Disease relevance of Tst

• When the mouse and rat cDNAs were expressed under the control of IPTG-inducible promoters in E. coli, the cell extracts exhibited cyanide-metabolizing activity, indicating that both genes encode functional rhodanese molecules [1].
• The basis for this age-related difference in in vivo toxicity was examined by studying biotransformation of KCN to thiocyanate by liver and brain rhodanese (RHO), as well as activity of liver and brain cytochrome oxidase (C-OX), inhibition of C-OX by KCN, and activity of beta-mercaptopyruvate transsulfurase (MT) [2].
• The activity of some heme enzymes and rhodanese in streptozotocin (STZ) induced diabetic mice and in allylisopropylacetamide (AIA) induced experimental acute porphyria mice has been examined [3].
• 1. The activity of cysteine aminotransferase (CAT), 3-mercaptopyruvate sulfurtransferase (MPST) and rhodanese is much lower in Ehrlich ascites tumor cells (EATC) than in mouse liver [4].

Psychiatry related information on Tst

• Effects of protein-free diet and food deprivation on hepatic rhodanese activity, serum proteins and acute cyanide lethality in mice [5].

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 2.8.1.1) 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 2.8.1.1) and 3-mercaptopyruvate sulphurtransferase (EC 2.8.1.2) 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

• Cystationine did not influence sulfane sulfur level and rhodanese and gamma-cystathionase activity in the livers of EAT-bearing mice [18].
• To study the mechanism of action of the SSD, the candidate compounds were examined in vitro for their effect on rhodanese and 3-mercaptopyruvate sulfurtransferase (MST) activity under increasing SSD concentrations [19].
• Erythrocyte encapsulated thiosulfate sulfurtransferase [20].
• 2. The poisoning action was determined by measuring cytochrome oxidase, rhodanese and delta-aminolevulinic acid dehydratase (ALA-D) activity [21].

Analytical, diagnostic and therapeutic context of Tst

• Hepatic rhodanese activity was higher in the protein-free diet group than in either of the other two groups [5].
• 4. Mitochondrial and cytoplasmic rhodanese activity was also measured in tumor and liver of TBM at different intervals after transplantation [22].

References