Regulation of endoplasmic reticulum stress in rat cortex by p62/ZIP through the Keap1-Nrf2-ARE signalling pathway after transient focal cerebral ischaemia

References

• Margaill I, Plotkine M, Lerouet D. Antioxidant strategies in the treatment of stroke. Free Radical Biology and Medicine 2005;39:429–443
   PubMed Web of Science ®Google Scholar
• Saleem S, Ahmad M, Ahmad AS, Yousuf S, Ansari MA, Khan MB, Ishrat T, Islam F. Behavioral and histologic neuroprotection of aqueous garlic extract after reversible focal cerebral ischemia. Journal of Medicinal Food 2006;9:537–544
   PubMed Web of Science ®Google Scholar
• Mirzaei H, Regnier F. Protein: protein aggregation induced by protein oxidation. Analytical Technologies in the Biomedical and Life Sciences 2008;873:8–14
   PubMed Web of Science ®Google Scholar
• Liu C, Gao Y, Barrett J, Hu B. Autophagy and protein aggregation after brain ischemia. Journal of Neurochemistry 2010;115:68–78
   PubMed Web of Science ®Google Scholar
• Carloni S, Buonocore G, Balduini W. Protective role of autophagy in neonatal hypoxia-ischemia induced brain injury. Neurobiology of Disease 2008;32:329–339
   PubMed Web of Science ®Google Scholar
• Balduini W, Carloni S, Buonocore G. Autophagy in hypoxia-ischemia induced brain injury: evidence and speculations. Autophagy 2009;5:221–223
   PubMed Web of Science ®Google Scholar
• Puyal J, Clarke PG. Targeting autophagy to prevent neonatal stroke damage. Autophagy 2009;5:1060–1061
   PubMed Web of Science ®Google Scholar
• Puyal J, Vaslin A, Mottier V, Clarke PGH. Postischemic treatment of neonatal cerebral ischemia should target autophagy. Annals of Neurology 2009;66:378–389
   PubMed Web of Science ®Google Scholar
• Zheng Y-Q, Liu J-X, Li X-Z, Xu L, Xu, Y-G. RNA interference-mediated downregulation of Beclin1 attenuates cerebral ischemic injury in rats. Acta Pharmacologica Sinica 2009;30:919–927
   PubMedGoogle Scholar
• Rami A, Langhagen A, Steiger S. Focal cerebral ischemia induces upregulation of Beclin 1 and autophagy-like cell death. Neurobiology of Disease 2008;29:132–141
   PubMed Web of Science ®Google Scholar
• Kobayashi M, Yamamoto M. Nrf2-Keap1 regulation of cellular defense mechanisms against electrophiles and reactive oxygen species. Advances in Enzyme Regulation 2006;46:113–140
   PubMedGoogle Scholar
• Kobayashi A, Kang MI, Okawa H, Ohtsuji M, Zenke Y, Chiba T, Igarashi K, Yamamoto M. Oxidative stress sensor Keap1 functions as an adaptor for Cul3-based E3 ligase to regulate for proteasomal degradation of Nrf2. Molecular and Cellular Biology 2004;24:7130–7139
   PubMed Web of Science ®Google Scholar
• Motohashi H, Yamamoto M. Nrf2-Keap1 defines a physiologically important stress response mechanism. Trends in Molecular Medicine 2004;10:549–557
   PubMed Web of Science ®Google Scholar
• Jaiswal AK. Nrf2 signaling in coordinated activation of antioxidant gene expression. Free Radical Biology and Medicine 2004;36:1199–1207
   PubMed Web of Science ®Google Scholar
• Holtzclaw WD, Dinkova-Kostova AT, Talalay P. Protection against electrophile and oxidative stress by induction of phase 2 genes: the quest for the elusive sensor that responds to inducers. Advances in Enzyme Regulation 2004;44:335–367
   PubMedGoogle Scholar
• Ding W-X, Yin X-M. Sorting, recognition and activation of the misfolded protein degradation pathways through macroautophagy and the proteasome. Autophagy 2008;4:141–150
   PubMed Web of Science ®Google Scholar
• Bjorkoy G, Lamark T, Brech A, Outzen H, Perander M, Overvatn A, Stenmark H, Johansen T. p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death. Journal of Cell Biology 2005;171:603–614
   PubMed Web of Science ®Google Scholar
• Knaevelsrud H, Simonsen A. Fighting disease by selective autophagy of aggregate-prone proteins. FEBS Letters 2010;584:2635–2645
   PubMed Web of Science ®Google Scholar
• Moscat J, Diaz-Meco MT. p62 at the crossroads of autophagy, apoptosis, and cancer. Cell 2009;137:1001–1004
   PubMed Web of Science ®Google Scholar
• Mathew R, Karp CM, Beaudoin B, Vuong N, Chen G, Chen H-Y, Bray K, Reddy A, Bhanot G, Gelinas C, DiPaola RS, Karantza-Wadsworth V, White E. Autophagy suppresses tumorigenesis through elimination of p62. Cell 2009;137:1062–1075
   PubMed Web of Science ®Google Scholar
• Jain A, Lamark T, Sjottem E, Larsen KB, Awuh JA, Overvatn A, McMahon M, Hayes JD, Johansen T. p62/SQSTM1 Is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription. Journal of Biological Chemistry 2010;285:22576–22591
   PubMed Web of Science ®Google Scholar
• Komatsu M, Kurokawa H, Waguri S, Taguchi K, Kobayashi A, Ichimura Y, Sou Y-S, Ueno I, Sakamoto A, Tong KI, et al. The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1. Nature Cell Biology 2010;12:213–217
   PubMed Web of Science ®Google Scholar
• Lau A, Wang X-J, Zhao F, Villeneuve NF, Wu T, Jiang T, Sun Z, White E, Zhang DD. A noncanonical mechanism of Nrf2 activation by autophagy deficiency: Direct interaction between Keap1 and p62. Molecular and Cellular Biology 2010;30:3275–3285
   PubMed Web of Science ®Google Scholar
• Sheng R, Zhang L-S, Han R, Liu X-Q, Gao B, Qin Z-H. Autophagy activation is associated with neuroprotection in a rat model of focal cerebral ischemic preconditioning. Autophagy 2010;6:482–494
   PubMed Web of Science ®Google Scholar
• Nagasawa H, Kogure K. Correlation between cerebral blood flow and histologic changes in a new rat model of middle cerebral artery occlusion. Stroke 1989;20:1037–1043
   PubMed Web of Science ®Google Scholar
• Lourbopoulos A, Karacostas D, Artemis N, Milonas I, Grigoriadis N. Effectiveness of a new modified intraluminal suture for temporary middle cerebral artery occlusion in rats of various weight. Journal of Neuroscience Methods 2008;173:225–234
   PubMedGoogle Scholar
• Longa EZ, Weinstein PR, Carlson S, Cummins R. Reversible middle cerebral artery occlusion without craniectomy in rats. Stroke 1989;20:84–91
   PubMed Web of Science ®Google Scholar
• Swanson RA, Morton MT, Tsao-Wu G, Savalos RA, Davidson C, Sharp FR. A semiautomated method for measuring brain infarct volume. Journal of Cerebral Blood Flow and Metabolism 1990;10:290–293
   PubMed Web of Science ®Google Scholar
• Tatlisumak T, Takano K, Carano RA, Miller LP, Foster AC, Fisher M. Delayed treatment with an adenosine kinase inhibitor, GP683, attenuates infarct size in rats with temporary middle cerebral artery occlusion. Stroke 1998;29:1952–1958
   PubMed Web of Science ®Google Scholar
• Tatlisumak T, Carano RA, Takano K, Meiler MR, Li F, Sotak CH, Arndts D, Pschorn U, Fisher M. Broad-spectrum cation channel inhibition by LOE 908 MS reduces infarct volume in vivo and postmortem in focal cerebral ischemia in the rat. Journal of the Neurological Sciences 2000;178:107–113
   PubMedGoogle Scholar
• Neese SL, Sherill LK, Tan AA, Roosevelt RW, Browning RA, Smith DC, Duke A, Clough RW. Vagus nerve stimulation may protect GABAergic neurons following traumatic brain injury in rats: an immunocytochemical study. Brain Research 2007;1128:157–163
   PubMed Web of Science ®Google Scholar
• Mehta SL, Manhas N, Raghubir R. Molecular targets in cerebral ischemia for developing novel therapeutics. Brain Research Reviews 2007;54:34–66
   PubMed Web of Science ®Google Scholar
• Nakka VP, Gusain A, Mehta SL, Raghubir R. Molecular mechanisms of apoptosis in cerebral ischemia: Multiple neuroprotective opportunities. Molecular Neurobiology 2008;37:7–38
   PubMed Web of Science ®Google Scholar
• Jin X, Liu J, Yang Y, Liu KJ, Liu W. Spatiotemporal evolution of blood brain barrier damage and tissue infarction within the first 3h after ischemia onset. Neurobiology of Disease 2012;48:309–316
   PubMedGoogle Scholar
• Rogers DC, Campbell CA, Stretton JL, Mackay KB. Correlation between motor impairment and infarct volume after permanent and transient middle cerebral artery occlusion in the rat. Stroke 1997;28:2060–2066
   PubMed Web of Science ®Google Scholar
• Hayashi T, Saito A, Okuno S, Ferrand-Duke M, Dodd RL, Chan PH. Damage to the endoplasmic reticulum and activation of apoptotic machinery by oxidative stress in ischemic neurons. Journal of Cerebral Blood Flow and Metabolism 2005;25:41–53
   PubMed Web of Science ®Google Scholar
• Hayashi T, Saito A, Okuno S, Ferrand-Drake M, Dodd RL, Chan PH. Oxidative injury to the endoplasmic reticulum in mouse brains after transient focal ischemia. Neurobiology of Diseasenm 2004;15:229–239
   PubMed Web of Science ®Google Scholar
• Jayanthi S, Deng XL, Noailles PAH, Ladenheim B, Cadet JL. Methamphetamine induces neuronal apoptosis via cross-talks between endoplasmic reticulum and mitochondria-dependent death cascades. FASEB Journal 2004;18:238–251
   PubMed Web of Science ®Google Scholar
• Nakka VP, Gusain A, Raghubir R. Endoplasmic reticulum stress plays critical role in brain damage after cerebral ischemia/reperfusion in rats. Neurotoxicity Research 2010;17:189–202
   PubMed Web of Science ®Google Scholar
• Keller JN, Kindy MS, Holtsberg FW, St Clair DK, Yen HC, Germeyer A, Steiner SM, Bruce-Keller AJ, Hutchins JB, Mattson MP. Mitochondrial manganese superoxide dismutase prevents neural apoptosis and reduces ischemic brain injury: suppression of peroxynitrite production, lipid peroxidation, and mitochondrial dysfunction. Journal of Neuroscience 1998;18:687–697
   PubMed Web of Science ®Google Scholar
• Murakami K, Kondo T, Kawase M, Li Y, Sato S, Chen SF, Chan PH. Mitochondrial susceptibility to oxidative stress exacerbates cerebral infarction that follows permanent focal cerebral ischemia in mutant mice with manganese superoxide dismutase deficiency. The Journal of Neuroscience 1998;18:205–213
   PubMed Web of Science ®Google Scholar
• Aoki M, Tamatani M, Taniguchi M, Yamaguchi A, Bando Y, Kasai K, Miyoshi Y, Nakamura Y, Vitek MP, Tohyama M, et al. Hypothermic treatment restores glucose regulated protein 78 (GRP78) expression in ischemic brain. Brain research. Molecular Brain Research 2001;95:117–128
   PubMedGoogle Scholar
• Shibata M, Hattori H, Sasaki T, Gotoh J, Hamada J, Fukuuchi Y. Activation of caspase-12 by endoplasmic reticulum stress induced by transient middle cerebral artery occlusion in mice. Neuroscience 2003;118:491–499
   PubMed Web of Science ®Google Scholar
• Lee AS. The glucose-regulated proteins: stress induction and clinical applications. Trends in Biochemical Sciences 2001;26:504–510
   PubMed Web of Science ®Google Scholar
• Liu H, Bowes RC 3rd, van de Water B, Sillence C, Nagelkerke JF, Stevens JL. Endoplasmic reticulum chaperones GRP78 and calreticulin prevent oxidative stress, Ca2 + disturbances, and cell death in renal epithelial cells. Journal of Biological Chemistry 1997;272:21751–21759
   PubMed Web of Science ®Google Scholar
• Eymin B, Dubrez L, Allouche M, Solary E. Increased gadd153 messenger RNA level is associated with apoptosis in human leukemic cells treated with etoposide. Cancer Research 1997;57:686–695
   PubMedGoogle Scholar
• Hu BR, Janelidze S, Ginsberg MD, Busto R, Perez-Pinzon M, Sick TJ, Siesjo BK, Liu CL. Protein aggregation after focal brain ischemia and reperfusion. Journal of Cerebral Blood Flow and Metabolism 2001;21:865–875
   PubMed Web of Science ®Google Scholar
• Seki T, Takahashi H, Adachi N, Abe N, Shimahara T, Saito N, Sakai N. Aggregate formation of mutant protein kinase C gamma found in spinocerebellar ataxia type 14 impairs ubiquitin-proteasome system and induces endoplasmic reticulum stress. European Journal of Neuroscience 2007;26:3126–3140
   PubMedGoogle Scholar
• Uchio N, Oma Y, Toriumi K, Sasagawa N, Tanida I, Fujita E, Kouroku Y, Kuroda R, Momoi T, Ishiura S. Endoplasmic reticulum stress caused by aggregate-prone proteins containing homopolymeric amino acids. The FEBS Journal 2007;274:5619–5627
   PubMedGoogle Scholar
• Huang CJ, Haataja L, Gurlo T, Butler AE, Wu X, Soeller WC, Butler PC. Induction of endoplasmic reticulum stress-induced beta-cell apoptosis and accumulation of polyubiquitinated proteins by human islet amyloid polypeptide. American Journal of Physiology. Endocrinology And Metabolism 2007;293:E1656–1662
   PubMed Web of Science ®Google Scholar
• Hanada T, Ohsumi Y. Structure-function relationship of Atg12, a ubiquitin-like modifier essential for autophagy. Autophagy 2005;1:110–118
   PubMed Web of Science ®Google Scholar
• Geng J, Klionsky DJ. The Atg8 and Atg12 ubiquitin-like conjugation systems in macroautophagy. Embo Reports 2008;9:859–864
   PubMed Web of Science ®Google Scholar
• Liverman CS, Cui L, Yong C, Choudhuri R, Klein RM, Welch KM, Berman NE. Response of the brain to oligemia: gene expression, c-Fos, and Nrf2 localization. Brain Research. Molecular Brain Research 2004;126:57–66
   PubMedGoogle Scholar
• Shih AY, Li P, Murphy TH. A small-molecule-inducible Nrf2-mediated antioxidant response provides effective prophylaxis against cerebral ischemia in vivo. Journal of Neuroscience 2005;25:10321–10335
   PubMed Web of Science ®Google Scholar
• Innamorato NG, Rojo AI, Garcia-Yaguee AJ, Yamamoto M, de Ceballos ML, Cuadrado A. The transcription factor Nrf2 is a therapeutic target against brain inflammation. Journal of Immunology 2008;181:680–689
   PubMed Web of Science ®Google Scholar
• Zhao J, Kobori N, Aronowski J, Dash PK. Sulforaphane reduces infarct volume following focal cerebral ischemia in rodents. Neuroscience Letters 2006;393:108–112
   PubMed Web of Science ®Google Scholar
• Ping Z, Liu W, Kang Z, Cai J, Wang Q, Cheng N, Wang S, Wang S, Zhang JH, Sun X. Sulforaphane protects brains against hypoxic-ischemic injury through induction of Nrf2-dependent phase 2 enzyme. Brain Research 2010;1343:178–185
   PubMed Web of Science ®Google Scholar
• Yang C, Zhang X, Fan H, Liu Y. Curcumin upregulates transcription factor Nrf2, HO-1 expression and protects rat brains against focal ischemia. Brain Research 2009;1282:133–141
   PubMed Web of Science ®Google Scholar
• Ichimura Y, Komatsu M. Selective degradation of p62 by autophagy. Seminars in Immunopathology 2010;32:431–436
   PubMed Web of Science ®Google Scholar
• Kirkin V, McEwan DG, Novak I, Dikic I. A role for ubiquitin in selective autophagy. Molecular Cell 2009;34:259–269
   PubMed Web of Science ®Google Scholar