SIRT1-mediated deacetylation of PGC1α attributes to the protection of curcumin against glutamate excitotoxicity in cortical neurons

Biochemical and Biophysical Research Communications

Volumn 478, Issue 3, 2016, Pages 1376-1381

  Jia, Ning ^a   Sun, Qinru ^a   Su, Qian ^b   Chen, Guomin ^a  

^a MEDICAL SCHOOL OF XI AN JIAOTONG UNIVERSITY   (China)

^b XI'AN JIAOTONG UNIVERSITY   (China)

Author keywords

Cultured neuron; Curcumin; Glutamate excitotoxicity; PGC1 ; SIRT1

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM; CURCUMIN; CYTOCHROME C OXIDASE; GLUTAMIC ACID; PEROXISOME PROLIFERATOR ACTIVATED RECEPTOR GAMMA COACTIVATOR 1ALPHA; REACTIVE OXYGEN METABOLITE; SIRTUIN 1; BENZAMIDE DERIVATIVE; NAPHTHOL DERIVATIVE; NEUROPROTECTIVE AGENT; NEUROTOXIN; PPARGC1A PROTEIN, RAT; SIRTINOL;

ANIMAL CELL; APOPTOSIS; ARTICLE; BRAIN CELL; CALCIUM CELL LEVEL; CELL VIABILITY; CONTROLLED STUDY; DEACETYLATION; DRUG MECHANISM; EXCITOTOXICITY; MITOCHONDRIAL MEMBRANE POTENTIAL; MTT ASSAY; NERVE CELL NECROSIS; NEUROPROTECTION; NONHUMAN; PRIORITY JOURNAL; PROTEIN ACETYLATION; PROTEIN EXPRESSION; RAT; TUNEL ASSAY; ACETYLATION; ANIMAL; BRAIN CORTEX; CELL CULTURE; CELL DEATH; DRUG EFFECTS; INTRACELLULAR SPACE; METABOLISM; MITOCHONDRION; NERVE CELL; PATHOLOGY; SPRAGUE DAWLEY RAT;

ACETYLATION; ADENOSINE TRIPHOSPHATE; ANIMALS; BENZAMIDES; CALCIUM; CELL DEATH; CELLS, CULTURED; CEREBRAL CORTEX; CURCUMIN; ELECTRON TRANSPORT COMPLEX IV; GLUTAMIC ACID; INTRACELLULAR SPACE; MEMBRANE POTENTIAL, MITOCHONDRIAL; MITOCHONDRIA; NAPHTHOLS; NEURONS; NEUROPROTECTION; NEUROPROTECTIVE AGENTS; NEUROTOXINS; PEROXISOME PROLIFERATOR-ACTIVATED RECEPTOR GAMMA COACTIVATOR 1-ALPHA; RATS, SPRAGUE-DAWLEY; REACTIVE OXYGEN SPECIES; SIRTUIN 1;

EID: 84994048785     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2016.08.132     Document Type: Article

References (31)

1. [1] Pita-Almenar, J.D., Collado, M.S., Colbert, C.M., Eskin, A., Different mechanisms exist for the plasticity of glutamate reuptake during early long-term potentiation (LTP) and late LTP. J. Neurosci. 26 (2006), 10461–10471.
2. [2] Chen, Q.Y., Alarcon, S., Tharp, A., Ahmed, O.M., Estrella, N.L., Greene, T.A., Rucker, J., Breslin, P.A., Perceptual variation in umami taste and polymorphisms in TAS1R taste receptor genes. Am. J. Clin. Nutr. 90 (2009), 770S–779S.
3. [3] Dirnagl, U., Iadecola, C., Moskowitz, M.A., Pathobiology of ischaemic stroke: an integrated view. Trends Neurosci. 22 (1999), 391–397.
4. [4] Lee, S.M., Wong, M.D., Samii, A., Hovda, D.A., Evidence for energy failure following irreversible traumatic brain injury. Ann. N. Y. Acad. Sci. 893 (1999), 337–340.
5. [5] Dong, X.X., Wang, Y., Qin, Z.H., Molecular mechanisms of excitotoxicity and their relevance to pathogenesis of neurodegenerative diseases. Acta Pharmacol. Sin. 30 (2009), 379–387.
6. [6] Jankovic, J., Parkinson's disease: clinical features and diagnosis. J. Neurol. Neurosurg. Psychiatry 79 (2008), 368–376.
7. [7] Olney, J.W., Ho, O.L., Rhee, V., DeGubareff, T., Letter: neurotoxic effects of glutamate. N. Engl. J. Med. 289 (1973), 1374–1375.
8. [8] Reynolds, I.J., Hastings, T.G., Glutamate induces the production of reactive oxygen species in cultured forebrain neurons following NMDA receptor activation. J. Neurosci. 15 (1995), 3318–3327.
9. [9] Abramov, A.Y., Duchen, M.R., Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity. Biochim. Biophys. Acta 1777 (2008), 953–964.
10. [10] Jia, N., Yang, K., Sun, Q., Cai, Q., Li, H., Cheng, D., Fan, X., Zhu, Z., Prenatal stress causes dendritic atrophy of pyramidal neurons in hippocampal CA3 region by glutamate in offspring rats. Dev. Neurobiol. 70 (2010), 114–125.
11. [11] Li, H., Li, X., Jia, N., Cai, Q., Bai, Z., Chen, R., Song, T., Zhu, Z., Liu, J., NF-kappaB regulates prenatal stress-induced cognitive impairment in offspring rats. Behav. Neurosci. 122 (2008), 331–339.
12. [12] Zhang, X.H., Jia, N., Zhao, X.Y., Tang, G.K., Guan, L.X., Wang, D., Sun, H.L., Li, H., Zhu, Z.L., Involvement of pGluR1, EAAT2 and EAAT3 in offspring depression induced by prenatal stress. Neuroscience 250 (2013), 333–341.
13. [13] Jia, N., Li, Q., Sun, H., Song, Q., Tang, G., Sun, Q., Wang, W., Chen, R., Li, H., Zhu, Z., Alterations of group I mGluRs and BDNF associated with behavioral abnormity in prenatally stressed offspring rats. Neurochem. Res. 40 (2015), 1074–1082.
14. [14] Michaels, R.L., Rothman, S.M., Glutamate neurotoxicity in vitro: antagonist pharmacology and intracellular calcium concentrations. J. Neurosci. 10 (1990), 283–292.
15. [15] Reisberg, B., Doody, R., Stoffler, A., Schmitt, F., Ferris, S., Mobius, H.J., Memantine Study, G., Memantine in moderate-to-severe Alzheimer's disease. N. Engl. J. Med. 348 (2003), 1333–1341.
16. [16] Sulkowski, G., Dabrowska-Bouta, B., Salinska, E., Struzynska, L., Modulation of glutamate transport and receptor binding by glutamate receptor antagonists in EAE rat brain. PLoS One, 9, 2014, e113954.
17. [17] Krystal, J.H., Karper, L.P., Seibyl, J.P., Freeman, G.K., Delaney, R., Bremner, J.D., Heninger, G.R., Bowers, M.B. Jr., Charney, D.S., Subanesthetic effects of the noncompetitive NMDA antagonist, ketamine, in humans. Psychotomimetic, perceptual, cognitive, and neuroendocrine responses. Arch. Gen. Psychiatry 51 (1994), 199–214.
18. [18] Iadarola, N.D., Niciu, M.J., Richards, E.M., Vande Voort, J.L., Ballard, E.D., Lundin, N.B., Nugent, A.C., Machado-Vieira, R., Zarate, C.A. Jr., Ketamine and other N-methyl-D-aspartate receptor antagonists in the treatment of depression: a perspective review. Ther. Adv. Chronic Dis. 6 (2015), 97–114.
19. [19] Kim, H.U., Sohn, S.B., Lee, S.Y., Metabolic network modeling and simulation for drug targeting and discovery. Biotechnol. J. 7 (2012), 330–342.
20. [20] Sun, Q., Jia, N., Wang, W., Jin, H., Xu, J., Hu, H., Activation of SIRT1 by curcumin blocks the neurotoxicity of amyloid-beta25-35 in rat cortical neurons. Biochem. Biophys. Res. Commun. 448 (2014), 89–94.
21. [21] Darvesh, A.S., Carroll, R.T., Bishayee, A., Novotny, N.A., Geldenhuys, W.J., Van der Schyf, C.J., Curcumin and neurodegenerative diseases: a perspective. Expert Opin. Investig. Drugs 21 (2012), 1123–1140.
22. [22] Jiang, H., Wang, Z., Wang, Y., Xie, K., Zhang, Q., Luan, Q., Chen, W., Liu, D., Antidepressant-like effects of curcumin in chronic mild stress of rats: involvement of its anti-inflammatory action. Prog. Neuropsychopharmacol. Biol. Psychiatry 47 (2013), 33–39.
23. [23] Chen, K., An, Y., Tie, L., Pan, Y., Li, X., Curcumin protects neurons from glutamate-induced excitotoxicity by membrane anchored AKAP79-PKA interaction network. Evid. Based Complement. Altern. Med., 2015, 2015, 706207.
24. [24] Liu, W., Fan, Z., Han, Y., Lu, S., Zhang, D., Bai, X., Xu, W., Li, J., Wang, H., Curcumin attenuates peroxynitrite-induced neurotoxicity in spiral ganglion neurons. Neurotoxicology 32 (2011), 150–157.
25. [25] Zhao, L., An, R., Yang, Y., Yang, X., Liu, H., Yue, L., Li, X., Lin, Y., Reiter, R.J., Qu, Y., Melatonin alleviates brain injury in mice subjected to cecal ligation and puncture via attenuating inflammation, apoptosis, and oxidative stress: the role of SIRT1 signaling. J. Pineal Res. 59 (2015), 230–239.
26. [26] Scarpulla, R.C., Metabolic control of mitochondrial biogenesis through the PGC-1 family regulatory network. Biochim. Biophys. Acta 1813 (2011), 1269–1278.
27. [27] Lin, J., Handschin, C., Spiegelman, B.M., Metabolic control through the PGC-1 family of transcription coactivators. Cell Metab. 1 (2005), 361–370.
28. [28] Paoletti, P., Molecular basis of NMDA receptor functional diversity. Eur. J. Neurosci. 33 (2011), 1351–1365.
29. [29] Vergun, O., Keelan, J., Khodorov, B.I., Duchen, M.R., Glutamate-induced mitochondrial depolarisation and perturbation of calcium homeostasis in cultured rat hippocampal neurones. J. Physiol. 519:Pt 2 (1999), 451–466.
30. [30] Sena, L.A., Chandel, N.S., Physiological roles of mitochondrial reactive oxygen species. Mol. Cell 48 (2012), 158–167.
31. [31] Rodgers, J.T., Lerin, C., Haas, W., Gygi, S.P., Spiegelman, B.M., Puigserver, P., Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1. Nature 434 (2005), 113–118.