M.; Pineiro, Z.; Alcolea, S.; Garcia, J.; Balart, J.; Terra, X.; Aviles-Jurado, F.X.; Soler, M.; Quer, M.; Leon, X.; Vila, L.
Prostacyclin-synthase expression in head and neck carcinoma patients and its prognostic value in the response to radiotherapy
J. Pathol.
235
125-135
2015
Homo sapiens
Yang, H.C.; Yang, C.H.; Huang, M.Y.; Lu, J.F.; Wang, J.S.; Yeh, Y.Q.; Jeng, U.S.
Homology modeling and molecular dynamics simulation combined with X-ray solution scattering defining protein structures of thromboxane and prostacyclin synthases
J. Phys. Chem. B
121
11229-11240
2017
Homo sapiens
Klein, T.; Klaus, G.; Koemhoff, M.
Prostacyclin synthase upregulation during renal development and in glomerular disease as well as its constitutive expression in cultured human mesangial cells
Mediators Inflamm.
2015
654151
2015
Homo sapiens
Sasaki, Y.; Ochiai, T.; Takamura, M.; Kondo, Y.; Yokoyama, C.; Hara, S.
Role of prostacyclin synthase in carcinogenesis
Prostaglandins Other Lipid Mediat.
133
49-52
2017
Homo sapiens
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