<strong>Progress on the Involvement of GRP78 and ATF4 – CHOP – Puma Signaling Pathway in Endoplasmic Reticulum Stress and Parkinson's Disease</strong>

Abstract

Abstract:Endoplasmic reticulum is one of the important organelles in eukaryotic cells, and it is closely related to the cellular homeostasis state. Glucose shortage, hypoxia, calcium imbalance and oxidative stress all can lead to the accumulation of unfolded or misfolded proteins in the cells，which will lead to endoplasmic reticulum stress. Parkinson's disease is a chronic progressive neurodegenerative disease, with the typical pathological changes being the lack of the neurotransmitter dopamine resulting from the degeneration and loss of the dopaminergic nerve cells in the substantia nigra striatum. Current treatments of Parkinson's disease is to relieve the symptoms rather than prevent the progression of the disease. Recent research suggests that the selective death of dopaminergic neurons is associated with endoplasmic reticulum stress in the process of the Parkinson's disease. The central modulating factors of endoplasmic reticulum stress, i.e. glucose regulated protein 78 (GRP78) and the downstream ATF4 - CHOP - Puma signaling pathway, are closely linked to the progress of the Parkinson's disease. This review summarized recent developments of the GRP78 and its downstream ATF4 - CHOP - Puma signaling pathways, in the hope of providing information for the potential new targets in the treatment of Parkinson's disease.

Key words:endoplasmic reticulum stress（ERS）,signal transduction pathway,Parkinson's disease（PD）,glucose regulated protein 78 (GRP78),ATF4&,ndash,CHOP&,ndash,Puma

CLC Number:

R964

WANG Qi, DUAN Leng-xin.Progress on the Involvement of GRP78 and ATF4 – CHOP – Puma Signaling Pathway in Endoplasmic Reticulum Stress and Parkinson's Disease[J]. ACTA NEUROPHARMACOLOGICA, 2013, 3(3): 19-26.

References

[1] Do Yeon Lee, Kyu-Sun Lee, Hyun Jung Lee, et al. Activation of PERK signaling attenuates Abetamediated ER stress[J]. PLoS One, 2010, 5(5):10489.

[2] Xu Chun-yan, Beatrice Bailly-Maitre, John C Reed. Endoplasmic reticulum stress: cell life and death decisions[J]. J Clin Invest, 2005, 115(10):2656-2664.

[3] Peter J Belmont, Archana Tadimalla, Chen Wen-qiong, et al. Coordination of growth and endoplasmic reticulum stress signaling by regulator of calcineurin 1 (RCAN1), a novel ATF6-inducible gene[J]. J Biol Chem, 2008, 283(20):14012-14021.

[4] Peter Walter, David Ron. The unfolded protein response: from stress pathway to homeostatic regulation[J]. Science, 2011, 334(6059):1081-1086.

[5] Rammohan V Rao, Dale E Bredesen. Misfolded proteins, endoplasmic reticulum stress and neurodegeneration[J]. Curr Opin Cell Biol, 2004, 16(6):653-662.

[6] Tomohiro Omura, Masayuki Kaneko, Yasunobu Okuma, et al. Endoplasmic reticulum stress and Parkinson's disease: the role of HRD1 in averting apoptosis inneurodegenerative disease[J]. Oxid Med Cell Longev, 2013, 2013:239854.

[7] Claudio Hetz. The unfolded protein response: controlling cell fate decisions under ER stress and beyond[J]. Nature Reviews Molecular Cell Biology, 2012, 13(2):89-102.

[8] Zohreh Galehdar, Patrick Swan, Benjamin Fuerth, et al. Neuronal apoptosis induced by endoplasmic reticulum stress is regulated by ATF4-CHOP-mediated induction of the Bcl-2 homology 3-only member PUMA[J]. J Neurosci, 2010, 30(50):16938-16948.

[9] Wang Xiao-tian, Pei Dong-sheng, Xu Jing, et al. Opposing effects of bad phosphorylation at two distinctsites by Akt1 and JNK1/2 on ischemic brain injury[J]. Cell Signalling, 2007, 19(9):1844-1856．

[10] Weng Shao-xiang, Zhu Xiao-qing, Jin Yue, et al. Protective effect of erythropoietin on myocardial infarction in rats by inhibition of caspase-12 expression[J]. Exp Ther Med, 2011, 2(5):833-836.

[11] Chen Yi-hong, Wu Xu-dong, Yao Shu-tong, et al. Calcineurin is involved in cardioprotection induced by ischemic postconditioning through attenuating endoplasmic reticulum stress[J]. Chin Med J, 2011, 124(20):3334-3340.

[12] Rammohan V Rao, Ellerby H M, Dale E Bredesen. Coupling endoplasmic reticulum stress to the cell death program[J]. Cell Death Differ, 2004, 11(4):372-380.

[13] Liu Di, Zhang Meng-ren, Yin Hong-chao. Signaling pathways involved in endoplasmic reticulum stress-induced neuronal apoptosis[J]. Int J Neurosci, 2013, 123(3):155-162．

[14] Hyun-Jung Lee, Sung-Haeng Lee, Sung-Hee Park, et al. Purification of catalytically active caspase-12 and its biochemical characterization[J]. Arch Biochem Biophys, 2010, 502(1):68-73.

[15] Lesage S, Brice A. Parkinson’s disease: from monogenic forms to genetic susceptibility factors[J]. Hum Mol Genet, 2009, 18(1):48-59.

[16] Christian Wider, Tatiana Foroud, Zbigniew K Wszolek, et al. Clinical implications of gene discovery in Parkinson’s disease and parkinsonism[J]. Mov Disord, 2010, 25(1):15-20.

[17] Wataru Satake, Yuko Nakabayashi, Ikuko Mizuta, et al. Genome-wide association study identiies common variants at four loci as genetic risk factors for Parkinson’s disease[J]. Nature Genetics, 2009, 41(12):1303-1307.

[18] Javier Simon-Sanchez, Claudia Schulte, Jose M Bras, et al. Genome-wide association study reveals genetic risk underlying Parkinson’s disease[J]. Nat Genet, 2009, 41(12):1308-1312.

[19] Karen M Doyle, Donna Kennedy, Adrienne M Gorman, et al. Unfolded proteins and endoplasmic reticulum stress in neurodegenerative disorders[J]. J Cell Mol Med, 2011, 15(10):2025-2039.

[20] Joseph Jankovic, L Giselle Aguilar. Current approaches to the treatment of Parkinson's disease[J]. Neuropsychiatr Dis Treat, 2008, 4(4):743-757.

[21] Ghribi Othman, Herman Mary M, Pramoonjago Patcharin, et al. MPP+ induces the endoplasmic reticulum stress response in rabbit braininvolving activation of the ATF-6 and NF-JB signaling pathways[J]. J Neuropathol Exp Neurol, 2003, 2(11):1144-1153.

[22] Girardot Fabrice, Monnier Veronique, Tricoire Herve. Genome wide analysis of common and specific stress responses in adult drosophila melanogaster[J]. BMC Genomics, 2004, 5(1):74.

[23] Chen Gang, Kimberly A Bower, Cuiling Ma, et al. Glycogen synthase kinase 3beta (GSK3beta) mediates 6-hydroxydopamine-induced neuronal death[J]. FASEB J, 2004, 18(10):1162-1164.

[24] William A Holtz, Jay M Turetzky, Karen L O.Malley. Microarray expression profiling identifies early signaling transcripts associated with 6-OHDA-induced dopaminergic cell death[J]. Antioxid Redox Signal, 2005, 7(5-6):639-648

[25] Mohsen Kheradpezhouh, Shalk Shavali, Manuchair Ebadi. Salsolinol causing parkinsonism activates endoplasmic reticulum-stress signaling pathways in human dopaminergic SK-N-SH cells[J]. Neurosignals, 2003, 12(6):315-324.

[26] William A Holtz, Karen Laurel O.Malley. Parkinsonian mimetics induce aspects of unfolded protein response in death of dopaminergic neurons[J]. J Biol Chem, 2000, 278(21):19367-19377.

[27] Elizabeth J Ryu, Heather P Harding, James M Angelastro, et al. Endoplasmic reticulum stress and the unfolded protein response in cellular models of Parkinson,s disease[J]. J Neurosci, 2002, 22(24):10690-10698.

[28] Cristina Gomez-Santos, Marta Barrachina, Pol Gimenez-Xavier, et al. Induction of C /EBP beta and GADD153 expression by dopamine in human neuroblastoma cells relationship with alpha-synuclein increase and cell damage[J]. Brain Res Bull, 2005, 65(1):87-95.

[29] Hoozemans J J M, van Haastert E S, Eikelenboom P, et al. Activation of the unfolded protein response in Parkinson’s disease[J]. Biochem Biophys Res Commun, 2007, 354(3):707-711.

[30] Villar-Cheda B, Dominguez-Meijide A, Joglar B, et al. Involvement of microglial RhoA/Rho-kinase pathway activation in the dopaminergic neuron death role of angiotensin via angiotensin type 1 receptors[J]. Neurobiology Disease, 2012, 47(2):268-279.

[31] D Thomas Rutkowski, Ramanujan S Hegde. Regulation of basal cellular physiology by the homeostatic unfolded protein response[J]. J Cell Biol, 2010, 189(5):783-794.

[32] Nitza Goldenberg-Cohen, Annat Raiter, Vera Gaydar, et al. Peptide-binding GRP78 protects neurons from hypoxia-induced apoptosis[J]. Apoptosis, 2012, 17(3):278-288.

[33] Jiang Yu-feng, Lv Hai-long, Liao Min, et al. GRP78 counteracts cell death and protein aggregation caused by mutant huntingtin proteins[J]. Neuroscience Letters, 2012, 516(2):182-187.

[34] Oida Y, Kitaichi K, Nakayama H, et al. Rifampicin attenuates the MPTP-induced neurotoxicity in mouse brain[J]. Brain Res, 2006, 1082(1):196-204.

[35] Ulkan Kilic, Ertugrul Kilic, Paul Lingor, et al. Rifampicin inhibits neurodegeneration in the optic nerve transection model in vivo and after 1-methyl-4-phenylpyridinium intoxication in vitro[J]. Acta Neuropathol, 2004, 108(1):65-68.

[36] Marina S Gorbatyuk, Arseniy Shabashvili, Chen Wei-jun, et al. Glucose regulated protein 78 diminishes α-synuclein neurotoxicity in a rat model of Parkinson disease[J]. Mol Ther, 2012, 20(7):1327-1337.

[37] Sun Yuan-lin, Zhang Guo-hua, Xu Jie, et al. Effect of rifampicin pre- and post-treatment on rotenone-induced dopaminergic neuronal apoptosis and alpha-synuclein expression[J]. Neural Regenera Res, 2010, 5(2):85-91.

[38] Jing Xiuna, Shi Qiao-yun, Bi Wei, et al. Rifampicin protects PC12 cells from rotenone-induced cytotoxicity by activating GRP78 via PERK-eIF2a-ATF4 pathway[J]. PLoS One, 2014, 9(3):92110.

[39] Chen Yuan-yuan, Chen Gang, Fan Zhi-qin, et al. GSK3beta and endoplasmic reticulum-stress mediate rotenone-induced death of SK-N-MC neuroblastoma cells[J]. Biochem Pharmacol, 2008, 76(1):128-138.

[40] Arindam P Ghosh, Barbara J Klocke, Mary E Ballestas, et al. CHOP potentially co-operates with FOXO3a in neuronal cells to regulate PUMA and BIM expression in response to ER stress[J]. PLoS One, 2012, 7(6):39586.

[41] Jose L Labandeira-Garcia, Jannette Rodriguez-Pallares, B Villar-Cheda, et al. Guerra, aging, angiotensin system and dopaminergic degeneration in the substantia nigra[J]. Aging Dis, 2011, 2(3):257–274.

[42] Rodriguez-Pallares J, Rey P, Parga J A, et al. Brain angiotensin enhances dopaminergic cell death via microglial activation and NADPH-derived ROS[J]. Neurobiol Dis, 2008, 31(1):58-73.

[43] Tom N Grammatopoulos, Susan M Jones, Ferogh A Ahmadi, et al. Angiotensin type 1 receptor antagonist losartan, reduces MPTP-induced degeneration of dopaminergic neurons in substantia nigra[J]. Mol Neurodegener, 2007, 2:1.

[44] Liang Wu, Tian You-yong, Shi Jing-ping, et al. Inhibition of endoplasmic reticulum stress is involved in the neuroprotective effects of candesartan cilexitil in the rotenone rat model of Parkinson’s disease [J]. Neurosci Lett, 2013, 548:50–55.

Progress on the Involvement of GRP78 and ATF4 – CHOP – Puma Signaling Pathway in Endoplasmic Reticulum Stress and Parkinson's Disease

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