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Gene Review

Tst  -  thiosulfate sulfurtransferase, mitochondrial

Mus musculus

Synonyms: Rhodanese, Thiosulfate sulfurtransferase
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Disease relevance of Tst


Psychiatry related information on Tst


High impact information on Tst

  • MKP-7 possesses a long C-terminal stretch containing both a nuclear export signal and a nuclear localization signal, in addition to the rhodanese-like domain and the dual specificity phosphatase catalytic domain, both of which are conserved among MKP family members [6].
  • On the other hand, Arg185, Arg247, and Lys248 of rat rhodanese are critical residues in determining substrate specificity for thiosulfate [7].
  • Sequence identity in cDNA and the deduced amino acid sequence are 65 and 60% respectively, between rat MST and rhodanese [7].
  • In this study, we adapted a UV photolabeling approach, using an apolar fluorescent probe, 4,4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid (BisANS), to monitor changes in surface hydrophobic domains in either purified rhodanese or skeletal muscle cytosolic proteins by urea-induced unfolding or in response to in vitro metal-catalyzed oxidation [8].
  • We demonstrated differences in the kinetics for rhodanese derived from mitochondrial and cytoplasmic fractions of livers taken from tumor bearing mice [9].

Biological context of Tst

  • The full-length cDNA corresponding to the mouse rhodanese gene (Tst), which is located on chromosome 15, was cloned by PCR amplification of a liver cDNA library and subjected to DNA sequencing [1].
  • cDNA for the human rhodanese (thiosulfate; cyanide sulfurtransferase, EC was cloned from a human fetal liver cDNA library [10].
  • Sequence homology analysis showed that the human rhodanese is 89.6% identical to bovine, 90.2% identical to rat, 91.2% identical to mouse and Chinese hamster, and 71.4% similar to avian counterparts, respectively, and that rhodanese was highly conserved across evolution [10].
  • Rhodanese activity during the embryonic development of mouse liver and kidney [11].
  • The level of rhodanese may be correlated with the onset of organogenesis [11].

Anatomical context of Tst

  • Because rhodanese activity was slightly but significantly higher in mitochondria lysed by Triton X-100 than in intact mitochondria, the mitochondrial membrane may constitute a barrier to Na2S203 [12].
  • These results indicate that the administration of carrier erythrocytes containing rhodanese and thiosulfate alone can provide significant protection against the lethal effects of cyanide [13].
  • The activity of MPST and rhodanese showed also increased level in brain stem; 114% and 119% of the value determined in cortex, respectively [14].
  • Although the rhodanese-containing carrier cells with thiosulfate as the sulfur donor were efficacious, this approach has potential disadvantages, as thiosulfate has limited penetration of cell membrane and product inhibition of rhodanese can occur due to inorganic sulfite accumulation [15].

Associations of Tst with chemical compounds

  • 2-Substituted thiazolidine-4(R)-carboxylic acids (TD) were found to increase the concentration of non-protein sulphydryls (NPSH) and the activity of rhodanese (thiosulphate sulphurtransferase, EC and 3-mercaptopyruvate sulphurtransferase (EC in mouse liver [16].
  • These data suggest that hepatic rhodanese is not principally involved in the detoxication of cyanide even when exogenous thiosulfate is provided, nor does thiosulfate appear to exert its antidotal action by increasing the available cyanide-labile albumin-bound sulfane-sulfur [5].
  • Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice [9].
  • CPZ did not alter hepatic rhodanese kinetics nor did it enhance plasma thiocyanate concentrations in ST-pretreated mice [17].
  • In the liver of EAT-bearing mice, glutathione (GSH), cysteine and sulfane sulfur levels as well as the activities of: glutathione S-transferase, gamma-glutamyl transpeptidase, rhodanese and gamma-cystathionase significantly dropped in comparison with healthy animals [18].

Other interactions of Tst


Analytical, diagnostic and therapeutic context of Tst


  1. Mouse rhodanese gene (Tst): cDNA cloning, sequencing, and recombinant protein expression. Dooley, T.P., Nair, S.K., Garcia, R.E., Courtney, B.C. Biochem. Biophys. Res. Commun. (1995) [Pubmed]
  2. Age-related changes in toxicity and biotransformation of potassium cyanide in male C57BL/6N mice. McMahon, T.F., Birnbaum, L.S. Toxicol. Appl. Pharmacol. (1990) [Pubmed]
  3. STZ-induced diabetes in mice and heme pathway enzymes. Effect of allylisopropylacetamide and alpha-tocopherol. Polo, C.F., Vázquez, E.S., Gerez, E.N., Caballero, F.A., Batlle, A.M. Chem. Biol. Interact. (1995) [Pubmed]
  4. Transamination and transsulphuration of L-cysteine in Ehrlich ascites tumor cells and mouse liver. The nonenzymatic reaction of L-cysteine with pyruvate. Włodek, L., Wróbel, M., Czubak, J. Int. J. Biochem. (1993) [Pubmed]
  5. Effects of protein-free diet and food deprivation on hepatic rhodanese activity, serum proteins and acute cyanide lethality in mice. Rutkowski, J.V., Roebuck, B.D., Smith, R.P. J. Nutr. (1985) [Pubmed]
  6. MKP-7, a novel mitogen-activated protein kinase phosphatase, functions as a shuttle protein. Masuda, K., Shima, H., Watanabe, M., Kikuchi, K. J. Biol. Chem. (2001) [Pubmed]
  7. Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and site-directed mutagenesis. Nagahara, N., Nishino, T. J. Biol. Chem. (1996) [Pubmed]
  8. A novel approach for screening the proteome for changes in protein conformation. Pierce, A., deWaal, E., VanRemmen, H., Richardson, A., Chaudhuri, A. Biochemistry (2006) [Pubmed]
  9. Isolation and partial purification of mitochondrial and cytosolic rhodanese from liver of normal and p-dimethylaminoazobenzene treated mice. Vazquez, E., Polo, C., Stedile, G., Schebor, C., Karahanian, E., Batlle, A. Int. J. Biochem. Cell Biol. (1995) [Pubmed]
  10. Cloning and expression of human liver rhodanese cDNA. Aita, N., Ishii, K., Akamatsu, Y., Ogasawara, Y., Tanabe, S. Biochem. Biophys. Res. Commun. (1997) [Pubmed]
  11. Rhodanese activity during the embryonic development of mouse liver and kidney. Unsworth, B.R. Enzyme (1975) [Pubmed]
  12. Liver damage does not increase the sensitivity of mice to cyanide given acutely. Rutkowski, J.V., Roebuck, B.D., Smith, R.P. Toxicology (1986) [Pubmed]
  13. Antagonism of cyanide intoxication with murine carrier erythrocytes containing bovine rhodanese and sodium thiosulfate. Cannon, E.P., Leung, P., Hawkins, A., Petrikovics, I., DeLoach, J., Way, J.L. Journal of toxicology and environmental health. (1994) [Pubmed]
  14. Sulfurtransferases activity and the level of low-molecular-weight thiols and sulfane sulfur compounds in cortex and brain stem of mouse. Wróbel, M., Włodek, L., Srebro, Z. Neurobiology (Budapest, Hungary) (1996) [Pubmed]
  15. Cyanide antagonism with carrier erythrocytes and organic thiosulfonates. Petrikovics, I., Cannon, E.P., McGuinn, W.D., Pei, L., Pu, L., Lindner, L.E., Way, J.L. Fundamental and applied toxicology : official journal of the Society of Toxicology. (1995) [Pubmed]
  16. The effect of 2-substituted thiazolidine-4(R)-carboxylic acids on non-protein sulphydryl levels and sulphurtransferase activities in mouse liver and brain. Włodek, L., Radomski, J., Wróbel, M. Biochem. Pharmacol. (1993) [Pubmed]
  17. Antagonism of cyanide poisoning by chlorpromazine and sodium thiosulfate. Pettersen, J.C., Cohen, S.D. Toxicol. Appl. Pharmacol. (1985) [Pubmed]
  18. The selective effect of cystathionine on doxorubicin hepatotoxicity in tumor-bearing mice. Kwiecie??, I., Michalska, M., W??odek, L. Eur. J. Pharmacol. (2006) [Pubmed]
  19. In vitro and in vivo comparison of sulfur donors as antidotes to acute cyanide intoxication. Baskin, S.I., Porter, D.W., Rockwood, G.A., Romano, J.A., Patel, H.C., Kiser, R.C., Cook, C.M., Ternay, A.L. Journal of applied toxicology : JAT. (1999) [Pubmed]
  20. Erythrocyte encapsulated thiosulfate sulfurtransferase. Way, J.L., Leung, P., Ray, L., Sander, C. Bibliotheca haematologica. (1985) [Pubmed]
  21. Cyanide intoxication--III. On the analogous and different effects provoked by non-lethal and lethal challenged doses. Buzaleh, A.M., Vazquez, E.S., del Carmen Batlle, A.M. Gen. Pharmacol. (1990) [Pubmed]
  22. Rhodanese and ALA-S in mammary tumor and liver from normal and tumor-bearing mice. Navone, N.M., Vázquez, E.S., Polo, C.F., Batlle, A.M. Comp. Biochem. Physiol., B (1992) [Pubmed]
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