Ukr.Biochem.J. 2016; Volume 88, Issue 1, Jan-Feb, pp. 79-87

doi: https://doi.org/10.15407/ubj88.01.079

Amine oxidases as important agents of pathological processes of rhabdomyolysis in rats

O. O. Gudkova, N. V. Latyshko, S. G. Shandrenko

Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv;
e-mail: ogudkova@biochem.kiev.ua

In this study we have tested an idea on the important role of amine oxidases (semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase) as an additional source of oxidative/carbonyl stress under glycerol-induced rhabdomyolysis, since the enhanced formation of reactive oxygen species and reactive carbonyl species in a variety of tissues is linked to various diseases. In our experiments we used the sensitive fluorescent method devised for estimation of amine oxidases activity in the rat kidney and thymus as targeted organs under rhabdomyolysis. We have found in vivo the multiple rises in activity of semicarbazide-sensitive amine oxidase, diamine oxidase, polyamine oxidase (2-4.5 times) in the corresponding cell fractions, whole cells or their lysates at the 3-6th day after glycerol injection. Aberrant antioxidant activities depended on rhabdomyolysis stage and had organ specificity. Additional treatment of animals with metal chelator ‘Unithiol’ adjusted only the activity of antioxidant enzymes but not amine oxidases in both organs. Furthermore the in vitro experiment showed that Fenton reaction (hydrogen peroxide in the presence of iron) products alone had no effect on semicarbazide-sensitive amine oxidase activity in rat liver cell fraction whereas supplementation with methylglyoxal resulted in its significant 2.5-fold enhancement. Combined action of the both agents had additive effect on semicarbazide-sensitive amine oxidase activity. We can assume that biogenic amine and polyamine catabolism by amine oxidases is upregulated by oxidative and carbonyl stress factors directly under rhabdomyolysis progression, and the increase in catabolic products concentration contributes to tissue damage in glycerol-induced acute renal failure and apoptosis stimulation in thymus.

Keywords: , , , ,


References:

  1. Dalle-Donne I, Rossi R, Colombo R, Giustarini D, Milzani A. Biomarkers of oxidative damage in human disease. Clin Chem. 2006 Apr;52(4):601-23. PubMed, CrossRef
  2. Miyata T, Izuhara Y, Sakai H, Kurokawa K. Carbonyl stress: increased carbonyl modification of tissue and cellular proteins in uremia. Perit Dial Int. 1999;19 Suppl 2:S58-61. PubMed
  3. Khan FY. Rhabdomyolysis: a review of the literature. Neth J Med. 2009 Oct;67(9):272-83. Review. PubMed
  4. Shandrenko SH. Labile iron pool formation in rat’s blood under rhabdomyolysis. Ukr Biokhim Zhurn. 2012 Nov-Dec;84(6):124-30. Ukrainian. PubMed
  5. Chumachenko IM, Kapustyanenko LG, Shandrenko SG. Blood labile iron effect on nitrosative stress development under rat experimental rhabdomyolysis. Studia Biologica. 2012; 6(3): 105-114. (In Ukranian).
  6. Aydogdu N, Erbas H, Atmaca G, Erten O, Kaymak K. Melatonin reduces nitric oxide via increasing arginase in rhabdomyolysis-induced acute renal failure in rats. Ren Fail. 2006;28(5):435-40. PubMed, CrossRef
  7. Bagley WH, Yang H, Shah KH. Rhabdomyolysis. Intern Emerg Med. 2007 Oct;2(3):210-8. Review. PubMed, CrossRef
  8. Abboud HE, Ou SL, Velosa JA, Shah SV, Dousa TP. Dynamics of renal histamine in normal rat kidney and in nephrosis induced by aminonucleoside of puromycin. J Clin Invest. 1982 Feb;69(2):327-36. PubMed, PubMedCentral, CrossRef
  9. Floris G, Mondovi B. Copper amine oxidases: structures, catalytic mechanisms and role in pathophysiology. CRC Press, 2009; 374 p. CrossRef
  10. Yu PH, Zuo DM. Oxidative deamination of methylamine by semicarbazide-sensitive amine oxidase leads to cytotoxic damage in endothelial cells. Possible consequences for diabetes. Diabetes. 1993 Apr;42(4):594-603. PubMed, CrossRef
  11. Yu PH, Zuo DM. Formaldehyde produced endogenously via deamination of methylamine. A potential risk factor for initiation of endothelial injury. Atherosclerosis. 1996 Feb;120(1-2):189-97. PubMed, CrossRef
  12. Wong M, Saad S, Zhang J, Gross S, Jarolimek W, Schilter H, Chen JA, Gill AJ, Pollock CA, Wong MG. Semicarbazide-sensitive amine oxidase (SSAO) inhibition ameliorates kidney fibrosis in a unilateral ureteral obstruction murine model. Am J Physiol Renal Physiol. 2014 Oct 15;307(8):F908-16. PubMed, CrossRef
  13. Duperray A, Mantovani A, Introna M, Dejana E. Endothelial cell regulation of leukocyte infiltration in inflammatory tissues. Mediators Inflamm. 1995;4(5):322-30. PubMed, PubMedCentral, CrossRef
  14. Kaminska AM, Stern LZ, Russell DH. Altered muscle polyamine levels in human neuromuscular diseases. Ann Neurol. 1981 Jun;9(6):605-7. PubMed, CrossRef
  15. Sakata K, Kashiwagi K, Sharmin S, Ueda S, Igarashi K. Acrolein produced from polyamines as one of the uraemic toxins. Biochem Soc Trans. 2003 Apr;31(2):371-4. PubMed, CrossRef
  16. Latyshko N, Gudkova O, Dmytrenko M. Semicarbazide as potential source of formaldehyde and nitric oxide formation. Drugs Therapy Studies. 2012; 2(1): 43-47. CrossRef
  17. Strober W. Trypan blue exclusion test of cell viability. Curr Protoc Immunol. 2001 May;Appendix 3:Appendix 3B. PubMed, CrossRef
  18. Caillet S, Yu H, Lessard S, Lamoureux G, Ajdukovic D, Lacroix M. Fenton reaction applied for screening natural antioxidants. Food Chem. 2007 Jan; 100(2):542-552. CrossRef
  19. Hirakawa K. Fluorometry of hydrogen peroxide using oxidative decomposition of folic acid. Anal Bioanal Chem. 2006 Sep;386(2):244-8. PubMed, CrossRef
  20. Wheeler CR, Salzman JA, Elsayed NM, Omaye ST, Korte DW Jr. Automated assays for superoxide dismutase, catalase, glutathione peroxidase, and glutathione reductase activity. Anal Biochem. 1990 Feb 1;184(2):193-9. PubMed, CrossRef
  21. Eriksson UJ, Borg LA. Protection by free oxygen radical scavenging enzymes against glucose-induced embryonic malformations in vitro. Diabetologia. 1991 May;34(5):325-31. PubMed, CrossRef
  22. Beers RF Jr, Sizer IW. A spectrophotometric method for measuring the breakdown of hydrogen peroxide by catalase. J Biol Chem. 1952 Mar;195(1):133-40. PubMed
  23. Johansson LH, Borg LA. A spectrophotometric method for determination of catalase activity in small tissue samples. Anal Biochem. 1988 Oct;174(1):331-6. PubMed, CrossRef
  24. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem. 1976 May 7;72(1-2):248-54. PubMed, CrossRef
  25. Vetrano AM, Heck DE, Mariano TM, Mishin V, Laskin DL, Laskin JD. Characterization of the oxidase activity in mammalian catalase. J Biol Chem. 2005 Oct 21;280(42):35372-81. PubMedCrossRef
  26. Prousek J. Fenton chemistry in biology and medicine. Pure Appl Chem. 2007 Jan; 79(12): 2325-2338. CrossRef
  27. Bachrach U, Heimer YM. The Physiology of Polyamines, Vol. 1. CRC Press, Inc. 1989; 368 p.
  28. Latyshko NV, Gudkova LV, Gudkova OA. Effect of polyamines on superoxide dismutase activity under dexamethasone-induced apoptosis in rat thymocytes. Ukr Biokhim Zhurn. 2008 May-Jun;80(3):78-83. PubMed

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