Abstract
This study aims to investigate the relationship between sulfurtransferase (STS) activities [rhodanese (TST), mercaptopyruvate sulfurtransferase (MST)] involved in the catalysis of several biochemical reactions including detoxification of cyanide (CN−), restructuring of Fe-S cluster in proteins, and detoxification of oxygen radicals. Rats with type 1 diabetes mellitus induced by streptozotocin (STZ) were anesthetized at 14th day, and liver, lung, kidney, and heart tissues were extracted. All samples were homogenized, and mitochondrial parts were separated. Same processes were performed also in the control group, and TST and MST activities were measured in each part. The homogenate MST (MST Homo .) activities of the type 1 diabetes mellitus group were compared with the control group, and a decrease was observed in the lung, liver, and kidney, respectively; at the same time, an increase was seen in the heart tissue. The mitochondrial MST (MST Mito .) activities of rats with type 1 diabetes mellitus group were compared with the control group, and a decrease was found in all tissues. The highest decrease in the TST Mito . level of rats with type 1 diabetes mellitus was observed in kidney tissue. The TST activities of the type 1 diabetes mellitus group were compared with the control group, and a decrease was observed in the liver, lung, and kidney, respectively; at the same time, an increase was seen in the heart tissue. It is demonstrated in the present study that decreases occur both in enzyme levels of tissue homogenates and in mitochondria, of rats with induced type 1 diabetes mellitus. However, these results were not statistically significant. In the presence of these findings, we think that kidney, liver, lung, and heart tissue can be affected by type 1 diabetes in the long term.
Similar content being viewed by others
References
Agboola FK, Okonji RE. Presence of rhodanese in the cytosolic fraction of the fruit bat (Eidolon helvum) Liver. J Biochem Mol Biol. 2004;37:275–81.
Wasylewski Z, Basztura B, Koj A. Comparison of some physicochemical properties of rat and beef liver rhodanese. Bull Acad Pol Sci [Biol]. 1979;27:807–14.
Ogata K, Volini M. Mitochondrial rhodanese: membrane-bound and complexed activity. J Biol Chem. 1990;265:8087–93.
Westley J. Thiosulfate: cyanide sulfurtransferase (rhodanese). Methods Enzymol. 1981;77:285–91.
Dooley TP, Nair SK, Garcia R, Courtney BC. Mouse rhodanese gene (Tst): cDNA cloning, sequencing, and recombinant protein expression. Biochem Biophys Res Commun. 1995;216:1101–9.
Nagahara N, Okazaki T, Nishino T. Cytosolic mercaptopyruvate sulfurtransferase is evolutionarily related to mitochondrial rhodanese. Striking similarity in active site amino acid sequence and the increase in the mercaptopyruvate sulfurtransferase activity of rhodanese by site-directed mutagenesis. J Biol Chem. 1995;270:16230–5.
Berni R, Cannella C, Monaco HL, Rossi GL. New crystalline derivatives of bovine liver rhodanese. Biochem Int. 1986;12:733–40.
Colnaghi R, Pagani S, Kennedy C, Drummond M. Cloning, sequence analysis and overexpression of the rhodanese gene of Azotobacter vinelandii. Eur J Biochem. 1996;236:240–8.
Bordo D, Deriu D, Colnaghi R, Carpen A, Pagani S, et al. The crystal structure of a sulfurtransferase from Azotobacter vinelandii highlights the evolutionary relationship between the rhodanese and phosphatase enzyme families. J Mol Biol. 2000;298:691–704.
Aird BA, Heinrikson RL, Westley J. Isolation and characterization of a prokaryotic sulfurtransferase. J Biol Chem. 1987;262:17327–35.
Lányi B. Rhodanese activity: a simple and reliable taxonomic tool for gram negative bacteria. J Med Microbiol. 1982;15(2):263–6.
Alexander K, Volini M. Properties of an Escherichia coli rhodanese. J Biol Chem. 1987;262:6595–604.
Villarejo M, Westley J. Sulfur metabolism of Bacillus subtilis. Biochim Biophys Acta. 1966;117:209–16.
Laudenbach DE, Ehrhardt D, Green L, Grossmann A. Isolation and characterization of a sulfur-regulated gene encoding a periplasmatically localized protein with sequence similarity to rhodanese. J Bacteriol. 1991;173:2751–60.
Vennesland B, Castric PA, Conn EE, Solomonson LP, Volini M, et al. Cyanide metabolism. Fed Proc. 1982;41:2639–48.
Nagahara N, Ito T, Minami M. Mercaptopyruvate sulfurtransferase as a defense against cyanide toxication: molecular properties and mode of detoxification. Histol Histopathol. 1999;14:1277–86.
Blachier F, Davila AM, Mimoun S, Benetti PH, Atanasiu C, Andriamihaja M, et al. Luminal sulfide and large intestine mucosa: friend or foe? Amino Acids. 2010;39:335–47.
Wood JL, Fiedler H. β-mercaptopyruvate, a substrate for rhodanese. J Biol Chem. 1953;205:231–4.
Westley J, Adler H, Westley L, Nishida C. The sulfurtransferases. Fundam Appl Toxicol. 1983;3:377–82.
Nagahara N, Nishino T. Role of amino acid residues in the active site of rat liver mercaptopyruvate sulfurtransferase. CDNA cloning, overexpression, and sitedirected mutagenesis. J Biol Chem. 1996;271:27395–401.
Westley JE. Ciba Foundation Symposium 140 - cyanide compounds in biology: mammalian cyanide detoxification with sulphane sulphur. Ciba Foundation;1988
Nandi DL, Horowitz PM, Westley J. Rhodanese as a thioredoxin oxidase. Int J Biochem Cell Biol. 2000;32:465–73.
Sabelli R, Iorio E, De Martino A, Podo F, Ricci A, Viticchiè G, et al. Rhodanese-thioredoxin system and allyl sulfur compounds. FEBS J. 2008;275:3884–99.
Bonomi F, Pagani S, Cerletti P, Cannella C. Rhodanese mediated sulfur transfer to succinate dehydrogenase. Eur J Bioche. 1977;72:17–24.
Pagani S, Bonomi F, Cerletti P. Enzymic synthesis of the ironsulfur cluster of spinach ferredoxin. Eur J Biochem. 1984;142:361–6.
Pagani S, Eldridge M, Eady RR. Nitrogenase of Klebsiella pneumoniae: rhodanese-catalyzed restoration of activity of inactive 2Fe species of the Fe protein. Biochem J. 1987;244:485–8.
Max SR, Garbbus J, Wehmen HJ. Simple procedure for rapid isolation of functionally intact mitochondria from human and rat skeletal muscles. Anal Biochem. 1972;46:576–84.
Mousa HM, Davis RH. Alternative sulphur donors for detoxification of cyanide in the chicken. Comp Biochem Physiol C. 1991;99:309–15.
Tornqvist H, Belfrage P. Determination of protein in adipose tissue extracts. J Lipid Res. 1976;17:542–5.
Pagani S, Galante YM. Interaction of rhodanese with mitochondrial NADH dehydrogenase. Biochim Biophys Acta. 1983;742:278–84.
Matthies A, Rajagopalan KV, Mendel RR, Leimkühler S. Evidence for the physiological role of a rhodanese-like protein for the biosynthesis of the molybdenum cofactor in humans. Proc Natl Acad Sci U S A. 2004;101:5946–51.
Leimkühler S, Rajagopalan KV. A sulfurtransferase is required in the transfer of cysteine sulfur in the in vitro synthesis of molybdopterin from precursor Z in Escherichia coli. J Biol Chem. 2001;276:22024–31.
Palenchar PM, Buck CJ, Cheng H, Larson TJ, Mueller EG. Evidence that thil, an enzyme shared between thiamine and 4-thiouridine biosynthesis, may be a sulfurtransferase that proceeds through a persulfide intermediate. J Biol Chem. 2000;275:8283–6.
Pauwels PJ, Opperdoes FR, Trouet A. Effect of oxygen and glucose availability on the glycolytic rate in neuroblastoma cells under different conditions of culture. Neurochem Int. 1984;64:467–73.
Abdrakhmanova A, Dobrynin K, Zwicker K, Kerscher S, Brandt U. Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron–sulfur clusters. FEBS Lett. 2005;579:6781–5.
Reidy K, Kang HM, Hostetter T, Susztak K. Molecular mechanisms of diabetic kidney disease. J Clin Invest. 2014;124:2333–40.
Isfort M, Stevens SC, Schaffer S, Jong CJ, Wold LE. Metabolic dysfunction in diabetic cardiomyopathy. Heart Fail Rev. 2014;19:35–48.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Aydın, H., Çelik, V.K., Sarı, İ. et al. Comparison of sulfur transferases in various tissue and mitochondria of rats with type 1 diabetes mellitus induced by streptozotocin. Int J Diabetes Dev Ctries 36, 4–9 (2016). https://doi.org/10.1007/s13410-015-0377-1
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13410-015-0377-1