Sulfurtransferases and Cyanide Detoxification in Mouse Liver, Kidney, and Brain

The activity of rhodanese, 3-mercaptopyruvate sulfurtransferase (MPST) and cystathionase in mouse liver, kidney, and four brain regions: tele-, meso-, di- and rhombencephalon was studied 30 min and 2 h following a sublethal dose of cyanide (4 mg/ kg body weight) intraperitoneal injection. Simultaneously, sulfane sulfur levels and total sulfur content, a direct or indirect source of sulfur for CN− conversion to SCN−, were also investigated in these tissues. In the liver this dose of cyanide seemed to impair the process of cyanide detoxification by MPST, as well as rhodanese inhibition. The effects of cyanide administration to mice proved to be totally different in the liver and kidney. In the kidney, a significant increase in the rhodanese activity was observed as early as 30 min following cyanide intoxication, and an elevated cystathionase activity after 2 h was detected. This suggests the involvement of cystathionase in cyanide detoxification in the kidney. The activity of MPST remained at the same level as in the control group. In the rhombencephalon, similarly as in the kidney, L-cysteine desulfuration pathways, which generate sulfane sulfur and sulfurtransferases that transfer sulfane sulfur atoms to CN−, seemed to play an important role as a defense system against cyanide. The stable level of sulfane sulfur and total sulfur content was accompanied in the rhombencephalon by an increased activity of MPST, cystathionase and rhodanese. In other brain regions the role of these three sulfurtransferases was not so clear and it seemed that in the telencephalon, where the total sulfur content, but not the sulfane sulfur level, was significantly increased, some sulfur-containing compounds, such as GSH and/or cysteine, appeared in response to cyanide.

[1]  M. Wróbel,et al.  Effects of thiazolidine-4(R)-carboxylates and other low-molecular-weight sulfur compounds on the activity of mercaptopyruvate sulfurtransferase, rhodanese and cystathionase in Ehrlich ascites tumor cells and tumor-bearing mouse liver , 1997, Amino Acids.

[2]  J. Barrett,et al.  Cystathionine β-synthase and γ-cystathionase in helminths , 1991, Parasitology Research.

[3]  Marlan,et al.  Isolation of y-Glutamyl Transpeptidase from Hog Kidney* , 2003 .

[4]  Amanda M Li,et al.  Rhodanese distribution in porcine (Sus scrofa) tissues. , 2002, Comparative biochemistry and physiology. Part B, Biochemistry & molecular biology.

[5]  M. Wróbel,et al.  Cystathionine gamma-lyase [EC 4.4.1.1]: an enzymatic assay of alpha-ketobutyrate using lactate dehydrogenase , 2002 .

[6]  J. Borowitz,et al.  Acute and Chronic Cyanide Toxicity , 2000 .

[7]  J. Borowitz,et al.  Cyanide-induced apoptosis involves oxidative-stress-activated NF-kappaB in cortical neurons. , 2000, Toxicology and applied pharmacology.

[8]  P. Horowitz,et al.  Rhodanese as a thioredoxin oxidase. , 2000, The international journal of biochemistry & cell biology.

[9]  N. Nagahara,et al.  Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification. , 1999, Histology and histopathology.

[10]  D. Porter,et al.  In vitro and in vivo comparison of sulfur donors as antidotes to acute cyanide intoxication , 1999, Journal of applied toxicology : JAT.

[11]  N. Nagahara,et al.  Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis , 1998, Histochemistry and Cell Biology.

[12]  J. Borowitz,et al.  Cyanide-induced generation of oxidative species: involvement of nitric oxide synthase and cyclooxygenase-2. , 1998, The Journal of pharmacology and experimental therapeutics.

[13]  C. Pritsos,et al.  Tissue-specific bioenergetic effects and increased enzymatic activities following acute sublethal peroral exposure to cyanide in the mallard duck. , 1997, Toxicology and applied pharmacology.

[14]  D. Porter,et al.  In vivo detoxification of cyanide by cystathionase γ-lyase , 1996 .

[15]  G. Isom,et al.  Cyanide‐Induced Apoptosis and Oxidative Stress in Differentiated PC12 Cells , 1996, Journal of neurochemistry.

[16]  M. Wróbel,et al.  Sulfurtransferases activity and the level of low-molecular-weight thiols and sulfane sulfur compounds in cortex and brain stem of mouse. , 1996, Neurobiology.

[17]  Y. Ogasawara,et al.  Tissue and subcellular distribution of bound and acid-labile sulfur, and the enzymic capacity for sulfide production in the rat. , 1994, Biological & pharmaceutical bulletin.

[18]  D. Wing,et al.  The effect of picrylsulphonic acid on In vitro conversion of cyanide to thiocyanate by 3-mercaptopyruvate sulphurtransferase and rhodanese. , 1992, Toxicology in vitro : an international journal published in association with BIBRA.

[19]  M. Wróbel,et al.  The effect of cAMP and some sulphur compounds upon the activity of mercaptopyruvate sulphurtransferase and rhodanese in mouse liver. , 1992, Folia biologica.

[20]  J. Barrett,et al.  Cystathionine beta-synthase and gamma-cystathionase in helminths. , 1991, Parasitology research.

[21]  D. Choi,et al.  N-methyl-D-aspartate receptors mediate hypoxic neuronal injury in cortical culture. , 1987, The Journal of pharmacology and experimental therapeutics.

[22]  J. L. Wood.  Sulfane sulfur. , 1987, Methods in enzymology.

[23]  T. Nishino.  Reversible Interconversion Between Sulfo and Desulfo Xanthine Dehydrogenase , 1986 .

[24]  A. Meister,et al.  Extracellular metabolism of glutathione accounts for its disappearance from the basolateral circulation of the kidney. , 1984, The Journal of biological chemistry.

[25]  R. Parkhouse.  Methods in Enzymology: Vol.93, Part F , 1984 .

[26]  J. L. Way.  Cyanide intoxication and its mechanism of antagonism. , 1984, Annual review of pharmacology and toxicology.

[27]  S. Tuboi,et al.  The Mechanism of the L-Cystine Cleavage Reaction Catalyzed by Rat Liver γ-Cystathionase , 1981 .

[28]  S. Tuboi,et al.  The mechanism of the L-cystine cleavage reaction catalyzed by rat liver gamma-cystathionase. , 1981, Journal of biochemistry.

[29]  A. Koj,et al.  Subcellular compartmentation of rhodanese and 3-mercaptopyruvate sulphurtransferase in the liver of some vertebrate species , 1980 .

[30]  S. Pagani,et al.  Insertion of sulfide into ferredoxins catalyzed by rhodanese , 1977, FEBS letters.

[31]  S. Pagani,et al.  Rhodanese-Mediated sulfur transfer to succinate dehydrogenase. , 1977, European journal of biochemistry.

[32]  R. Baumeister,et al.  Toxicological and clinical aspects of cyanide metabolism. , 1975, Arzneimittel-Forschung.

[33]  B. Sörbo.  CHAPTER 10 – Thiosulfate Sulfurtransferase and Mercaptopyruvate Sulfurtransferase , 1975 .

[34]  D. M. Greenberg.  CHAPTER 12 – Biosynthesis of Cysteine and Cystine , 1975 .

[35]  W. Valentine,et al.  3-Mercaptopyruvate sulfurtransferase (EC 2.8.1.2): a simple assay adapted to human blood cells. , 1974, Clinica chimica acta; international journal of clinical chemistry.

[36]  J. L. Wood,et al.  The cystathionase-rhodanese system. , 1967, Biochimica et biophysica acta.

[37]  M. Orłowski,et al.  ISOLATION OF GAMMA-GLUTAMYL TRANSPEPTIDASE FROM HOG KIDNEY. , 1965, The Journal of biological chemistry.

[38]  A. Koj,et al.  The activity of cysteine desulphhydrase and rhodanase in animal tissues. , 1962, Acta biochimica Polonica.

[39]  Y. Matsuo,et al.  A crystalline enzyme that cleaves homoserine and cystathionine. II. Prosthetic group. , 1958, The Journal of biological chemistry.

[40]  B. Sörbo,et al.  Sulfite and Complex-bound Cyanide as Sulfur Acceptors for Rhodanese. , 1957 .

[41]  B. Sörbo.  [43] Rhodanese: CN−+S2O3−−→ CNS−+SO3−− , 1955 .

[42]  O. H. Lowry,et al.  Protein measurement with the Folin phenol reagent. , 1951, The Journal of biological chemistry.