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Chemical Compound Review

Tungstic acid     dihydroxy-dioxo-tungsten

Synonyms: Tunstic acid, AG-L-18591, CHEBI:36272, H2WO4, AC1L1AUE, ...
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Disease relevance of dihydroxy-dioxo-tungsten


High impact information on dihydroxy-dioxo-tungsten

  • Binding of tungstate triggers a conformational change that traps the oxyanion and swings Asp 356, an important catalytic residue, by approximately 6 A into the active site [5].
  • We also demonstrate that the SurE protein exhibits a divalent metal ion-dependent phosphatase activity that is inhibited by vanadate or tungstate [6].
  • A tungstate derivative used in the X-ray analysis is a competitive inhibitor and places the active site of fumarase in a region which includes atoms from three of the four subunits [7].
  • These results show a direct involvement of ERK1/2 in the mechanism of action of tungstate at the hepatic level [8].
  • In contrast, at low concentrations, tungstate induced a transient strong activation of extracellular signal-regulated kinases 1 and 2 (ERK1/2) after 5-10 min of treatment, in a similar way to insulin [8].

Chemical compound and disease context of dihydroxy-dioxo-tungsten


Biological context of dihydroxy-dioxo-tungsten


Anatomical context of dihydroxy-dioxo-tungsten

  • In primary cultured hepatocytes, tungstate showed insulin-like actions, which led to an increase in glycogen synthesis and accumulation [8].
  • Stable and functional regeneration of pancreatic beta-cell population in nSTZ-rats treated with tungstate [14].
  • We examined the effects of tungstate administration in the beta-cell mass of the pancreas as well as its therapeutic potential [14].
  • When the antiprogestin [3H]RU486 was used instead of [3H]R5020 as a ligand, a 9 S PR was also found in the cytosol, but a nonactivated "8.5 S" receptor complex was identified in the high salt nuclear fraction in presence of tungstate ions [18].
  • Micrographs of isolated gap junction specimens, negatively stained with one molybdate, three tungstate and three uranyl stains, were recorded at low and high irradiation [19].

Associations of dihydroxy-dioxo-tungsten with other chemical compounds

  • Among the various oxyanions tested, only tungstate replaced molybdate in the repression of modA by ModE, but the affinity of ModE-tungstate for modABCD operator DNA was 6 times lower than with ModE-molybdate [20].
  • The genes tupABC coding for an ABC transporter specific for tungstate were cloned in the downstream region of genes encoding a tungsten-containing formate dehydrogenase [3].
  • Transformation brought about at 0 degrees C by salt, ammonium sulfate precipitation, or gel filtration is also blocked by both molybdate and tungstate [21].
  • Stabilization with tungstate and/or cross-linking permitted immunoaffinity purification of untransformed rabbit as well as calf PR and ER on EC1-Affi-Gel 10 column (an anti-p59 immunoadsorbant) [22].
  • On the other hand, both molybdate and tungstate increase fructose 2,6-bisphosphate levels and counteract the decrease in this metabolite induced by glucagon [23].

Gene context of dihydroxy-dioxo-tungsten

  • Experiments with a specific inhibitor of ERK1/2 activation and kinase assays indicate that these proteins were directly involved in the stimulation of glycogen synthase and glycogen synthesis induced by tungstate without a direct involvement of protein kinase B (PKB/Akt) [8].
  • Herein, we report the 1.9 A X-ray crystal structures of a member of the third subclass, magnesium-dependent phosphatase-1 (MDP-1) both in its unliganded form and with the product analogue, tungstate, bound to the active site [24].
  • The modEABC operon was also repressed by tungstate and to a lesser extent by vanadate. modE, the first gene in the modEABC operon, controlled the Mo-dependent transcription of both operons [25].
  • Transition metal oxyanions, such as molybdate, tungstate and vandadate, have been shown to prevent in vitro hormone-induced activation of the glucocorticoid receptor (GR) by blocking dissociation of the GR/heat shock protein heterocomplex [26].
  • The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins [27].

Analytical, diagnostic and therapeutic context of dihydroxy-dioxo-tungsten

  • As observed for the tungstate-stabilized receptor, the cross-linked receptor dissociated neither on gradient containing 0.4 M KCl (9.5 +/- 0.1 S (n = 3] nor during HPLC performed in 0.4 M KCl (RS = 6.5 +/- 0.3 (n = 4] [28].
  • Oral administration of tungstate for 15 days normalized glycaemia in these diabetic animals (4.6 vs 7.8 mmol/l) [29].
  • Aortic occlusion was established in rabbits (standard or tungstate diet) for 40 min by 2 h reperfusion [30].
  • One hundred patients underwent excretory urography and a comparison was made of ten-minute, well-collimated images that were obtained with both par-speed and rare-earth screens, the latter being 6.5 times faster than the par-speed calcium tungstate screens [31].
  • Using isothermal titration calorimetry, WtpA was observed to bind tungstate (dissociation constant [K(D)] of 17 +/- 7 pM) and molybdate (K(D) of 11 +/- 5 nM) with a stoichiometry of 1.0 mol oxoanion per mole of protein [32].


  1. Effects of tungstate, a new potential oral antidiabetic agent, in Zucker diabetic fatty rats. Muñoz, M.C., Barberà, A., Domínguez, J., Fernàndez-Alvarez, J., Gomis, R., Guinovart, J.J. Diabetes (2001) [Pubmed]
  2. The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications. Fauman, E.B., Yuvaniyama, C., Schubert, H.L., Stuckey, J.A., Saper, M.A. J. Biol. Chem. (1996) [Pubmed]
  3. Tungstate Uptake by a highly specific ABC transporter in Eubacterium acidaminophilum. Makdessi, K., Andreesen, J.R., Pich, A. J. Biol. Chem. (2001) [Pubmed]
  4. Molybdenum cofactor requirement for in vitro activation of apo-molybdoenzymes of Escherichia coli. Giordano, G., Boxer, D.H., Pommier, J. Mol. Microbiol. (1990) [Pubmed]
  5. Crystal structure of Yersinia protein tyrosine phosphatase at 2.5 A and the complex with tungstate. Stuckey, J.A., Schubert, H.L., Fauman, E.B., Zhang, Z.Y., Dixon, J.E., Saper, M.A. Nature (1994) [Pubmed]
  6. Crystal structure and functional analysis of the SurE protein identify a novel phosphatase family. Lee, J.Y., Kwak, J.E., Moon, J., Eom, S.H., Liong, E.C., Pedelacq, J.D., Berendzen, J., Suh, S.W. Nat. Struct. Biol. (2001) [Pubmed]
  7. The multisubunit active site of fumarase C from Escherichia coli. Weaver, T.M., Levitt, D.G., Donnelly, M.I., Stevens, P.P., Banaszak, L.J. Nat. Struct. Biol. (1995) [Pubmed]
  8. The antidiabetic agent sodium tungstate activates glycogen synthesis through an insulin receptor-independent pathway. Domínguez, J.E., Muñoz, M.C., Zafra, D., Sanchez-Perez, I., Baqué, S., Caron, M., Mercurio, C., Barberà, A., Perona, R., Gomis, R., Guinovart, J.J. J. Biol. Chem. (2003) [Pubmed]
  9. Inhibition of phosphatase and sulfatase by transition-state analogues. Stankiewicz, P.J., Gresser, M.J. Biochemistry (1988) [Pubmed]
  10. Sulfonates as terminal electron acceptors for growth of sulfite-reducing bacteria (Desulfitobacterium spp.) and sulfate-reducing bacteria: effects of inhibitors of sulfidogenesis. Lie, T.J., Godchaux, W., Leadbetter, E.R. Appl. Environ. Microbiol. (1999) [Pubmed]
  11. Mitochondrial electron transport as a source for nitric oxide in the unicellular green alga Chlorella sorokiniana. Tischner, R., Planchet, E., Kaiser, W.M. FEBS Lett. (2004) [Pubmed]
  12. Influence of tungstate on the formation and activities of four reductases in Proteus mirabilis: identification of two new molybdo-enzymes: chlorate reductase and tetrathionate reductase. Oltmann, L.F., Claassen, V.P., Kastelein, P., Reijnders, W.N., Stouthamer, A.H. FEBS Lett. (1979) [Pubmed]
  13. Crystal structure of the catalytic domain of protein-tyrosine phosphatase SHP-1. Yang, J., Liang, X., Niu, T., Meng, W., Zhao, Z., Zhou, G.W. J. Biol. Chem. (1998) [Pubmed]
  14. Stable and functional regeneration of pancreatic beta-cell population in nSTZ-rats treated with tungstate. Fernández-Alvarez, J., Barberà, A., Nadal, B., Barceló-Batllori, S., Piquer, S., Claret, M., Guinovart, J.J., Gomis, R. Diabetologia (2004) [Pubmed]
  15. Tungstate decreases weight gain and adiposity in obese rats through increased thermogenesis and lipid oxidation. Claret, M., Corominola, H., Canals, I., Saura, J., Barcelo-Batllori, S., Guinovart, J.J., Gomis, R. Endocrinology (2005) [Pubmed]
  16. Interaction of porcine uterine fluid purple acid phosphatase with vanadate and vanadyl cation. Crans, D.C., Simone, C.M., Holz, R.C., Que, L. Biochemistry (1992) [Pubmed]
  17. Kinetic evidence for a substrate-induced fit in phosphonoacetaldehyde hydrolase catalysis. Zhang, G., Mazurkie, A.S., Dunaway-Mariano, D., Allen, K.N. Biochemistry (2002) [Pubmed]
  18. Estrogen-inducible progesterone receptor in primary cultures of rat glial cells. Jung-Testas, I., Renoir, J.M., Gasc, J.M., Baulieu, E.E. Exp. Cell Res. (1991) [Pubmed]
  19. Gap junction structures. VII. Analysis of connexon images obtained with cationic and anionic negative stains. Baker, T.S., Sosinsky, G.E., Caspar, D.L., Gall, C., Goodenough, D.A. J. Mol. Biol. (1985) [Pubmed]
  20. An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli. Grunden, A.M., Self, W.T., Villain, M., Blalock, J.E., Shanmugam, K.T. J. Biol. Chem. (1999) [Pubmed]
  21. Molybdate inhibition of glucocorticoid receptor inactivation and transformation. Leach, K.L., Dahmer, M.K., Hammond, N.D., Sando, J.J., Pratt, W.B. J. Biol. Chem. (1979) [Pubmed]
  22. The non-DNA-binding heterooligomeric form of mammalian steroid hormone receptors contains a hsp90-bound 59-kilodalton protein. Renoir, J.M., Radanyi, C., Faber, L.E., Baulieu, E.E. J. Biol. Chem. (1990) [Pubmed]
  23. Molybdate and tungstate act like vanadate on glucose metabolism in isolated hepatocytes. Fillat, C., Rodríguez-Gil, J.E., Guinovart, J.J. Biochem. J. (1992) [Pubmed]
  24. X-ray crystal structure of the hypothetical phosphotyrosine phosphatase MDP-1 of the haloacid dehalogenase superfamily. Peisach, E., Selengut, J.D., Dunaway-Mariano, D., Allen, K.N. Biochemistry (2004) [Pubmed]
  25. The modE gene product mediates molybdenum-dependent expression of genes for the high-affinity molybdate transporter and modG in Azotobacter vinelandii. Mouncey, N.J., Mitchenall, L.A., Pau, R.N. Microbiology (Reading, Engl.) (1996) [Pubmed]
  26. Vanadate increases glucocorticoid receptor-mediated gene expression: a novel mechanism for potentiation of a steroid receptor. Li Calzi, S., Periyasamy, S., Li, d.a. .P., Sánchez, E.R. J. Steroid Biochem. Mol. Biol. (2002) [Pubmed]
  27. Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate. Stavridi, E.S., Huyen, Y., Loreto, I.R., Scolnick, D.M., Halazonetis, T.D., Pavletich, N.P., Jeffrey, P.D. Structure (Camb.) (2002) [Pubmed]
  28. Mineralocorticosteroid receptor of the chick intestine. Oligomeric structure and transformation. Rafestin-Oblin, M.E., Couette, B., Radanyi, C., Lombes, M., Baulieu, E.E. J. Biol. Chem. (1989) [Pubmed]
  29. Effects of tungstate in neonatally streptozotocin-induced diabetic rats: mechanism leading to normalization of glycaemia. Barberà, A., Fernàndez-Alvarez, J., Truc, A., Gomis, R., Guinovart, J.J. Diabetologia (1997) [Pubmed]
  30. Lung injury after hepatoenteric ischemia-reperfusion: role of xanthine oxidase. Nielsen, V.G., Tan, S., Weinbroum, A., McCammon, A.T., Samuelson, P.N., Gelman, S., Parks, D.A. Am. J. Respir. Crit. Care Med. (1996) [Pubmed]
  31. Clinical comparison of high-speed rare-earth screen and par-speed screen for diagnostic efficacy and radiation dosage. Robinson, T., Becker, J.A., Olson, A.P. Radiology. (1982) [Pubmed]
  32. Tungsten transport protein A (WtpA) in pyrococcus furiosus: the first member of a new class of tungstate and molybdate transporters. Bevers, L.E., Hagedoorn, P.L., Krijger, G.C., Hagen, W.R. J. Bacteriol. (2006) [Pubmed]
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