Superoxide anion, uncoupling proteins and Alzheimer's disease

Journal of Clinical Biochemistry and Nutrition

Volumn 46, Issue 3, 2010, Pages 187-194

  Wu, Zhaofei ^a,b   Zhao, Yan ^c   Zhao, Baolu ^a  

^a INSTITUTE OF BIOPHYSICS   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c HARBIN INSTITUTE OF TECHNOLOGY   (China)

Author keywords

Alzheimer's disease; Neurodegeneration; Oxidative stress; Superoxide anion; Uncoupling protein

Indexed keywords

CALCIUM; REACTIVE OXYGEN METABOLITE; SUPEROXIDE; UNCLASSIFIED DRUG; UNCOUPLING PROTEIN; UNCOUPLING PROTEIN 2; UNCOUPLING PROTEIN 4;

ALZHEIMER DISEASE; APOPTOSIS; BIOENERGY; CALCIUM METABOLISM; CELL DIFFERENTIATION; CELL PROLIFERATION; DISEASE ASSOCIATION; ENZYME ACTIVATION; HUMAN; IMMUNE RESPONSE; MICROENVIRONMENT; MITOCHONDRION; NERVE CELL; NONHUMAN; OXIDATIVE STRESS; PATHOGENESIS; PROTEIN EXPRESSION; REVIEW; SIGNAL TRANSDUCTION; THERMOGENESIS; TRANSCRIPTION INITIATION; TRANSCRIPTION REGULATION;

EID: 77952537062     PISSN: 09120009     EISSN: None     Source Type: Journal    
DOI: 10.3164/jcbn.09-104-2     Document Type: Review

References (52)

1. Grivennikova, V.G. and Vinogradov, A.D.: Generation of superoxide by the mitochondrial Complex I. Biochim. Biophys. Acta, 1757, 553-561, 2006.
2. Lin, M.T. and Beal, M.F.: Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature, 443, 787-795, 2006. (Pubitemid 44622683)
3. Echtay, K.S.: Mitochondrial uncoupling proteins - what is their physiological role?. Free Radic. Biol. Med., 43, 1351-1371, 2007.
4. Afanas'ev, I.B.: On mechanism of superoxide signaling under physiological and pathophysiological conditions. Med. Hypotheses, 64, 127-129, 2005.
5. Baas, A.S. and Berk, B.C.: Differential activation of mitogen-activated protein kinases by H2O2 and O2- in vascular smooth muscle cells. Circ. Res., 77, 29-36, 1995.
6. Huang, W.C., Chio, C.C., Chi, K.H., Wu, H.M., and Lin, W.W.: Superoxide anion-dependent Raf/MEK/ERK activation by peroxisome proliferator activated receptor gamma agonists 15-deoxy-delta(12,14)-prostaglandin J(2), ciglitazone, and GW1929. Exp. Cell Res., 277, 192-200, 2002.
7. Hongpaisan, J., Winters, C.A., and Andrews, S.B.: Calcium-dependent mitochondrial superoxide modulates nuclear CREB phosphorylation in hippocampal neurons. Mol. Cell. Neurosci., 24, 1103-1115, 2003.
8. Voet, D. and Voet, J.D.: Biochemistry, New Jersey, USA, John Wiley and Sons, 2004.
9. Akram, S., Teong, H.F., Fliegel, L., Pervaiz, S., and Clement, M.V.: Reactive oxygen species-mediated regulation of the Na+-H+ exchanger 1 gene expression connects intracellular redox status with cells' sensitivity to death triggers. Cell Death Differ., 13, 628-641, 2006.
10. Smith, J., Ladi, E., Mayer-Proschel, M., and Noble, M.: Redox state is a central modulator of the balance between self-renewal and differentiation in a dividing glial precursor cell. Proc. Natl. Acad. Sci. U.S.A., 97, 10032-10037, 2000.
11. Pimentel, D.R., Amin, J.K., Xiao, L., Miller, T., Viereck, J., Oliver-Krasinski, J., Baliga, R., Wang, J., Siwik, D.A., Singh, K., Pagano, P., Colucci, W.S., and Sawyer, D.B.: Reactive oxygen species mediate amplitude-dependent hypertrophic and apoptotic responses to mechanical stretch in cardiac myocytes. Circ. Res., 89, 453-460, 2001.
12. Sauer, H., Wartenberg, M., and Hescheler, J.: Reactive oxygen species as intracellular messengers during cell growth and differentiation. Cell. Physiol. Biochem., 11, 173-186, 2001.
13. Buetler, T.M., Krauskopf, A., and Ruegg, U.T.: Role of superoxide as a signaling molecule. News Physiol. Sci., 19, 120-123, 2004.
14. Yang, J.Q., Buettner, G.R., Domann, F.E., Li, Q., Engelhardt, J.F., Weydert, C.D., and Oberley, L.W.: v-Ha-ras mitogenic signaling through superoxide and derived reactive oxygen species. Mol. Carcinog., 33, 206-218, 2002.
15. Wang, F.S., Wang, C.J., Sheen-Chen, S.M., Kuo, Y.R., Chen, R.F., and Yang, K.D.: Superoxide mediates shock wave induction of ERK-dependent osteogenic transcription factor (CBFA1) and mesenchymal cell differentiation toward osteoprogenitors. J. Biol. Chem., 277, 10931-10937, 2002.
16. Mouche, S., Mkaddem, S.B., Wang, W., Katic, M., Tseng, Y.H., Carnesecchi, S., Steger, K., Foti, M., Meier, C.A., Muzzin, P., Kahn, C.R., Ogier-Denis, E., and Szanto, I.: Reduced expression of the NADPH oxidase NOX4 is a hallmark of adipocyte differentiation. Biochim. Biophys. Acta, 1773, 1015-1027, 2007.
17. Droge, W.: Free radicals in the physiological control of cell function. Physiol. Rev., 82, 47-95, 2002.
18. Linnane, A.W., Kios, M., and Vitetta, L.: Healthy aging: regulation of the metabolome by cellular redox modulation and prooxidant signaling systems: the essential roles of superoxide anion and hydrogen peroxide. Biogerontology, 8, 445-467, 2007. (Pubitemid 47365335)
19. Wang, Y., Zeigler, M.M., Lam, G.K., Hunter, M.G., Eubank, T.D., Khramtsov, V.V., Tridandapani, S., Sen, C.K., and Marsh, C.B.: The role of the NADPH oxidase complex, p38 MAPK, and Akt in regulating human monocyte/macrophage survival. Am. J. Respir. Cell Mol. Biol., 36, 68-77, 2007.
20. Wu, L. and de Champlain, J.: Effects of superoxide on signaling pathways in smooth muscle cells from rats. Hypertension, 34, 1247-1253, 1999. (Pubitemid 30002390)
21. Yin, D., Sun, H., Weaver, R.F., and Squier, T.C.: Non-essential role for methionines in the productive association between calmodulin and the plasma membrane Ca-ATPase. Biochemistry, 38, 13654-13660, 1999. (Pubitemid 129515691)
22. Yin, D., Kuczera, K., and Squier, T.C.: The sensitivity of carboxyl-terminal methionines in calmodulin isoforms to oxidation by H(2)O(2) modulates the ability to activate the plasma membrane Ca-ATPase. Chem. Res. Toxicol., 13, 103-110, 2000.
23. Sun, H., Gao, J., Ferrington, D.A., Biesiada, H., Williams, T.D., and Squier, T.C.: Repair of oxidized calmodulin by methionine sulfoxide reductase restores ability to activate the plasma membrane Ca-ATPase. Biochemistry, 38, 105-112, 1999. (Pubitemid 29035676)
24. Linnane, A.W., Kios, M., and Vitetta, L.: Coenzyme Q(10) - its role as a prooxidant in the formation of superoxide anion/ hydrogen peroxide and the regulation of the metabolome. Mitochondrion, 7 Suppl, S51-S61, 2007.
25. Clement, M.V., Hirpara, J.L., and Pervaiz, S.: Decrease in intracellular superoxide sensitizes Bcl-2-overexpressing tumor cells to receptor and drug-induced apoptosis independent of the mitochondria. Cell Death Differ., 10, 1273-1285, 2003.
26. Pervaiz, S. and Clement, M.V.: A permissive apoptotic environment: function of a decrease in intracellular superoxide anion and cytosolic acidification. Biochem. Biophys. Res., 290, 1145-1150, 2002.
27. Irani, K. and Goldschmidt-Clermont, P.J.: Ras, superoxide and signal transduction. Biochem. Pharmacol., 55, 1339-1346, 1998.
28. Pervaiz, S., Cao, J., Chao, O.S., Chin, Y.Y., and Clement, M.V.: Activation of the RacGTPase inhibits apoptosis in human tumor cells. Oncogene, 20, 6263-6268, 2001. (Pubitemid 32970414)
29. Brandes, R.P.: Role of NADPH oxidases in the control of vascular gene expression. Antioxid. Redox Signal., 5, 803-811, 2003.
30. Andrews, Z.B., Diano, S., and Horvath, T.L.: Mitochondrial uncoupling proteins in the CNS: in support of function and survival. Nat. Rev., 6, 829-840, 2005.
31. Hurtaud, C., Gelly, C., Chen, Z., Levi-Meyrueis, C., and Bouillaud, F.: Glutamine stimulates translation of uncoupling protein 2mRNA. Cell Mol. Life Sci., 64, 1853-1860, 2007.
32. Trenker, M., Malli, R., Fertschai, I., Levak-Frank, S., and Graier, W.F.: Uncoupling proteins 2 and 3 are fundamental for mitochondrial Ca2+ uniport. Nat. Cell Biol., 9, 445-452, 2007.
33. Chan, S.L., Liu, D., Kyriazis, G.A., Bagsiyao, P., Ouyang, X., and Mattson, M.P.: Mitochondrial uncoupling protein-4 regulates calcium homeostasis and sensitivity to store depletion-induced apoptosis in neural cells. J. Biol. Chem., 281, 37391-37403, 2006.
34. Wu, Z., Zhang, J., and Zhao, B.: Superoxide anion regulates the mitochondrial free Ca2+ through uncoupling proteins. Antioxid. Redox Signal., 11, 1805-1818, 2009.
35. Horvath, T.L., Warden, C.H., Hajos, M., Lombardi, A., Goglia, F., and Diano, S.: Brain uncoupling protein 2: uncoupled neuronal mitochondria predict thermal synapses in homeostatic centers. J. Neurosci., 19, 10417-10427, 1999. (Pubitemid 30228049)
36. Mattson, M.P.: Pathways towards and away from Alzheimer's disease. Nature, 430, 631-639, 2004. (Pubitemid 39061671)
37. Li, F., Calingasan, N.Y., Yu, F., Mauck, W.M., Toidze, M., Almeida, C.G., Takahashi, R.H., Carlson, G.A., Flint Beal, M., Lin, M.T., and Gouras, G.K.: Increased plaque burden in brains of APP mutant MnSOD heterozygous knockout mice. J. Neurochem., 89, 1308-1312, 2004. (Pubitemid 38715849)
38. Lovell, M.A., Xiong, S., Xie, C., Davies, P., and Markesbery, W.R.: Induction of hyperphosphorylated tau in primary rat cortical neuron cultures mediated by oxidative stress and glycogen synthase kinase-3. J. Alzheimers Dis., 6, 659-671, discussion 673-681, 2004.
39. Pastorino, L., Sun, A., Lu, P.J., Zhou, X.Z., Balastik, M., Finn, G., Wulf, G., Lim, J., Li, S.H., Li, X., Xia, W., Nicholson, L.K., and Lu, K.P.: The prolyl isomerase Pin1 regulates amyloid precursor protein processing and amyloidbeta production. Nature, 440, 528-534, 2006.
40. Liou, Y.C., Sun, A., Ryo, A., Zhou, X.Z., Yu, Z.X., Huang, H.K., Uchida, T., Bronson, R., Bing, G., Li, X., Hunter, T., and Lu, K.P.: Role of the prolyl isomerase Pin1 in protecting against age-dependent neurodegeneration. Nature, 424, 556-561, 2003. (Pubitemid 36975777)
41. de la Monte, S.M. and Wands, J.R.: Molecular indices of oxidative stress and mitochondrial dysfunction occur early and often progress with severity of Alzheimer's disease. J. Alzheimers Dis., 9, 167-181, 2006.
42. Anandatheerthavarada, H.K., Biswas, G., Robin, M.A., and Avadhani, N.G.: Mitochondrial targeting and a novel transmembrane arrest of Alzheimer's amyloid precursor protein impairs mitochondrial function in neuronal cells. J. Cell Biol., 161, 41-54, 2003. (Pubitemid 36459078)
43. Lustbader, J.W., Cirilli, M., Lin, C., Xu, H.W., Takuma, K., Wang, N., Caspersen, C., Chen, X., Pollak, S., Chaney, M., Trinchese, F., Liu, S., Gunn-Moore, F., Lue, L.F., Walker, D.G., Kuppusamy, P., Zewier, Z.L., Arancio, O., Stern, D., Yan, S.S., and Wu, H.: ABAD directly links Abeta to mitochondrial toxicity in Alzheimer's disease. Science, 304, 448-452, 2004. (Pubitemid 38495942)
44. Crouch, P.J., Blake, R., Duce, J.A., Ciccotosto, G.D., Li, Q.X., Barnham, K.J., Curtain, C.C., Cherny, R.A., Cappai, R., Dyrks, T., Masters, C.L., and Trounce, I.A.: Copper-dependent inhibition of human cytochrome c oxidase by a dimeric conformer of amyloid-beta1-42. J. Neurosci., 25, 672-679, 2005.
45. Casley, C.S., Canevari, L., Land, J.M., Clark, J.B., and Sharpe, M.A.: Beta-amyloid inhibits integrated mitochondrial respiration and key enzyme activities. J. Neurochem., 80, 91-100, 2002. (Pubitemid 34614581)
46. Park, H.J., Seong, Y.M., Choi, J.Y., Kang, S., and Rhim, H.: Alzheimer's disease-associated amyloid beta interacts with the human serine protease HtrA2/Omi. Neurosci. Lett., 357, 63-67, 2004.
47. Hansson, C.A., Frykman, S., Farmery, M.R., Tjernberg, L.O., Nilsberth, C., Pursglove, S.E., Ito, A., Winblad, B., Cowburn, R.F., Thyberg, J., and Ankarcrona, M.: Nicastrin, presenilin, APH-1, and PEN-2 form active gamma-secretase complexes in mitochondria. J. Biol. Chem., 279, 51654-51660, 2004.
48. Echtay, K.S., Roussel, D., St-Pierre, J., Jekabsons, M.B., Cadenas, S., Stuart, J.A., Harper, J.A., Roebuck, S.J., Morrison, A., Pickering, S., Clapham, J.C., and Brand, M.D.: Superoxide activates mitochondrial uncoupling proteins. Nature, 415, 96-99, 2002. (Pubitemid 34062457)
49. Echtay, K.S., Esteves, T.C., Pakay, J.L., Jekabsons, M.B., Lambert, A.J., Portero-Otin, M., Pamplona, R., Vidal-Puig, A.J., Wang, S., Roebuck, S.J., and Brand, M.D.: A signalling role for 4-hydroxy-2-nonenal in regulation of mitochondrial uncoupling. EMBO J., 22, 4103-4110, 2003. (Pubitemid 37021739)
50. Liu, D., Chan, S.L., de Souza-Pinto, N.C., Slevin, J.R., Wersto, R.P., Zhan, M., Mustafa, K., de Cabo, R., and Mattson, M.P.: Mitochondrial UCP4 mediates an adaptive shift in energy metabolism and increases the resistance of neurons to metabolic and oxidative stress. Neuromolecular Med., 8, 389-414, 2006. (Pubitemid 43918160)
51. Watson, G.S. and Craft, S.: The role of insulin resistance in the pathogenesis of Alzheimer's disease: implications for treatment. CNS Drugs, 17, 27-45, 2003. (Pubitemid 36044347)
52. Mattson, M.P. and Liu, D.: Mitochondrial potassium channels and uncoupling proteins in synaptic plasticity and neuronal cell death. Biochem. Biophys. Res. Commun., 304, 539-549, 2003.