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Information on EC 3.5.1.92 - pantetheine hydrolase and Organism(s) Mus musculus and UniProt Accession Q9Z0K8
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3.5.1.92 pantetheine hydrolaseIUBMB Comments
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant .
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Word Map
- 3.5.1.92
- cysteamine
-
pantothen
-
gpi-anchored
-
ectoenzyme
- pantothenamides
-
gelatinase-associated
-
walter
-
aminothiol
- pantethine
- biotinidase
-
julius
- medicine
- diagnostics
- drug development
The taxonomic range for the selected organisms is: Mus musculus
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
vanin-1, pantetheinase, gpi-80, vanin, pagel, vanin 1, pantetheinases, vanin-3, vanin-2, vascular noninflammatory molecule 1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
vanin-1
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
(R)-pantetheine amidohydrolase
The enzyme hydrolyses only one of the amide bonds of pantetheine. The substrate analogues phosphopantetheine and CoA are not substrates. The enzyme recycles pantothenate (vitamin B5) and produces 2-aminoethanethiol (cysteamine), a potent anti-oxidant [5].
CAS REGISTRY NUMBER
COMMENTARY
56093-18-6
-
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
(R)-pantetheine + H2O
(R)-pantothenate + 2-aminoethanethiol
-
-
-
?
2-(6-[[N-(2,4-dihydroxy-3,3-dimethylbutanoyl)-beta-alanyl]amino]-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-5-carboxylic acid + H2O
2-(6-amino-1,3-benzothiazol-2-yl)-4,5-dihydro-1,3-thiazole-5-carboxylic acid + N-(2,4-dihydroxy-3,3-dimethylbutanoyl)-beta-alanine
design, synthesis, and biological examination of a highly sensitive bioluminogenic probe for pantetheinase with a limit of detection of 1.14 ng/ml. Validation of the probe for application to detect the endogenous pantetheinase activity, overview
-
-
ir
pantothenate-7-amido-4-methylcoumarin + H2O
pantothenic acid + 7-amino-4-methylcoumarin
-
-
based on LC-MS analysis
-
?
additional information
?
-
-
membrane-bound pantetheinase is the main source of cysteamine in tissues under physiological conditions. The enzyme might by involved in the regulation of some immune functions maybe in the context of the response to oxidative stress
-
-
?
additional information
?
-
-
the transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development. The sex- and cell-type-specific expression of vanin-1 in the developing mpouse gonad in vivo is required to provide an appropriate environment for male germ cell development
-
-
?
additional information
?
-
-
the vanin-1 gene is involved in testis development in mouse
-
-
?
additional information
?
-
-
vanin-1 is a key molecule to regulate the GSH-dependent response to oxidative injury in tissue at the epithelial level
-
-
?
additional information
?
-
-
vanin-1 plays a role in thymic reconstitution following damage by irradiation
-
-
?
additional information
?
-
-
vanin-1 regulates late adhesion steps of thymus homing under physiological, noninflammatory conditions
-
-
?
additional information
?
-
-
vanin-1-/- mice are less susceptible to intestinal inflammation, either acute or chronic. Pantetheinase activity of vanin-1 is a major regulator of intestinal inflammation, acting through cysteamine release
-
-
?
additional information
?
-
-
vanin-1 controls granuloma formation and macrophage polarization in Coxiella burnetii infection
-
-
?
additional information
?
-
-
vanin-1 is cytoprotective for islet beta cells and regulates the development of type 1 diabetes
-
-
?
additional information
?
-
-
vanin-1 regulates chondrogenesis via glutathione metabolism and is critical for accelerated chondrogenesis of ank/anf mesenchymal precursors and phosphate donor-driven chondrogenic transdifferentiation and calcification of aortic smooth muscle cells
-
-
?
additional information
?
-
-
vanin-1, by antagonizing PPARgamma, licenses the production of inflammatory mediators by intestinal epithelial cells
-
-
?
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
(R)-pantetheine + H2O
(R)-pantothenate + 2-aminoethanethiol
-
-
-
?
additional information
?
-
-
membrane-bound pantetheinase is the main source of cysteamine in tissues under physiological conditions. The enzyme might by involved in the regulation of some immune functions maybe in the context of the response to oxidative stress
-
-
?
additional information
?
-
-
the transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development. The sex- and cell-type-specific expression of vanin-1 in the developing mpouse gonad in vivo is required to provide an appropriate environment for male germ cell development
-
-
?
additional information
?
-
-
the vanin-1 gene is involved in testis development in mouse
-
-
?
additional information
?
-
-
vanin-1 is a key molecule to regulate the GSH-dependent response to oxidative injury in tissue at the epithelial level
-
-
?
additional information
?
-
-
vanin-1 plays a role in thymic reconstitution following damage by irradiation
-
-
?
additional information
?
-
-
vanin-1 regulates late adhesion steps of thymus homing under physiological, noninflammatory conditions
-
-
?
additional information
?
-
-
vanin-1-/- mice are less susceptible to intestinal inflammation, either acute or chronic. Pantetheinase activity of vanin-1 is a major regulator of intestinal inflammation, acting through cysteamine release
-
-
?
additional information
?
-
-
vanin-1 controls granuloma formation and macrophage polarization in Coxiella burnetii infection
-
-
?
additional information
?
-
-
vanin-1 is cytoprotective for islet beta cells and regulates the development of type 1 diabetes
-
-
?
additional information
?
-
-
vanin-1 regulates chondrogenesis via glutathione metabolism and is critical for accelerated chondrogenesis of ank/anf mesenchymal precursors and phosphate donor-driven chondrogenic transdifferentiation and calcification of aortic smooth muscle cells
-
-
?
additional information
?
-
-
vanin-1, by antagonizing PPARgamma, licenses the production of inflammatory mediators by intestinal epithelial cells
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
RR6
shows high specificity towards vanin 1 and competitively and reversibly inhibits pantetheinase activity at nanomolar concentration
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics and Lineweaver-Burk plots
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
comparisons of healthy with Malaria red blood cells
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
mice injected i.p. with 106 Plasmodium berghei ANKA infected red blood cells
UniProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
vanin 1 expression specifically by the centrilobular hepatocytes in zone 3 adjacent to the central vein
-
epithelium. Vanin-1 controls the inflammatory response in injured colon. Vanin-1 regulates the expression of PPARgamma in epithelial cells
additional information
pantetheinase is a glycosylphosphatidylinositol (GPI) anchored enzyme, overexpressed in intestine, liver, and kidney
-
higher level in kidney than in liver, similar expression in lung, determined by RT-PCR
-
the transcription factors steroidogenic factor-1 and SOX9 regulate expression of vanin-1 during mouse testis development
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
pantetheinase is an ectoenzyme that is attached to the outer plasma membrane by a glycosylphosphatidylinositol (GPI) anchor. GPI anchors consist of three domains: a phosphoethanolamine linker that attaches to the C terminal end of the target protein, a conserved glycan core and a phospholipid tail for anchoring to the lipid membrane
additional information
vanin 1 is membrane-associated via a glycosylphosphatidylinositol (GPI)-anchor, though soluble enzyme forms are detected as well
-
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
-
vanin 1 knockout mice display an enhanced resistance to oxidative stress and show down-regulated tissue inflammation in response to oxidative stress. Vanin knockout mice exhibit a loss of cysteamine-mediated inhibition of peroxisome proliferator-activated receptor gamma. Vanin 1 deficient islets are twice as susceptible to cell death as wild type cells
physiological function
-
vanin plays a role in inflammation, oxidative stress, cell migration and numerous diseases including cardiovascular disease (increased vanin 1 activity has a protective effect against cardiovascular disease). Vanin 1 has a cytoprotective effect against type 1 diabetes in islet cells. Vanin 1 is a central regulator of not only stress responses via production of cysteamine but also lipid biosynthesis by controlling the flux through the fatty acid and/or cholesterol biosynthetic pathways
malfunction
evaluation of the effects of the inactivation of vnn1 on the development of fibrosis, endothelial alterations, and immunological activation in mice with HOCl- and bleomycin-induced systemic sclerosis (SSc). The vanin-1/pantetheinase pathway is activated in wild-type BALB/c mice through hypochlorous acid (HOCl)-induced SSc. Hyperactivity of the vanin-1/pantetheinase pathway may reduce the vasculoprotective effects of pantethine, while genetic inactivation of vanin-1 has a protective effect
malfunction
mutant mice with a reduced serum pantetheinase activity are anemic and prone to phenylhydrazine-induced anemia. A cytofluorometric and spectroscopic analysis documents an increased frequency of erythrocytes with an autofluorescent aging phenotype. This is associated with an enhanced oxidative stress and shear stress-induced hemolysis. Red blood cell transfer and bone marrow chimera experiments show that the aging phenotype is not cell intrinsic but conferred by the environment, leading to a shortening of red blood cell half-life. Phenotype analysis, detailed overview
malfunction
PPAR-alpha KO mice show a negligible liver vnn1 expression, even after stimulation with various agonists. Vanin 1 overexpression increases glucose output by specifically increasing the hepatic transcription levels of gluconeogenic genes, while vnn1 knockdown decreases the glucose output of murine hepatocytes
malfunction
Vnn1 deficiency favors soft tissue sarcoma development in p16/p19-/- mice
metabolism
enzyme Vnn1 is a valid biomarker for aggressive soft tissue sarcomas (STS) prognosis. Analysis of a route to regulate tumor growth rates through the modulation of CoA and cysteamine levels
metabolism
formation of pantothenic acid allows for a continuous production of CoA, as pantothenic acid is a structural component of this cofactor. In addition, pantothenic acid appears to have profibrotic effects, being involved in the promotion of proliferation and migration of dermal fibroblasts. Moreover, pantothenic acid contributes to restoring CoA levels in the mitochondria, resulting in enhanced mitochondrial activity. Vanin 1 also plays a role in the regulation of a number of metabolic pathways. In fact, the vnn1 gene is one of the positive targets of the peroxisome proliferator-activated receptor alpha (PPAR-alpha) in mouse liver. PPAR-alpha is a key regulator of the liver's response to fasting
metabolism
inactivation of vnn1 on the development of fibrosis, endothelial alterations, and immunological activation in mice with HOCl- and bleomycin-induced systemic sclerosis (SSc)
metabolism
the availability of free cysteamine is also regulated by hydrolysis of pantetheine by pantetheinase. This cleavage results in the formation of pantothenic acid, a precursor to coenzyme A which is prominently involved with lipid metabolism and energy production by the beta-oxidation pathway and TCA cycle, respectively. Expression of pantetheinase is controlled by the Vnn1 gene and is upregulated in response to free fatty acids, PPAR activation or oxidative stress. Vanin-1 is believed to be the primary transcript responsible for pantetheinase activity. Successful attachment of GPI following its synthesis in the endoplasmic reticulum (ER) requires two signal sequences within the protein. The first is an N terminal signal peptide (amino acids 1-21 of human pantetheinase) that retains the target protein within the ER lumen. The second necessary sequence is a C-terminal 22 amino acid propeptide downstream of the Gly491 residue, termed the omega site, which is removed and replaced by the GPI anchor. This process is mediated by a GPI-transamidase complex composed mainly of members of the phosphatidylinositol glycan (PIG) family, including PIG-K, the catalytic subunit
physiological function
pantetheinase hydrolyzes pantetheine to pantothenic acid (Vitamin B5) in a reaction that cleaves cysteamine from the pantetheine molecule. Pantetheinase activity regulates the availability of pantothenic acid and cysteamine which are involved in several critical pathways of cell homeostasis including lipid catabolism, synthesis of cholesterol, taurine and NADH as well as maintenance of cellular redox balance. Vascular non-inflammatory molecule 1 (Vanin 1 or Vnn1) modulates redox and immune pathways in vivo, both of which appear at least partially due to a loss of cysteamine/cystamine. Vnn1 expression may influence cell signaling indirectly through maintenance of disulfide bonds or directly by interaction with pantetheinase on the cell surface. Involvement of vanin-1 and pantetheinase in liver homeostasis. Pantetheinase activity can directly influence lipid metabolism, the effects are due to decreased availability of pantothenic acid, resulting in suppression of CoA activity. Pantetheinase likely acts as a regulator of CoA-dependent metabolism by controlling the availability of pantothenic acid in liver. Pantetheinase-mediated catalysis is the main source of endogenous cysteamine in mice. Pantetheinase activity might be protective by augmenting the availability of taurine
physiological function
pantetheinase is a glycosylphosphatidylinositol (GPI) anchored enzyme, overexpressed in intestine, liver, and kidney with various biological functions such as its linkage to the inflammation and some metabolic diseases. It can hydrolyze pantetheine to cysteamine, an antioxidant, and pantothenic acid (vitamin B5) that is an essential component of coenzyme A (CoA). Starvation induces pantetheinase upregulation
physiological function
the vanin-1 gene (vnn1) encodes an enzyme with pantetheinase activity that converts vasculoprotective pantethine into profibrotic pantothenic acid and pro-oxidant cystamine. By hydrolyzation of pantethine, vanin-1 delivers cysteamine and pantothenic acid to tissues. Cysteamine is rapidly converted into cystamine that can regulate the function of other target proteins by a disulfide reaction. In particular, cystamine abrogates glutathione (GSH) production by inhibiting gamma-glutamyl synthase, the rate-limiting enzyme of GSH synthesis, thus strongly reducing reactive oxygen species (ROS) scavenging. In contrast, pantothenic acid, the other by-product of vanin-1, exerts profibrotic effects by promoting the proliferation and migration of dermal fibroblasts, as well as collagen synthesis
physiological function
tissue pantetheinase, encoded by the VNN1 gene, regulates response to stress. VNN genes contribute to the susceptibility to malaria. Serum pantetheinase contributes to erythrocyte resistance to stress under homeostatic conditions. Serum pantetheinase level regulates erythrocyte life span and modulates the risk of developing complicated malaria
physiological function
vanin 1 breaks down pantetheine in cysteamine and pantothenic acid, a precursor of coenzyme A. Its physiological role is not strictly related to coenzyme A metabolism, lipid metabolism, and energy production. It also plays a role under physiological conditions in relation to oxidative stress and inflammation. Vanin's enzymatic activity is of key importance in certain diseases, either for its protective effect or as a sensitizer, depending on the diseased organ. But vanin-1's primary function is the recycling of pantothenic acid (vitamin B5), an important precursor in the biosynthesis of coenzymeA (CoA). Vanin 1 also plays a role in the regulation of a number of metabolic pathways. Gene vnn1 directly regulates PPAR-alpha mRNA expression in gut epithelial. Vanin 1 is an activator of hepatic gluconeogenesis in mice. Role of vanin 1 in diseases of organs in which it is highly expressed (liver, kidney, intestine, lung), detailed overview
physiological function
Vnn1 pantetheinase acts as a tumor suppressor for the development of aggressive soft tissue sarcomas (STS). The two products of pantetheinase activity exert complementary effects on the tumor, explaining the basis for Vnn1's suppression on tumor growth. Pantothenate production restores CoA levels leading to an enhanced mitochondrial activity, whereas cysteamine reduces glycolysis and prevents the transition to the Warburg effect, a feature of the most aggressive tumors. Vnn1 expression antagonizes the glycolytic switch in Ras-driven tumors. Vnn1 expression antagonizes the glycolytic switch in Ras-driven tumors
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). VNN1_MOUSE
512
0
57091
Swiss-Prot
Secretory Pathway (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
construction of in p16/p19-/- mutant mice. Comparison of mouse survival and tumor incidence in three independent cohorts of p16/p19/Vnn1-/- versus p16/p19-/- mice, derived from two independently derived crosses between p16/p19-/- and Vnn1-/- mice. Whereas 35% p16p19-/- mice progressively develop lethal tumors within 220 days, 70% p16p19/Vnn1-/- die of aggressive tumors before 220 days. Whereas p16p19-/- mice develop various tumor types with a majority of lymphomas, p16/p19/Vnn1-/- mice predominantly develop skin STS typed as fibrosarcomas
additional information
development of vnn1 KO mice, which do not have an obvious spontaneous phenotype, they are resistant to inflammation and oxidative stress, thus indisputably proving a correlation between vanin 1, its pantetheinase activity and pro-inflammatory mediators
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of pantetheinase is controlled by the Vnn1 gene and is upregulated in response to free fatty acids, PPAR activation or oxidative stress. PPARalpha-mediated upregulation of Vnn1 translates to enhanced pantetheinase activity in vivo
inactivation of vnn1 on the development of fibrosis, endothelial alterations, and immunological activation in mice with HOCl- and bleomycin-induced systemic sclerosis (SSc)
PPAR-alpha KO mice show a negligible liver vnn1 expression, even after stimulation with various agonists
upon administration of the PPAR-alpha agonists fenofibrate, clofibrate, or Wy-14,643, gene vnn1 expression is increased. The transcription of vnn1 itself is activated by PPAR-alpha coactivator 1 (PGC-1) in complex with the hepatocyte nuclear factor-4alpha (HNF-4alpha). In turn, this complex is mediated by the Akt signaling pathway
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
medicine
diagnostics
enzyme Vnn1 is a valid biomarker for aggressive soft tissue sarcomas (STS) prognosis
diagnostics
potential use of vanin-1 as a marker of severity and therapeutic target in systemic sclerosis (SSc)
medicine
-
the pantetheinase activity of vanin-1 molecule could be a target for a new anti-inflammatory strategy
medicine
-
manipulation the Vanin-1/pantetheinase activity represents an attractive therapeutic strategy for the treatment of inflammatory bowel disease
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maras, B.; Barra, D.; Dupre, S.; Pitari, G.
Is pantetheinase the actual identity of mouse and human vanin-1 proteins?
FEBS Lett.
461
149-152
1999
Mus musculus, Sus scrofa
Pitari, G.; Malergue, F.; Martin, F.; Philippe, J.M.; Massucci, M.T.; Chabret, C.; Maras, B.; Dupre, S.; Naquet, P.; Galland, F.
Pantetheinase activity of membrane-bound vanin-1: lack of free cysteamine in tissues of vanin-1 deficient mice
FEBS Lett.
483
149-154
2000
Mus musculus
Bowles, J.; Bullejos, M.; Koopman, P.
A subtractive gene expression screen suggests a role for vanin-1 in testis development in mice
Genesis
27
124-135
2000
Mus musculus
Aurrand-Lions, M.; Galland, F.; Bazin, H.; Zakharyev, V.M.; Imhof, B.A.; Naquet, P.
Vanin-1, a novel GPI-linked perivascular molecule involved in thymus homing
Immunity
5
391-405
1996
Mus musculus
Martin, F.; Malergue, F.; Pitari, G.; Philippe, J.M.; Philips, S.; Chabret, C.; Granjeaud, S.; Mattei, M.G.; Mungall, A.J.; Naquet, P.; Galland, F.
Vanin genes are clustered (human 6q22-24 and mouse 10A2B1) and encode isoforms of pantetheinase ectoenzymes
Immunogenetics
53
296-306
2001
Mus musculus
Wilson, M.J.; Jeyasuria, P.; Parker, K.L.; Koopman, P.
The transcription factors steroidogenic factor-1 and SOX9 regulate expression of Vanin-1 during mouse testis development
J. Biol. Chem.
280
5917-5923
2005
Mus musculus
Martin, F.; Penet, M.F.; Malergue, F.; Lepidi, H.; Dessein, A.; Galland, F.; de Reggi, M.; Naquet, P.; Gharib, B.
Vanin-1(-/-) mice show decreased NSAID- and Schistosoma-induced intestinal inflammation associated with higher glutathione stores
J. Clin. Invest.
113
591-597
2004
Mus musculus
Berruyer, C.; Martin, F.M.; Castellano, R.; Macone, A.; Malergue, F.; Garrido-Urbani, S.; Millet, V.; Imbert, J.; Dupre, S.; Pitari, G.; Naquet, P.; Galland, F.
Vanin-1-/- mice exhibit a glutathione-mediated tissue resistance to oxidative stress
Mol. Cell. Biol.
24
7214-7224
2004
Mus musculus
Johnson, K.A.; Yao, W.; Lane, N.E.; Naquet, P.; Terkeltaub, R.A.
Vanin-1 pantetheinase drives increased chondrogenic potential of mesenchymal precursors in ank/ank mice
Am. J. Pathol.
172
440-453
2008
Mus musculus
Roisin-Bouffay, C.; Castellano, R.; Valero, R.; Chasson, L.; Galland, F.; Naquet, P.
Mouse vanin-1 is cytoprotective for islet beta cells and regulates the development of type 1 diabetes
Diabetologia
51
1192-1201
2008
Mus musculus
Meghari, S.; Berruyer, C.; Lepidi, H.; Galland, F.; Naquet, P.; Mege, J.L.
Vanin-1 controls granuloma formation and macrophage polarization in Coxiella burnetii infection
Eur. J. Immunol.
37
24-32
2007
Mus musculus
Berruyer, C.; Pouyet, L.; Millet, V.; Martin, F.M.; LeGoffic, A.; Canonici, A.; Garcia, S.; Bagnis, C.; Naquet, P.; Galland, F.
Vanin-1 licenses inflammatory mediator production by gut epithelial cells and controls colitis by antagonizing peroxisome proliferator-activated receptor gamma activity
J. Exp. Med.
203
2817-2827
2006
Mus musculus
Ruan, B.H.; Cole, D.C.; Wu, P.; Quazi, A.; Page, K.; Wright, J.F.; Huang, N.; Stock, J.R.; Nocka, K.; Aulabaugh, A.; Krykbaev, R.; Fitz, L.J.; Wolfman, N.M.; Fleming, M.L.
A fluorescent assay suitable for inhibitor screening and vanin tissue quantification
Anal. Biochem.
399
284-292
2010
Homo sapiens, Mus musculus
Kaskow, B.J.; Michael Proffit, J.; Blangero, J.; Moses, E.K.; Abraham, L.J.
Diverse biological activities of the vascular non-inflammatory molecules - the Vanin pantetheinases
Biochem. Biophys. Res. Commun.
417
653-658
2012
Homo sapiens, Mus musculus
Rommelaere, S.; Millet, V.; Rihet, P.; Atwell, S.; Helfer, E.; Chasson, L.; Beaumont, C.; Chimini, G.; Sambo, M.d.o. .R.; Viallat, A.; Penha-Goncalves, C.; Galland, F.; Naquet, P.
Serum pantetheinase/vanin levels regulate erythrocyte homeostasis and severity of malaria
Am. J. Pathol.
185
3039-3052
2015
Homo sapiens (O95497), Homo sapiens, Mus musculus (Q9Z0K8), Mus musculus, Mus musculus C57BL/6 (Q9Z0K8)
Lin, Y.; Gao, Y.; Ma, Z.; Li, Z.; Tang, C.; Qin, X.; Zhang, Z.; Wang, G.; Du, L.; Li, M.
Bioluminescent probe for detection of starvation-induced pantetheinase upregulation
Anal. Chem.
90
9545-9550
2018
Mus musculus (Q9Z0K8)
Ferreira, D.W.; Naquet, P.; Manautou, J.E.
Influence of vanin-1 and catalytic products in liver during normal and oxidative stress conditions
Curr. Med. Chem.
22
2407-2416
2015
Mus musculus (Q9Z0K8), Mus musculus C57BL/6 (Q9Z0K8)
Bartucci, R.; Salvati, A.; Olinga, P.; Boersma, Y.L.
Vanin 1 its physiological function and role in diseases
Int. J. Mol. Sci.
20
E3891
2019
Rattus norvegicus, Sus scrofa (Q9BDJ5), Mus musculus (Q9Z0K8)
Kavian, N.; Mehlal, S.; Marut, W.; Servettaz, A.; Giessner, C.; Bourges, C.; Nicco, C.; Chereau, C.; Lemarechal, H.; Dutilh, M.F.; Cerles, O.; Guilpain, P.; Vuiblet, V.; Chouzenoux, S.; Galland, F.; Quere, I.; Weill, B.; Naquet, P.; Batteux, F.
Imbalance of the vanin-1 pathway in systemic sclerosis
J. Immunol.
197
3326-3335
2016
Mus musculus (Q9Z0K8), Mus musculus BALB/c (Q9Z0K8)
Giessner, C.; Millet, V.; Mostert, K.J.; Gensollen, T.; Vu Manh, T.P.; Garibal, M.; Dieme, B.; Attaf-Bouabdallah, N.; Chasson, L.; Brouilly, N.; Laprie, C.; Lesluyes, T.; Blay, J.Y.; Shintu, L.; Martin, J.C.; Strauss, E.; Galland, F.; Naquet, P.
Vnn1 pantetheinase limits the Warburg effect and sarcoma growth by rescuing mitochondrial activity
Life Sci. Alliance
1
e201800073
2018
Mus musculus (Q9Z0K8)
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