350 rub
Journal №1 for 2015 г.
Article in number:
Structural-functional state of the cytochromic part of liver mitochondria respiratory chain under the conditions of alimentary deprivation of protein
Keywords:
alimentary deprivation of protein
mitochondria
cytochromes b
c1
с
aа3
cytochrome oxidase
δ
-aminolevulinate synthase
heme oxygenase
Authors:
O.N. Voloshchuk - Ph.D. (Biol.), Associate Professor, Yuriy Fedkovych Chernivtsi National University (Chernivtsi, Ukraine). E-mail: oxbm@mail.ru
G.P. Kopylchuk - Dr.Sc. (Biol.), Professor, Yuriy Fedkovych Chernivtsi National University (Chernivtsi, Ukraine). E-mail: kopilchuk@gmail.com
G.P. Kopylchuk - Dr.Sc. (Biol.), Professor, Yuriy Fedkovych Chernivtsi National University (Chernivtsi, Ukraine). E-mail: kopilchuk@gmail.com
Abstract:
Activity of the key enzyme of the cytochromic part of respiratory chain - cytochrome oxidase, quantitative redistribution of the mitochondrial cytochromes b, c1, с and aа3, activity of the key enzymes of cytochromes - heme metabolism ? δ-aminolevulinate synthase and heme oxygenase under the conditions of alimentary deprivation of protein were studied in the research.
The research was carried out on white non-linear rats, divided according to quantity of protein in the ration into groups: 1 - rats maintained on low-protein diet, 2 - rats maintained on full semi-synthetic ration.
It was estimated, that under the conditions of alimentary deprivation of protein decrease of the quantitative content of mitochondrial cytochromes b, c1, с and aа3 in the liver mitochondrial fraction, inhibition of the activity of key enzyme of the cytochromic part of respiratory chain - cytochrome oxidase against the background increase of the heme oxygenase activity and maintenance on the control level δ-aminolevulinate synthase activity is observed. Conclusion was made, that estimated changes of the structural-functional organization of cytochromic part of respiratory chain may be considered as one of the possible mechanisms of energy biotransformation system disturbances under the conditions of alimentary deprivation of protein.
Pages: 43-47
References
- Xarchenko N.V., Anoxina G.A., Kravchenko V.V. Optimizacziya parenteral'nogo pitaniya bol'ny'x v posleoperaczionny'j period // Suchasna gastroenterologіya. 2012. № 4 (66). S. 76 - 79.
- Pasini E., Aquilani R., Dioguardi F.S., D'Antona G., Gheorghiade M., Taegtmeyer H. Hypercatabolic syndrome: Molecular basis and effects of nutritional supplements with aminoacids // Am. J. Cardiol. 2008. V. 101 (1). P. 11E-15E.
- Sangar V., Eddy A., Price N.D., Simeonidis E. Mechanistic modeling of aberrant energy metabolism in human disease // Front. Physiol. 2012. V. 3. P. 404.
- Tanakaa M., Ishibashia T., Toyomizua M. Time course of oxidative phosphorylation in liver mitochondria of chickens fed on high-protein diet // British Poultry Science. 1995. V. 36. № 1. R. 143-154.
- Tyzbir R.S., Kunin A.S., Sims N.M., Danforth E.Jr. Influence of diet composition on serum triiodothyronine concentration, hepatic mitochondrial metabolism and shuttle system activity in rats // J. Nutr. 1981. V. 111(2). P. 252-259.
- Theys N., Bouckenooghe T., Ahn M.T., Remacle C., Reusens B. Maternal low-protein diet alters pancreatic islet mitochondrial function in a sex-specific manner in the adult rat // Am. J. Physiol. Regul. Integ. Comp. Physiol. 2009. V. 297. P. 1516-1525.
- Jia Y., Li R., Cong R. et al. Maternal low-protein diet affects pigenetic regulation of hepatic mitochondrial DNA transcription in a sex-specific manner in newborn piglets associated with GR binding to its promoter // PLoS One. 2013. V. 8. № 5. e63855.
- Voloshhuk O.N., Kopy'l'chuk G.P., Kadajskaya T.G. Sostoyanie sistemy' e'nergoobespecheniya mitoxondrij pecheni v usloviyax alimentarnoj deprivaczii proteina // Voprosy' pitaniya. 2014. № 3. S. 12-16.
- Barannik T.V., Inshina N.M., Kaliman P.A. Free heme pool and activity of key enzyme of heme synthesis in the rat liver under action of agents affecting reduced glutathione level // Ukr. bіoxіm. zhurn. 2005. T. 77. № 5. S. 120-122.
- Bansal S., Biswas G., Avadhan N.G. Mitochondria-targeted heme oxygenase-1 induces oxidative stress and mitochondrial dysfunction in macrophages, kidney fibroblasts and in chronic alcohol hepatotoxicity // Redox Biology. 2014. V. 2. P. 273-283.
- Reeves P., Nielsen F., Fahey G. AIN-93 Purified Diets for Laboratory Rodents: Final Report of the American Institute of Nutrition Ad Hoc Writing Committee on the Reformulation of the AIN-76A Rodent Diet // J. Nutr. 1993. V. 123. № 11. P. 1939-1951.
- Voloshhuk O.N., Marchenko M.M. Vliyanie maly'x doz radiaczii na glutamatdegidrogenaznuyu aktivnost' tkanej kry's s transplantirovannoj karczinomoj Gerena // Byulleten' e'ksperimental'noj biologii i medicziny'. 2013. T. 156. № 7. S. 103-106.
- Voloshhuk O.N., Marchenko M.M., Mudrak M.S. Izmenenie strukturno-funkczional'noj organizaczii czitoxromnogo uchastka dy'xatel'noj czepi karczinomy' Gerena predvaritel'no obluchenny'x opuxolenositelej // Biomediczinskaya ximiya. 2012. T. 58. № 6. S. 684-690.
- Collins A., Marver H., Tschudy P. δ-Aminolevulinic Acid Synthetase // J. Biol. Chem. 1966. V. 241. № 19. P. 4323-4329.
- Converso D.P., Taille C., Carreras M.S., Jaitovich A. et al. HO-1 is located in liver mitochondria and modulates mitochondrial heme content and metabolism // The FASEB Journal. 2006. V. 20. № 8. R. 1236-1238.
- Lowry O.H., Rosenbrough M.J., Farr A.L., Rendal R.J. Protein measurement with the folin phenol reagent // J. Biol. Chem. 1951. V. 193. № 1. P. 265-275.
- Kim H.J., Khalimonchuk O., Smith P.M., Winge D.R. Structure, function, and assembly of heme centers in mitochondrial respiratory complexes // Biochim. Biophys. Acta. 2012. V. 1823(9). P. 1604-1616.
- Smith P.M., Fox J.L., Winge D.R. Biogenesis of the cytochrome bc1 complex and role of assembly factors // Biochim. Biophys. Acta. 2012. V. 1817 (6). P. 872-882.
- Vartak R., Porras C. A.-M., Bai Y. Respiratory supercomplexes: structure, function and assembly // Protein & Cell. 2013. V. 4. № 8. P. 582-590.
- Djeridane Y., Lyoumi S., Puy H., Touitou Y. Light Pulse Induces Ala-S Gene Expression in the Rat Harderian Gland // J. Physiol. Pharmacol. 2010. V. 61. № 1. R. 115-117.