Low expression of thiosulfate sulfurtransferase (rhodanese) predicts mortality in hemodialysis patients

Clinical Biochemistry

Volumn 43, Issue 1-2, 2010, Pages 95-101

  Krueger, Katharina ^a   Koch, Kathrin ^a   Jühling, Anja ^a   Tepel, Martin ^a   Scholze, Alexandra ^a  

^a CHARITÉ UNIVERSITÄTSMEDIZIN BERLIN   (Germany)

Author keywords

Hemodialysis; Mortality; Oxidative stress; Patients with chronic kidney disease stage 5; Rhodanese; Uremia

Indexed keywords

GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; MESSENGER RNA; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; THIOSULFATE SULFURTRANSFERASE;

ADULT; ARTICLE; CHRONIC KIDNEY DISEASE; CONTROLLED STUDY; FEMALE; GENE EXPRESSION; HEMODIALYSIS; HEMODIALYSIS PATIENT; HUMAN; MAJOR CLINICAL STUDY; MALE; MONOCYTE; MORTALITY; PREDICTION; PRIORITY JOURNAL; PROTEIN EXPRESSION; SPECTROFLUOROMETRY; SURVIVAL TIME;

ADULT; AGED; AGED, 80 AND OVER; ANIMALS; FEMALE; HUMANS; KIDNEY FAILURE, CHRONIC; MALE; MIDDLE AGED; MITOCHONDRIA; MONOCYTES; OXIDATIVE STRESS; PREGNANCY; REACTIVE OXYGEN SPECIES; RENAL DIALYSIS; SUPEROXIDES; THIOSULFATE SULFURTRANSFERASE; YOUNG ADULT;

EID: 72649105688     PISSN: 00099120     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.clinbiochem.2009.08.005     Document Type: Article

References (35)

1. Himmelfarb J., Stenvinkel P., Ikizler T.A., and Hakim R.M. The elephant in uremia: oxidant stress as a unifying concept of cardiovascular disease in uremia. Kidney Int. 62 (2002) 1524-1538
2. Pawlak K., Pawlak D., and Mysliwiec M. Impaired renal function and duration of dialysis therapy are associated with oxidative stress and proatherogenic cytokine levels in patients with end-stage renal disease. Clin. Biochem. 40 (2007) 81-85
3. Tepel M., Echelmeyer M., Orie N.N., and Zidek W. Increased intracellular reactive oxygen species in patients with end-stage renal failure: effect of hemodialysis. Kidney Int. 58 (2000) 867-872
4. Bayés B., Pastor M.C., Bonal J., Foraster A., and Romero R. Oxidative stress, inflammation and cardiovascular mortality in haemodialysis-role of seniority and intravenous ferrotherapy: analysis at 4 years of follow-up. Nephrol. Dial. Transplant. 21 (2006) 984-990
5. Boaz M., Smetana S., Weinstein T., Matas Z., et al. Secondary prevention with antioxidants of cardiovascular disease in endstage renal disease (SPACE): randomised placebo-controlled trial. Lancet 356 (2000) 1213-1218
6. Tepel M., van der Giet M., Statz M., Jankowski J., and Zidek W. The antioxidant acetylcysteine reduces cardiovascular events in patients with end-stage renal failure: a randomized, controlled trial. Circulation 107 (2003) 992-995
7. Brookes P.S., Yoon Y., Robotham J.L., Anders M.W., and Sheu S.S. Calcium, ATP, and ROS: a mitochondrial love-hate triangle. Am. J. Physiol. Cell. Physiol. 287 (2004) C817-C833
8. Aita N., Ishii K., Akamatsu Y., Ogasawara Y., and Tanabe S. Cloning and expression of human liver rhodanese cDNA. Biochem. Biophys. Res. Commun. 231 (1997) 56-60
9. Nandi D.L., Horowitz P.M., and Westley J. Rhodanese as a thioredoxin oxidase. Int. J. Biochem. Cell. Biol. 32 (2000) 465-473
10. Cipollone R., Ascenzi P., Tomao P., Imperi F., and Visca P. Enzymatic detoxification of cyanide: clues from Pseudomonas aeruginosa rhodanese. J. Mol. Microbiol. Biotechnol. 15 (2008) 199-211
11. Bonomi F., Pagani S., Cerletti P., and Canella C. Rhodanese-mediated sulfur transferase to succinate dehydrogenase. Eur. J. Biochem. 72 (1977) 17-24
12. Pagani S., and Galante Y.M. Interaction of rhodanese with mitochondrial NADH dehydrogenase. Biochim. Biophys. Acta 742 (1983) 278-284
13. Abdrakhmanova A., Dobrynin K., Zwicker K., Kerscher S., and 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. 579 (2005) 6781-6785
14. Ogata K., and Volini M. Mitochondrial rhodanese: membrane-bound and complexed activity. J. Biol. Chem. 265 (1990) 8087-8093
15. Nishino T., Usami C., and Tsushima K. 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 (1983) 1826-1829
16. Papa S., and Skulachev V.P. Reactive oxygen species, mitochondria, apoptosis and aging. Mol. Cell. Biochem. 174 (1997) 305-319
17. Sanz A., Caro P., Ibanez J., Gomez J., Gredilla R., and Barja G. Dietary restriction at old age lowers mitochondrial oxygen radical production and leak at complex I and oxidative DNA damage in rat brain. J. Bioenerg. Biomembr. 37 (2005) 83-90
18. Liu D., Scholze A., Zhu Z., Krueger K., et al. Transient receptor potential channels in essential hypertension. J. Hypertens. 24 (2006) 1105-1114
19. Thilo F., Scholze A., Liu D.Y., Zidek W., and Tepel M. Association of transient receptor potential canonical type 3 (TRPC3) channel transcripts with proinflammatory cytokines. Arch. Biochem. Biophys. 471 (2008) 57-62
20. 2+ release. Antioxid. Redox Signal. 3 (2008) 525-530
21. Batandier C., Fontaine E., Kériel C., and Leverve X.M. Determination of mitochondrial reactive oxygen species: methodological aspects. J. Cell. Mol. Med. 6 (2002) 175-187
22. Kudin A.P., Bimpong-Buta N.Y., Vielhaber S., Elger C.E., and Kunz W.S. Characterization of superoxide-producing sites in isolated brain mitochondria. J. Biol. Chem. 279 (2004) 4127-4135
23. Cereda A., Carpen A., Picariello G., Tedeschi G., and Pagani S. The lack of rhodanese RhdA affects the sensitivity of Azotobacter vinelandii to oxidative events. Biochem. J. 418 (2009) 135-143
24. Lecker S.H., Jagoe R.T., Gilbert A., et al. Multiple types of skeletal muscle atrophy involve a common program of changes in gene expression. FASEB J. 18 (2004) 39-51
25. Horowitz P.M., Butler M., and McClure G.D. Reducing sugars can induce the oxidative inactivation of rhodanese. J. Biol. Chem. 267 (1992) 23596-23600
26. Hasuike Y., Nakanishi T., Moriguchi R., et al. Accumulation of cyanide and thiocyanate in haemodialysis patients. Nephrol. Dial Transplant. 19 (2004) 1474-1479
27. Mendoza J.A., Rogers E., Lorimer G.H., and Horowitz P.M. Chaperonins facilitate the in vitro folding of monomeric mitochondrial rhodanese. J. Biol. Chem. 266 (1991) 13044-13049
28. Brazil B.T., and Horowitz P.M. The hydrophobic properties of GroEL: a review of ligand effects on the modulation of GroEL hydrophobic surfaces. Cell. Stress Chaperones 4 (1999) 177-190
29. Melkani G.C., Zardeneta G., and Mendoza J.A. GroEL interacts transiently with oxidatively inactivated rhodanese facilitating its reactivation. Biochem. Biophys. Res. Commun. 294 (2002) 893-899
30. Vaziri N.D., Dicus M., Ho N.D., Boroujerdi-Rad L., and Sindhu R.K. Oxidative stress and dysregulation of superoxide dismutase and NADPH oxidase in renal insufficiency. Kidney Int. 63 (2003) 179-185
31. Crowe A.V., McArdle A., McArdle F., et al. Markers of oxidative stress in the skeletal muscle of patients on haemodialysis. Nephrol. Dial Transplant. 22 (2007) 1177-1183
32. Jiang N., Zhang G., Bo H., et al. Upregulation of uncoupling protein-3 in skeletal muscle during exercise: a potential antioxidant function. Free Rad. Med. 46 (2009) 138-145
33. Ryter S.W., Kim H.P., Hoetzel A., et al. Mechanisms of cell death in oxidative stress. Antioxid. Redox Signal. 9 (2007) 49-89
34. Monsalve M., Borniquel S., Valle I., and Lamas S. Mitochondrial dysfunction in human pathologies. Front. Biosci. 12 (2007) 1131-1153
35. Valko M., Rhodes C.J., Moncol J., Izakovic M., and Mazur M. Free radicals, metals and antioxidants in oxidative stress-induced cancer. Chem. Biol. Interact. 160 (2006) 1-40