Preview

Nephrology (Saint-Petersburg)

Advanced search

CATALASE METABOLISM IN RATS WITH CHRONIC GLOMERULONEPHRITIS

https://doi.org/10.24884/1561-6274-2004-8-3-70-73

Abstract

THE AIM of the investigation was to study catalase metabolism in experimental animals with chronic glomerulonephritis. MATERIAL AND METHODS. The work was carried out in not thoroughbred male white rats with body mass 140160 g. Experimental model of glomerulonephritis (Heimann nephritis) was induced in experimental animals by intramuscular injecting homogenate of healthy rat kidneys in Freund’s adjuvant. The biochemical indices in rats were specified in three weeks after autoimmunization of the animals. RESULTS. It was found that chronic glomerulonephritis resulting from oxidative stress was followed by a sharp drop of catalase activity. It was shown to be due to a sharp inhibition of the rate of accumulation (Ks) of enzyme protein (from 5 to 8 times) in blood, kidneys and liver of the rats with glomerulonephritis as compared with control animals and to lead to a reliable decrease of catalase concentration in those tissues. At the same time the obviously compensatory decrease of decomposition (Kd) of the fermentative protein was observed and, as a result, a longer period of its «halflife» (t1/2) which in certain degree compensated the deficit of newly synthesized molecules of catalase. CONCLUSION. It was established that the earlier found reliable drop of catalase activity in blood, kidneys and liver of rats during the development of glomerulonephritis was due to sharply decreased rate of its biosynthesis / accumulation in these tissues.

About the Authors

N. V. Kirillova
Санкт-Петербургская государственная химико-фармацевтическая академия
Russian Federation


M. M. Debel
Санкт-Петербургская государственная химико-фармацевтическая академия
Russian Federation


References

1. Альдебель ММ, Кириллова НВ. Окислительное повреждение белков при экспериментальном гломерулонефрите. Нефрология 2003; 6 (2): 7376

2. Halliwell B. Free radicals, antioxidants and human disease: curiosity, cause, or consequence. Lancet 1994; 344: 721724

3. Fridovich I. Superoxide radical and Superoxide dismutase. Annu Rev Biochem 1995; 64: 97112

4. Escobar JA, Rubio MA, Lissi EA. SOD and catalase inactivation by singlet oxygen and peroxyl radicals. Free Radical Biol Med 1996; 20 (3 ): 285290

5. Fridovich I. Superoxide dismutase anion radical, superoxide dismutases, and related matters. J Biol Chem 1997; 272: 1851518517

6. Wallace SS. Oxidative stress and the molecular biology of antioxidant defenses. In: Scandalios JG ed. CSHL Press, 1997; 4990

7. Западнюк ИП, Западнюк ВИ, Захария УА, Западнюк БВ. Лабораторные животные. Разведение, содержание, использование в эксперименте. Вища школа, Киев, 1983; 383

8. Альбини Б. Иммунопатология почки. Медицина, М., 1983; 116259

9. Butler E. Red cell metabolism. New York; London, 1975; 198

10. Chiga M, Redy J, Svoboda D. Degradation kinetics of liver catalase in rats treated with ethylαp chlorphenoxyisobutirate. Lab Invest 1971; 25: 4952

11. Schimke RT, Bradly MO. Properties of protein turnover in animal cells and a possible role for turnover in quality control of proteins. Proteinases and biological control. In: Reich E, Rifkin DE, Shaw E, eds. Gold Spring Harbor Lab., 1975; 2: 515 530

12. Price VE, Strerling WR, Tarantola VA, Rеchcingle MJ. The kinetics of catalase synthesis and distruction in vivo. J Biol Chem 1962; 237: 3468 – 3476

13. Смирнова ГВ, Музыка НГ, Глуховенко МН, Октябрьс кий ОН. Устойчивость к окислительному стрессу у штаммов E. coli, дефицитных по синтезу глутатиона. Биохимия 1999; 64 (10): 13181324

14. Fridovich I. Biological effects of the superoxide radical. Arch Biochem Biophys 1986; 247: 111

15. Arias IM, Dogle D, Schimke RT. Studies on the synthesis and dagradation of the endoplasmic reticulum of rat liver. J Biol Chem 1969; 244 (12): 33033315

16. Jones GL, Msters CJ. On the turnover and proteolysis of catalase in tissue of the guinea pig and acatalasemic mice. Acta Biochem Biophys 1976; 173: 463489

17. Loewen PC. Molecular Biology of free radical scavering systems. Laboratory Press Cold Spring Harbor, NewYork, 1992; 97115

18. Копылов ПХ. Изучение биосинтеза и посттрансляционного созревания отдельных молекулярных форм ката лазы печени крыс в норме и при некоторых экстремальных воздействиях на организм. Дисс. ……канд. наук. ЛХФИ, Л., 1983; 175 с.

19. Nakamura A, Minakami S. Turnover of hepatic catalase modified by aminotriazole. J Biochem 1973; 74( 4): 683689

20. Poole B, Leighton F, de Duve Ch. The synthesis and turnover of rat liver peroxisomes. J Cell Biol 1969; 41: 536546

21. Carney JM, StarkeReed PE, Oliver CN et al. Reversal of agerelated changes in brain protein oxidation, decrease in enzymatic activity, and loss in temporal and spatial memory by chronic administration of the spin trapping compound Ntret butilaphenilnitrone. Proc Nath Acad Sci USA 1991; 88: 3633 3636

22. Комов ВП, Рахманина ТФ. Синтез каталазы печени крыс при опухолевом росте. Вопр онкологии 1974; 20 (11): 4850


Review

For citations:


Kirillova N.V., Debel M.M. CATALASE METABOLISM IN RATS WITH CHRONIC GLOMERULONEPHRITIS. Nephrology (Saint-Petersburg). 2004;8(3):70-73. (In Russ.) https://doi.org/10.24884/1561-6274-2004-8-3-70-73

Views: 411


ISSN 1561-6274 (Print)
ISSN 2541-9439 (Online)