Functional Significance of the Mitochondrial Membrane Potential

Pleiades Publishing Ltd - Tập 12 Số 1 - Trang 20-26 - 2018
Ljubava D. Zorova1, Vasily A. Popkov1, Egor Y. Plotnikov1, Denis N. Silachev1, Irina B. Pevzner1, Stanislovas S. Jankauskas1, Savva D. Zorov2, Valentina A. Babenko3, Dmitry B. Zorov3
1Belozersky Institute of Physico-chemical biology, Moscow Lomonosov State University, Moscow, 119991, Russia
2Faculty of Bioengineering and Bioinformatics, Moscow Lomonosov State University, Moscow, 119991, Russia
3Kulakov Scientific Center of Obstetrics, Gynecology and Perinatology, Moscow, 117997, Russia

Tóm tắt

Từ khóa


Tài liệu tham khảo

Mitchell P. 1961. Coupling of phosphorylation to electron and hydrogen transfer by a chemi-osmotic type of mechanism. Nature. 191, 144–148.

Mitchell P. 1966. Chemiosmotic coupling in oxidative and photosynthetic phosphorylation. Biol. Rev. Cambridge Philos. Soc. 41, 445–502.

Liberman E.A., Topaly V.P., Tsofina L.M., Jasaitis A.A., Skulachev V.P. 1969. Mechanism of coupling of oxidative phosphorylation and the membrane potential of mitochondria. Nature. 222, 1076–1078.

Williams R.J. 1961. Possible functions of chains of catalysts. J. Theor. Biol. 1, 1–17.

Medvedev E.S., Stuchebrukhov A.A. 2014. Mechanisms of generation of local pH in mitochondria and bacteria. Biochemistry (Moscow). 79, 425–434.

Eremeev S.A., Yaguzhinsky L.S. 2015. On Local Coupling of Electron Transport and ATP-Synthesis System in Mitochondria. Theory and Experiment. Biochemistry (Moscow). 80, 576–581.

Johnson L.V., Walsh M.L., Bockus B.J., Chen L.B. 1981. Monitoring of relative mitochondrial membrane potential in living cells by fluorescence microscopy. J. Cell Biol. 88, 526–535.

Pinchot G.B. 1960. A high-energy intermediate of oxidative phosphorylation. Proc. Natl. Acad. Sci. USA. 46, 929–938.

Griffiths D.E., Chaplain R.A. 1962. Evidence for a phosphorylated intermediate in oxidative phosphorylation. Biochem. Biophys. Res. Comm. 8, 497–500.

Slater E.C., Kemp A., Jr., Tager J.M. 1964. Utilization of high-energy intermediates of oxidative phosphorylation and the proposed function of imidazole phosphate as an intermediate in oxidative phosphorylation. Nature. 201, 781–784

Glagolev A.N., Skulachev V.P. 1978. The proton pump is a molecular engine of motile bacteria. Nature. 272, 280–282.

Rikmenspoel R., Sinton S., Janick J.J. 1969. Energy conversion in bull sperm flagella. J. Gen. Physiol. 54, 782–805.

Davis T.R., Johnston D.R., Bell F.C., Cremer B.J. 1960. Regulation of shivering and non-shivering heat production during acclimation of rats. Am. J. Physiol. 198, 471–475.

Cannon B., Nedergaard J. 2011. Nonshivering thermogenesis and its adequate measurement in metabolic studies. J. Exp. Biol. 214, 242–253.

Skulachev V.P., Maslov S.P., Sivkova V.G., Kalinichenko L.P., Maslova G.M. 1963. Cold uncoupling of oxidative phosphorylation in the muscles of white mice. Biokhimiia (Rus.). 28, 70–79.

Mokhova E.N., Zorov D.B. 1973. Effect of cold stress on respiration of diaphragm muscle. J. Bioenerg. 5, 119–128.

Hirokawa N., Bloom G.S., Vallee R.B. 1985. Cytoskeletal architecture and immunocytochemical localization of microtubule-associated proteins in regions of axons associated with rapid axonal transport: The beta, beta’-iminodipropionitrile-intoxicated axon as a model system. J. Cell Biol. 101, 227–239.

Linden M., Nelson B.D., Leterrier J.F. 1989. The specific binding of the microtubule-associated protein 2 (MAP2) to the outer membrane of rat brain mitochondria. Biochem. J. 261, 167–173.

Nekrasova O.E., Mendez M.G., Chernoivanenko I.S., Tyurin-Kuzmin P.A., Kuczmarski E.R, Gelfand V.I., Goldman R.D., Minin A.A. 2011. Vimentin intermediate filaments modulate the motility of mitochondria. Mol. Biol. Cell. 22, 2282–2289.

Monaghan R.M., Whitmarsh A.J. 2015. Mitochondrial proteins moonlighting in the nucleus. Trends Biochem. Sci. 40, 728–735.

Kleine T., Leister D. 2016. Retrograde signaling: Organelles go networking. Biochim. Biophys. Acta. 1857, 1313–1325.

Popkov V.A., Zorova L.D., Korvigo I.O., Silachev D.N., Jankauskas S.S., Babenko V.A., Pevzner I.B., Danilina T.I., Zorov S.D., Plotnikov E.Y., Zorov D.B. 2016. Do mitochondria have an immune system? Biochemistry (Moscow), 81, 1229–1236.

Sutovsky P., Moreno R.D., Ramalho-Santos J., Dominko T., Simerly C., Schatten G. 2000. Ubiquitinated sperm mitochondria, selective proteolysis, and the regulation of mitochondrial inheritance in mammalian embryos. Biol. Reprod. 63, 582–590.

Margulis L. 1971. Symbiosis and evolution. Sci. Amer. 225, 48–57.

Zorov D.B., Plotnikov E.Y., Silachev D.N., Zorova L.D., Pevzner I.B., Zorov S.D., Babenko V.A., Jankauskas S.S., Popkov V.A., Savina P.S. 2014. Microbiota and mitobiota. Putting an equal sign between mitochondria and bacteria. Biochemistry (Moscow). 79, 1017–1031.

Di Lisa F., Blank P.S., Colonna R., Gambassi G., Silverman H.S., Stern M.D., Hansford R.G. 1995. Mitochondrial membrane potential in single living adult rat cardiac myocytes exposed to anoxia or metabolic inhibition. J. Physiol. 486 (Pt 1), 1–13.

Pullman M.E., Monroy G.C. 1963. A naturally occurring inhibitor of mitochondrial adenosine triphosphatase. J. Biol. Chem. 238, 3762–3769.

Hashimoto T., Yoshida Y., Tagawa K. 1990. Regulatory proteins of F1F0-ATPase: Role of ATPase inhibitor. J. Bioenerg. Biomembr. 22, 27–38.

Zorov D.B., Juhaszova M., Sollott S.J. 2014. Mitochondrial reactive oxygen species (ROS) and ROSinduced ROS release. Physiol. Rev. 94, 909–950.

Neupert W., Herrmann J.M. 2007. Translocation of proteins into mitochondria. Ann. Rev. Biochem. 76, 723–749.

Attardi G., Schatz G. 1988. Biogenesis of mitochondria. Ann. Rev. Cell Biol. 4, 289–333.

Zimmerman R., Paluch U., Sprinzl M., Neupert W. 1979. Cell-free synthesis of the mitochondrial ADP/ATP carrier protein of Neurospora crassa. Eur. J. Biochem. 99, 247–252.

Zimmermann R., Paluch U., Neupert W. 1979. Cellfree synthesis of cytochrome c. FEBS Lett. 108, 141–146.

Garlid K.D., Paucek P. 2003. Mitochondrial potassium transport: The K(+) cycle. Biochim. Biophys. Acta. 1606, 23–41.

Hansford R.G., Zorov D. 1998. Role of mitochondrial calcium transport in the control of substrate oxidation. Mol. Cell. Biochem. 184, 359–369.

Maguire M.E. 2006. Magnesium transporters: Properties, regulation and structure. Front. Biosci. 11, 3149–3163.

Korshunov S.S., Skulachev V.P., Starkov A.A. 1997. High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416, 15–18

Cunha F.M., Caldeira da Silva C.C., Cerqueira F.M., Kowaltowski A.J. 2011. Mild mitochondrial uncoupling as a therapeutic strategy. Curr. Drug Targ. 12, 783–789.

Correia-Melo C., Marques F.D., Anderson R., Hewitt G., Hewitt R., Cole J., Carroll B.M., Miwa S., Birch J., Merz A., Rushton M.D., Charlesb M., Jurk D., Tait S.W., Czapiewski R., Greaves L., Nelson G., Bohlooly-Y M., Rodriguez-Cuenca S., Vidal-Puig A., Mann D., Saretzki G., Quarato G., Green D.R., Adams P.D., von Zglinicki T., Korolchuk V.I., Passos J.F. 2016. Mitochondria are required for pro-ageing features of the senescent phenotype. EMBO J. 35, 724–742.

Zorov D.B., Popkov V.A., Zorova L.D., Vorobjev I.A., Pevzner I.B., Silachev D.N., Zorov S.D., Jankauskas S.S., Babenko V.A., Plotnikov E.Y. 2017. Mitochondrial aging: Is there a mitochondrial clock? J. Gerontol. Ser. A, Biol. Sci. 72, 1171–1179.

Zorov D.B., Filburn C.R., Klotz L.O., Zweier J.L., Sollott S.J. 2000. Reactive oxygen species (ROS)-induced ROS release: A new phenomenon accompanying induction of the mitochondrial permeability transition in cardiac myocytes. J. Exp. Med. 192, 1001–1014.

Jin S.M., Lazarou M., Wang C., Kane L.A., Narendra D.P., Youle R.J. 2010. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191, 933–942.

Popkov V.A., Plotnikov E.Y., Lyamzaev K.G., Silachev D.N., Zorova L.D., Pevzner I.B., Jankauskas S.S., Zorov S.D., Babenko V.A., Zorov D.B. 2015. Mitodiversity. Biochemistry (Moscow). 80, 532–541.

Baker D.J., Childs B.G., Durik M., Wijers M.E., Sieben C.J., Zhong J., Saltness R.A., Jeganathan K.B., Verzosa G.C., Pezeshki A., Khazaie K., Miller J.D., van Deursen J.M. 2016. Naturally occurring p16(Ink4a)-positive cells shorten healthy lifespan. Nature. 530, 184–189.

Scaduto R.C., Jr., Grotyohann L.W. 1999. Measurement of mitochondrial membrane potential using fluorescent rhodamine derivatives. Biophys. J. 76, 469–477.

Forster S., Thumser A.E., Hood S.R., Plant N. 2012. Characterization of rhodamine-123 as a tracer dye for use in in vitro drug transport assays. PloS One. 7, e33253.

Fugit K.D., Anderson B.D. 2014. The role of pH and ring-opening hydrolysis kinetics on liposomal release of topotecan. J. Control. Release. 174, 88–97.