Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases

Lang, 1933, Die Rhodanbildung im Tierkorpor, Biochem. Z., 259

Horowitz, 1980, Some comparisons between solution and crystal properties of thiosulfate sulfurtransferase, Biochem. Biophys. Res. Commun., 94, 419, 10.1016/0006-291X(80)91247-4

Isom, 1984, Effects of oxygen on the antagonism of cyanide intoxication: cytochrome oxidase, in vitro, Toxicol. Appl. Pharmacol., 74, 57, 10.1016/0041-008X(84)90269-2

Mimori, 1984, Regional and subcellular distribution of cyanide metabolizing enzymes in the central nervous system, J. Neurochem., 43, 540, 10.1111/j.1471-4159.1984.tb00932.x

Sylvester, 1990, Immunohistochemical localization of rhodanese, Histochem. J., 22, 197, 10.1007/BF02386005

Cipollone, 2007, Common themes and variations in the rhodanese superfamily, IUBMB Life, 59, 51, 10.1080/15216540701206859

Nagahara, 1998, Tissue and subcellular distribution of mercaptopyruvate sulfurtransferase in the rat: confocal laser fluorescence and immunoelectron microscopic studies combined with biochemical analysis, Histochem. Cell Biol., 110, 243, 10.1007/s004180050286

Nagahara, 2019, T Ito: novel characterization of antioxidant enzyme, 3-mercaptopyruvate sulfurtransferase-knockout mice: overexpression of the evolutionarily-related enzyme rhodanese, Antioxidants (Basel), 8, 116, 10.3390/antiox8050116

Sörbo, 1951, On the properties of rhodanese, Acta Chem. Scand., 5, 724, 10.3891/acta.chem.scand.05-0724

Ramasamy, 2006, Sulfide-detoxifying enzymes in the human colon are decreased in cancer and upregulated in differentiation, Am. J. Physiol. Gastrointest. Liver Physiol., 291, G288, 10.1152/ajpgi.00324.2005

Gliubich, 1998, Structure of sulfur-substituted rhodanese at 1.36 Å resolution, Acta Crystallogr. D Biol. Crystallogr., 54, 481, 10.1107/S090744499701216X

Cianci, 2000, Specific interaction of lipoate at the active site of rhodanese, Biochim. Biophys. Acta Protein Struct. Mol. Enzymol., 1481, 103, 10.1016/S0167-4838(00)00114-X

Bhattacharyya, 2000, Alteration around the active site of rhodanese during urea-induced denaturation and its implications for folding, J. Biol. Chem., 275, 14860, 10.1074/jbc.275.20.14860

Libiad, 2015, Polymorphic variants of human rhodanese exhibit differences in thermal stability and sulfur transfer kinetics, J. Biol. Chem., 290, 23579, 10.1074/jbc.M115.675694

Green, 1961, Mechanism of rhodanese action: polarographic studies, J. Biol. Chem., 236, 3047, 10.1016/S0021-9258(19)76426-6

Westley, 1981, Thiosulfate: cyanide sulfurtransferase (rhodanese), Methods Enzymol., 77, 285, 10.1016/S0076-6879(81)77039-3

Blicharska, 1982, A nuclear magnetic relaxation study of conformational changes induced by substrate and temperature in bovine liver thiosulfate sulfurtransferase and yeast hexokinase, Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 708, 326, 10.1016/0167-4838(82)90444-7

Horowitz, 1983, Proteolytic interconversion of electrophoretic variants of the enzyme rhodanese, J. Biol. Chem., 258, 1614, 10.1016/S0021-9258(18)33029-1

Chow, 1985, Spectral differences between rhodanese catalytic intermediates unrelated to enzyme conformation, J. Biol. Chem., 260, 9593, 10.1016/S0021-9258(17)39277-3

Horowitz, 1987, Conformational changes accompany the oxidative inactivation of rhodanese by a variety of reagents, J. Biol. Chem., 262, 8728, 10.1016/S0021-9258(18)47476-5

Horowitz, 1987, Oxidation increases the proteolytic susceptibility of a localized region in rhodanese, J. Biol. Chem., 262, 14544, 10.1016/S0021-9258(18)47830-1

Libiad, 2018, Thiosulfate sulfurtransferase like domain containing 1 protein interacts with thioredoxin, J. Biol. Chem., 293, 2675, 10.1074/jbc.RA117.000826

Nandi, 2000, Rhodanese as a thioredoxin oxidase, Int. J. Biochem. Cell Biol., 32, 465, 10.1016/S1357-2725(99)00035-7

Nagahara, 1995, J. Biol. Chem., 270, 16230, 10.1074/jbc.270.27.16230

Miller-Martini, 1994, Mutations of noncatalytic sulfhydryl groups influence the stability, folding, and oxidative susceptibility of rhodanese, Journal of Biological Chemistry, 269, 3423, 10.1016/S0021-9258(17)41879-5

Volini, 1978, Effects of metal-ion binding on rhodanese activity, Arch. Biochem. Biophys., 191, 205, 10.1016/0003-9861(78)90083-8

Libiad, 2014, Organization of the human mitochondrial hydrogen sulfide oxidation pathway, J. Biol. Chem., 289, 30901, 10.1074/jbc.M114.602664

Dudek, 1980, Subcellular compartmentation of rhodanese and 3-mercaptopyruvate sulphurtransferase in the liver of some vertebrate species, Comparative Biochemistry and Physiology – Part B: Biochemistry and, 65, 383, 10.1016/0305-0491(80)90031-0

Koj, 1975, Subcellular distribution and intramitochondrial localization of three sulfurtransferases in rat liver, FEBS Lett., 57, 42, 10.1016/0014-5793(75)80148-7

Walker, 1991, Pyridoxal 5′-phosphate dependent enzymes in the nematode Nippostrongylus brasiliensis, Int. J. Parasitol., 21, 641, 10.1016/0020-7519(91)90075-I

Westley, 1973, Rhodanese, Adv. Enzymol. Relat. Areas Mol. Biol., 39, 327

Frankenberg, 1975, Effect of cyanide antidotes on the metabolic conversion of cyanide to thiocyanate, Arch. Toxicol., 33, 81, 10.1007/BF00353233

Ogata, 1989, Bovine mitochondrial rhodanese is a phosphoprotein, J. Biol. Chem., 264, 2718, 10.1016/S0021-9258(19)81672-1

Bonomi, 1977, Insertion of sulfide into ferredoxins catalyzed by rhodanese, FEBS Lett., 84, 149, 10.1016/0014-5793(77)81076-4

Bonomi, 1977, Rhodanese-mediated sulfur transfer to succinate dehydrogenase, Eur. J. Biochem., 72, 17, 10.1111/j.1432-1033.1977.tb11219.x

Wróbel, 2014, Is development of high-grade gliomas sulfur dependent?, Molecules, 19, 21350, 10.3390/molecules191221350

Szczepkowski, 1967, The cystathionase-rhodanese system, Biochim. Biophys. Acta, 139, 469, 10.1016/0005-2744(67)90050-2

Weng, 1978, Active site cysteinyl and arginyl residues of rhodanese. A novel formation of disulfide bonds in the active site promoted by phenylglyoxal, J. Biol. Chem., 253, 8109, 10.1016/S0021-9258(17)34369-7

Cerletti, 1986, Seeking a better job for an under-employed enzyme: rhodanese, Trends Biochem. Sci., 11, 369, 10.1016/0968-0004(86)90206-9

Pagani, 1983, Interaction of rhodanese with mitochondrial NADH dehydrogenase, Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 742, 278, 10.1016/0167-4838(83)90312-6

Nishino, 1983, Reversible interconversion between sulfo and desulfo xanthine oxidase in a system containing rhodanese, thiosulfate, and sulfhydryl reagent, Proc. Natl. Acad. Sci. U. S. A., 80, 1826, 10.1073/pnas.80.7.1826

Tomati, 1976, NADH: nitrate reductase activity restoration by rhodanese [wheat], Phytochemistry (UK), 15, 597, 10.1016/S0031-9422(00)94400-5

Krueger, 2010, Low expression of thiosulfate sulfurtransferase (rhodanese) predicts mortality in hemodialysis patients, Clin. Biochem., 43, 95, 10.1016/j.clinbiochem.2009.08.005

Pagani, 1982, Sulfide insertion into spinach ferredoxin by Rhodanese, Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular, 700, 154, 10.1016/0167-4838(82)90092-9

Lu, 2013, The thioredoxin antioxidant system, Free Radic. Biol. Med., 66, 75, 10.1016/j.freeradbiomed.2013.07.036

Vazquez, 1987, Red blood cell rhodanese: its possible role in modulating delta-aminolaevulinate synthetase activity in mammals, The International Journal of Biochemistry, 19, 217, 10.1016/0020-711X(87)90337-5

Yadav, 2013, Structure and kinetic analysis of H2S production by human mercaptopyruvate sulfurtransferase, J. Biol. Chem., 288, 20002, 10.1074/jbc.M113.466177

Nandi, 1998, Reduced thioredoxin as a sulfur-acceptor substrate for rhodanese, Int. J. Biochem. Cell Biol., 30, 973, 10.1016/S1357-2725(98)00050-8

Jackson, 2012, Human sulfide:quinone oxidoreductase catalyzes the first step in hydrogen sulfide metabolism and produces a sulfane sulfur metabolite, Biochemistry, 51, 6804, 10.1021/bi300778t

Muri, 2018, The thioredoxin-1 system is essential for fueling DNA synthesis during T-cell metabolic reprogramming and proliferation, Nat. Commun., 9, 1851, 10.1038/s41467-018-04274-w

Nishinaka, 2001, Regulatory roles of thioredoxin in oxidative stress-induced cellular responses, Redox Rep., 6, 289, 10.1179/135100001101536427

Dóka, 2016, A novel persulfide detection method reveals protein persulfide and polysulfide-reducing functions of thioredoxin and glutathione systems, Sci. Adv., 2, 10.1126/sciadv.1500968

Wedmann, 2016, Improved tags witch method reveals that thioredoxin acts as depersulfidase and controls the intracellular levels of protein persulfidation, Chem. Sci., 7, 3414, 10.1039/C5SC04818D

Mao, 2019, Pharmacological levels of hydrogen sulfide inhibit oxidative cell injury through regulating the redox state of thioredoxin, Free Radic. Biol. Med., 134, 190, 10.1016/j.freeradbiomed.2019.01.009

Mihm, 1995, Modulation of transcription factor NF kappa B activity by intracellular glutathione levels and by variations of the extracellular cysteine supply, FASEB J., 9, 246, 10.1096/fasebj.9.2.7781927

Heilman, 2011, Transactivation of gene expression by NF-κB is dependent on thioredoxin reductase activity, Free Radic. Biol. Med., 51, 1533, 10.1016/j.freeradbiomed.2011.06.028

Hsieh, 2006, Thioredoxin-ASK1 complex levels regulate ROS-mediated p38 MAPK pathway activity in livers of aged and long-lived Snell dwarf mice, FASEB Journal: Official Publication of the Federation of American Societies for Experimental Biology, 20, 259, 10.1096/fj.05-4376com

Song, 2003, Differential role of glutaredoxin and thioredoxin in metabolic oxidative stress-induced activation of apoptosis signal regulating kinase 1, The Biochemical Journal, 373, 845, 10.1042/bj20030275

Barrett, 1999

Dagnell, 2013, Selective activation of oxidized PTP1B by the thioredoxin system modulates PDGF-β receptor tyrosine kinase signaling, Proc. Natl. Acad. Sci. U. S. A., 110, 13398, 10.1073/pnas.1302891110

Yoshioka, 2012, Deletion of thioredoxin-interacting protein in mice impairs mitochondrial function but protects the myocardium from ischemia-reperfusion injury, J. Clin. Invest., 122, 267, 10.1172/JCI44927

Chutkow, 2008, Thioredoxin interacting protein (Txnip) is a critical regulator of hepatic glucose production, J. Biol. Chem., 283, 2397, 10.1074/jbc.M708169200

Hui, 2008, Txnip balances metabolic and growth signaling via PTEN disulfide reduction, Proc. Natl. Acad. Sci. U. S. A., 105, 3921, 10.1073/pnas.0800293105

Yoshihara, 2010, Disruption of TBP-2 ameliorates insulin sensitivity and secretion without affecting obesity, Nat. Commun., 1, 127, 10.1038/ncomms1127

Parikh, 2007, TXNIP regulates peripheral glucose metabolism in humans, PLoS Med., 4, e158, 10.1371/journal.pmed.0040158

Ogasawara, 2001, Formation of a selenium-substituted rhodanese by reaction with selenite and glutathione: possible role of a protein perselenide in a selenium delivery system, Proc. Natl. Acad. Sci. U. S. A., 98, 9494, 10.1073/pnas.171320998

Hatfield, 2014, Selenium and selenocysteine: roles in cancer, health, and development, Trends Biochem. Sci., 39, 112, 10.1016/j.tibs.2013.12.007

Morton, 2016, Genetic identification of thiosulfate sulfurtransferase as an adipocyte-expressed antidiabetic target in mice selected for leanness, Nat. Med., 22, 771, 10.1038/nm.4115

Yanai, 2019, Beneficial effects of adiponectin on glucose and lipid metabolism and atherosclerotic progression: mechanisms and perspectives, Int. J. Mol. Sci., 20, 1190, 10.3390/ijms20051190

Lontchi-Yimagou, 2013, Diabetes mellitus and inflammation, Current Diabetes Reports, 13, 435, 10.1007/s11892-013-0375-y

Picton, 2002, Mucosal protection against sulphide: importance of the enzyme rhodanese, Gut, 50, 201, 10.1136/gut.50.2.201

Picton, 2007, Impaired detoxication of hydrogen sulfide in ulcerative colitis?, Dig. Dis. Sci., 52, 373, 10.1007/s10620-006-9529-y

Taniguchi, 2009, Rhodanese, but not cystathionine-γ-lyase, is associated with dextran sulfate sodium-evoked colitis in mice: a sign of impaired colonic sulfide detoxification?, Toxicology, 264, 96, 10.1016/j.tox.2009.07.018

De Preter, 2012, Decreased mucosal sulfide detoxification is related to an impaired butyrate oxidation in ulcerative colitis, Inflamm. Bowel Dis., 18, 2371, 10.1002/ibd.22949

Yi, 2010, Identification of Rack1, EF-Tu and rhodanese as aging-related proteins in human colonic epithelium by proteomic analysis, J. Proteome Res., 9, 1416, 10.1021/pr9009386

Cagianut, 1984, Decreased thiosulfate sulfurtransferase (rhodanese) in Leber’s hereditary optic atrophy, Klin. Wochenschr., 62, 850, 10.1007/BF01712000

Nikoskelainen, 1984, Leber’s hereditary optic neuroretinopathy, a mitochondrial disease?, Lancet, 1474

Poole, 1986, Deficiency of thiosulphate sulphurtransferase (rhodanese) in Leber’s hereditary optic neuropathy, Br. Med. J. (Clin. Res. Ed.), 292, 1229, 10.1136/bmj.292.6530.1229

Bargiela, 2019, Mitochondria in neuroinflammation — multiple sclerosis (MS), Leber hereditary optic neuropathy (LHON) and LHON-MS, Neurosci. Lett., 710, 132932, 10.1016/j.neulet.2017.06.051

Whitehouse, 1989, Rhodanese isozymes in three subjects with Leber’s optic neuropathy, J. Med. Genet., 26, 113, 10.1136/jmg.26.2.113

Hunt, 2018, Metabolic acidosis after sodium thiosulfate infusion and the role of hydrogen sulfide, Clinical Case Reports, 6, 1595, 10.1002/ccr3.1673

Peng, 2018, Systematic review of sodium thiosulfate in treating calciphylaxis in chronic kidney disease patients, Nephrology, 23, 669, 10.1111/nep.13081

Snijder, 2014, Sodium thiosulfate attenuates angiotensin II-induced hypertension, proteinuria and renal damage, Nitric Oxide, 42, 87, 10.1016/j.niox.2014.10.002

Snijder, 2015, Administration of thiosulfate, a donor of hydrogen sulfide, attenuates angiotensin II-induced hypertensive heart disease in rats, Br. J. Pharmacol., 172, 1494, 10.1111/bph.12825

Ravindran, 2017, Sodium thiosulfate post-conditioning protects rat hearts against ischemia reperfusion injury via reduction of apoptosis and oxidative stress, Chem. Biol. Interact., 274, 24, 10.1016/j.cbi.2017.07.002

Kabil, 2014, H2S and its role in redox signaling, Biochim. Biophys. Acta, 1844, 1355, 10.1016/j.bbapap.2014.01.002

Kanagy, 2017, Vascular biology of hydrogen sulfide, Am J Physiol Cell Physiol, 312, C537, 10.1152/ajpcell.00329.2016

Perridon, 2016, The role of hydrogen sulfide in aging and age-related pathologies, Aging (Albany NY), 8, 2264, 10.18632/aging.101026

Koning, 2015, The role of hydrogen sulfide in aging and age-related pathologies, Nitric Oxide, 46, 37, 10.1016/j.niox.2015.01.005

Jurkowska, 2017, A possible mechanism of inhibition of U87MG and SH-SY5Y cancer cell proliferation by diallyl trisulfide and other aspects of its activity, Amino Acids, 49, 1855, 10.1007/s00726-017-2484-4

Eichmann, 2016, S-nitrosylation induces structural and dynamical changes in a rhodanese family protein, J. Mol. Biol., 428, 3737, 10.1016/j.jmb.2016.07.010