Activities of cytochrome c oxidase and mitochondrial lactate dehydrogenase isozymes and Cox1, Cox2, Cox4, and Cox6 gene subunit expression in cold adaptation of
详细信息 查看全文
- 作者：O. V. Meshcheryakova ; M. V. Churova…
- 关键词：cytochrome c oxidase ; gene expression ; mitochondrial lactate dehydrogenase ; Michaelis–Menten constant ; cold adaptation ; brown trout
- 刊名：Russian Journal of Bioorganic Chemistry
- 出版年：2016
- 出版时间：March 2016
- 年：2016
- 卷：42
- 期：2
- 页码：162-169
- 全文大小：406 KB
- 参考文献：1.White, C.R., Alton, L.A., and Frappell, P.B., Proc. Biol. Sci., 2012, vol. 279, pp. 1740–1747.CrossRef PubMed PubMedCentral
2.Somero, G., Comprehensive Physiology, Published Online: JAN 1, 2011. http://onlinelibrary.wiley.com/doi/10.1002/cphy.cp130219/
3.Boldyrev, A.A., Soros. Obrazovat. Zh., 1997, no. 6, pp. 21–27.
4.Capaldi, R.A., Annu. Rev. Biochem., 1990, vol. 59, pp. 569–596.CrossRef PubMed
5.Kadenbach, B. Huttemann, M., et al., Free Radic. Biol. Med., 2000, vol. 29, pp. 211–221.CrossRef PubMed
6.Carr, H.S., Acc. Chem. Res., 2003, vol. 36, pp. 309–316.CrossRef PubMed
7.Richter, O.M. and Ludwig, B., Rev. Physiol. Biochem. Pharmacol., 2003, vol. 147, pp. 47–74.PubMed
8.Fontanesi, F., 1st., Soto, I.C., Horn, D., and Barrientos, A., Am. J. Physiol. Cell. Physiol., 2006, vol. 291, pp. 1129–1147.CrossRef
9.LeMoine, C.M., Genge, C.E., and Moyes, C.D., J. Exp. Biol., 2008, vol. 211, pp. 1448–1455.CrossRef PubMed
10.Duggan, A.T., Kocha, K.M., Monk, C.T., Bremer, K., and Moyes, C.D., J. Exp. Biol., 2011, vol. 214, pp. 1880–1887.CrossRef PubMed
11.Dong, Y. and Somero, G., J. Exp. Biol., 2009, vol. 212, pp. 169–177.CrossRef PubMed
12.Somero, G.N., Comp. Biochem. Physiol., B: Biochem. Mol. Biol., 2004, vol. 139, pp. 321–333.CrossRef
13.Meshcheryakova, O.V., Churova, M.V., and Nemova, N.N., Trudy Karel. Nauch. Tsentra RAN, 2013, no. 3, pp. 136–142.
14.Battersby, B.J. and Moyes, C.D., Am. J. Physiol., 1998, vol. 275, pp. 905–912.
15.Hardewig, P., van Dijk, M., Moyes, C.D., and Portner, H.O., Am. J. Physiol. Regulat. Integrat. Comp. Physiol., 1999, vol. 277, no. 2, pp. 508–516.
16.Lucassen, M., Koschnik, N., Eckerle, L., and Portner, H., J. Exp. Biol., 2006, vol. 209, pp. 2462–2471.CrossRef PubMed
17.Guderley, H., Comp. Biochem. Physiol. B: Biochem. Mol. Biol., 2004, vol. 139, pp. 371–382.CrossRef
18.O’Brien, K.M., J. Exp. Biol., 2011, vol. 214, pp. 275–285.CrossRef PubMed
19.Williams, R., Salmons, S., Newsholme, E., Kaufman, R., and Mellor, G., J. Biol. Chem., 1996, vol. 261, pp. 376–380.
20.Stiburek, L., Hansikova, H., Tesarova, M., Cerna, L., and Zeman, J., Physiol. Res., 2006, vol. 55, Suppl. 2, pp. 27–41.
21.Fontanesi, F., Soto, I.C., and Barrientos, A., IUBMB Life, 2008, vol. 60, pp. 557–568.CrossRef PubMed PubMedCentral
22.Hyung, J., Khalimonchuk, O., Smith, P., and Winge, D., Biochim. Biophys. Acta, 2012, vol. 1823, pp. 1604–1616.CrossRef
23.Little, A.G., Kocha, K.M., Lougheed, S.C., and Moyes, C.D., Physiol. Genomics, 2010, vol. 42, pp. 76–84.CrossRef PubMed
24.Huttemann, M., Biochim. Biophys. Acta, 2000, vol. 1492, pp. 242–246.CrossRef PubMed
25.Ugalde, C., Coenen, M.H., Farhoud, S., Gilinsky, S., Koopman, W.J., Heuvel, L.P., Smeitink, J.A., and Nijtmans, L.G., Mitochondrion, 2002, vol. 2, pp. 117–128.CrossRef PubMed
26.Hashimoto, T. and Brooks, G.A., Med. Sci. Sport Exerc., 2008, vol. 40, no. 3, pp. 486–494.CrossRef
27.Hashimoto, T., Hussien, R., Cho, H.S., Kaufer, D., and Brooks, G.A., PLoS ONE, 2008, vol. 3, p. 2915.CrossRef
28.Smith, L., J. Methods Biochem. Analysis, 1955, vol. 2, no. 427, pp. 427–434.CrossRef
29.Kochetov, G.A., in Prakticheskoe rukovodstvo po enzimologii (A Practical Guide to Enzymology), Moscow: Vysshaya shkola, 1980.
30.Maurer, H.R., Disc Electrophoresis and Related Techniques of Polyacrylamide Gel Electrophoresis, Berlin: Walter de Gruyter, 1971.
31.Cornish-Bowden, A., Fundamentals of Enzyme Kinetics, London: Portland Press, 1976.
32.Livak, K.J. and Schmittgen, T.D., Methods, 2001, vol. 25, pp. 402–408.CrossRef PubMed
M. V. Churova (1)
A. E. Veselov (1)
N. N. Nemova (1)
1. Institute of Biology, Karelian Research Centre, Russian Academy of Science, ul. Pushkinskaya 11, Petrozavodsk, 185910, Russia
Biochemistry
Bioorganic Chemistry
Organic Chemistry
Biomedicine
Russian Library of Science
文摘
Characteristic changes in some parameters of white muscle mitochondria (mitochondrial volume, activity of cytochrome c oxidase (COX, EC 1.9.3.1) and the level of Cox1, Cox2, Cox4, and Cox6 subunit gene expression and activity and kinetic characteristics of mitochondrial lactate dehydrogenase isozymes (mtLDH, EC 1.1.1.27)) in adaptation to seasonal decrease in temperature from 16 to 6°C of one-year juvenile brown trout Salmo trutta L. from rivers of Lake Onega basin were investigated. A 1.5-fold increase in the activity of COX, and the increase in the levels of gene expression of both Cox4 and Cox6 nuclear subunits and increased activity of mitochondrial LDH isozymes, which have a low affinity towards lactate, has been shown. The possible role of nuclear and mitochondrial subunits of cytochrome c oxidase in improving the efficiency of the enzyme in molecule biogenesis and further modulation of its activity, as well as regulation of pyruvate formation to maintain the required rate of oxidative phosphorylation in mitochondria under low temperature were discussed.