Neuroprotective Effects of Protein Tyrosine Phosphatase 1B Inhibition against ER Stress-Induced Toxicity |
Jeon, Yu-Mi
(Department of Neural Development and Disease, Korea Brain Research Institute (KBRI))
Lee, Shinrye (Department of Neural Development and Disease, Korea Brain Research Institute (KBRI)) Kim, Seyeon (Department of Neural Development and Disease, Korea Brain Research Institute (KBRI)) Kwon, Younghwi (Department of Neural Development and Disease, Korea Brain Research Institute (KBRI)) Kim, Kiyoung (Department of Medical Biotechnology, Soonchunhyang University) Chung, Chang Geon (Department of Brain & Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST)) Lee, Seongsoo (Gwangju Center, Korea Basic Science Institute (KBSI)) Lee, Sung Bae (Department of Brain & Cognitive Sciences, Daegu Gyeongbuk Institute of Science and Technology (DGIST)) Kim, Hyung-Jun (Department of Neural Development and Disease, Korea Brain Research Institute (KBRI)) |
1 | Panzhinskiy, E., Hua, Y., Culver, B., Ren, J., and Nair, S. (2013b). Endoplasmic reticulum stress upregulates protein tyrosine phosphatase 1B and impairs glucose uptake in cultured myotubes. Diabetologia 56, 598-607. DOI |
2 | Pickering, A.M., Linder, R.A., Zhang, H., Forman, H.J., and Davies, K.J. (2012). Nrf2-dependent induction of proteasome and regulator are required for adaptation to oxidative stress. J. Biol. Chem. 287, 10021-10031. DOI |
3 | Popov, D. (2012). Endoplasmic reticulum stress and the on site function of resident PTP1B. Biochem. Biophys. Res. Commun. 422, 535-538. DOI |
4 | Prada, P.O., Quaresma, P.G., Caricilli, A.M., Santos, A.C., Guadagnini, D., Morari, J., Weissmann, L., Ropelle, E.R., Carvalheira, J.B., Velloso, L.A., et al. (2013). Tub has a key role in insulin and leptin signaling and action in vivo in hypothalamic nuclei. Diabetes 62, 137-148. DOI |
5 | Qiu, B., Hu, S., Liu, L., Chen, M., Wang, L., Zeng, X., and Zhu, S. (2013). CART attenuates endoplasmic reticulum stress response induced by cerebral ischemia and reperfusion through upregulating BDNF synthesis and secretion. Biochem. Biophys. Res. Commun. 436, 655-659. DOI |
6 | Radford, H., Moreno, J.A., Verity, N., Halliday, M., and Mallucci, G.R. (2015). PERK inhibition prevents tau-mediated neurodegeneration in a mouse model of frontotemporal dementia. Acta Neuropathol. 130, 633-642. DOI |
7 | Seoposengwe, K., van Tonder, J.J., and Steenkamp, V. (2013). In vitro neuroprotective potential of four medicinal plants against rotenone-induced toxicity in SH-SY5Y neuroblastoma cells. BMC Complement. Altern. Med. 13, 353. DOI |
8 | Shimoke, K., Utsumi, T., Kishi, S., Nishimura, M., Sasaya, H., Kudo, M., and Ikeuchi, T. (2004). Prevention of endoplasmic reticulum stress-induced cell death by brain-derived neurotrophic factor in cultured cerebral cortical neurons. Brain Res. 1028, 105-111. DOI |
9 | Bettaieb, A., Matsuo, K., Matsuo, I., Wang, S., Melhem, R., Koromilas, A.E., and Haj, F.G. (2012). Protein tyrosine phosphatase 1B deficiency potentiates signaling in brown adipocytes. PLoS One 7, e32212. DOI |
10 | Araki, W., Yuasa, K., Takeda, S., Shirotani, K., Takahashi, K., and Tabira, T. (2000). Overexpression of presenilin-2 enhances apoptotic death of cultured cortical neurons. Ann. N. Y. Acad. Sci. 920, 241-244. |
11 | Chen, G., Fan, Z., Wang, X., Ma, C., Bower, K.A., Shi, X., Ke, Z.J., and Luo, J. (2007). Brain-derived neurotrophic factor suppresses tunicamycin-induced upregulation of CHOP in neurons. J. Neurosci. Res. 85, 1674-1684. DOI |
12 | Chen, Y.Y., Chen, G., Fan, Z., Luo, J., and Ke, Z.J. (2008). GSK3beta and endoplasmic reticulum stress mediate rotenone-induced death of SK-N-MC neuroblastoma cells. Biochem. Pharmacol. 76, 128-138. DOI |
13 | Su, Q., Wang, S., Gao, H.Q., Kazemi, S., Harding, H.P., Ron, D., and Koromilas, A.E. (2008). Modulation of the eukaryotic initiation factor 2 alpha-subunit kinase PERK by tyrosine phosphorylation. J. Biol. Chem. 283, 469-475. DOI |
14 | Smith, H.L., and Mallucci, G.R. (2016). The unfolded protein response: mechanisms and therapy of neurodegeneration. Brain 139, 2113-2121. DOI |
15 | Song, J.X., Choi, M.Y., Wong, K.C., Chung, W.W., Sze, S.C., Ng, T.B., and Zhang, K.Y. (2012) Baicalein antagonizes rotenone-induced apoptosis in dopaminergic SH-SY5Y cells related to Parkinsonism. Chin. Med. 7, 1. DOI |
16 | Song, G.J., Jung, M., Kim, J.H., Park, H., Rahman, M.H., Zhang, S., Zhang, Z.Y., Park, D.H., Kook, H., Lee, I.K., et al. (2016). A novel role for protein tyrosine phosphatase 1B as a positive regulator of neuroinflammation. J. Neuroinflammation 13, 86. DOI |
17 | Swarnkar, S., Goswami, P., Kamat, P.K., Gupta, S., Patro, I.K., Singh, S., and Nath, C. (2012). Rotenone-induced apoptosis and role of calcium: a study on Neuro-2a cells. Arch. Toxicol. 86, 1387-1397. DOI |
18 | Vieira, M.N., Lyra E Silva, N.M., Ferreira, S.T., and De Felice, F.G. (2017). Protein tyrosine phosphatase 1B (PTP1B): a potential target for Alzheimer's therapy? Front. Aging Neurosci. 9, 7. |
19 | Wei, H.J., Xu, J.H., Li, M.H., Tang, J.P., Zou, W., Zhang, P., Wang, L., Wang, C.Y., and Tang, X.Q. (2014). Hydrogen sulfide inhibits homocysteine-induced endoplasmic reticulum stress and neuronal apoptosis in rat hippocampus via upregulation of the BDNF-TrkB pathway. Acta Pharmacol. Sin. 35, 707-715. DOI |
20 | Werner, E.D., Brodsky, J.L., and McCracken, A.A. (1996). Proteasome-dependent endoplasmic reticulum-associated protein degradation: an unconventional route to a familiar fate. Proc. Natl. Acad. Sci. USA 93, 13797-13801. DOI |
21 | Xu, Y., Liu, X., Guo, F., Ning, Y., Zhi, X., Wang, X., Chen, S., Yin, L., and Li, X. (2012). Effect of estrogen sulfation by SULT1E1 and PAPSS on the development of estrogen-dependent cancers. Cancer Sci. 103, 1000-1009. DOI |
22 | Wiesmann, C., Barr, K.J., Kung, J., Zhu, J., Erlanson, D.A., Shen, W., Fahr, B.J., Zhong, M., Taylor, L., Randal, M., et al. (2004). Allosteric inhibition of protein tyrosine phosphatase 1B. Nat. Struct. Mol. Biol. 11, 730-737. DOI |
23 | Xiang, C., Wang, Y., Zhang, H., and Han, F. (2017). The role of endoplasmic reticulum stress in neurodegenerative disease. Apoptosis 22, 1-26. DOI |
24 | Xu, C., Bailly-Maitre, B., and Reed, J.C. (2005). Endoplasmic reticulum stress: cell life and death decisions. J. Clin. Invest. 115, 2656-2664. DOI |
25 | Zhang, K. (2010). Integration of ER stress, oxidative stress and the inflammatory response in health and disease. Int. J. Clin. Exp. Med. 3, 33-40. |
26 | Cui, T., Lai, Y., Janicki, J.S., and Wang, X. (2016). Nuclear factor erythroid-2 related factor 2 (Nrf2)-mediated protein quality control in cardiomyocytes. Front. Biosci. (Landmark Ed.) 21, 192-202. DOI |
27 | Zhu, W., Bijur, G.N., Styles, N.A., and Li, X. (2004). Regulation of FOXO3a by brain-derived neurotrophic factor in differentiated human SH-SY5Y neuroblastoma cells. Brain Res. Mol. Brain Res. 126, 45-56. DOI |
28 | Zhu, X., Zhou, Y., Tao, R., Zhao, J., Chen, J., Liu, C., Xu, Z., Bao, G., Zhang, J., Chen, M., et al. (2015). Upregulation of PTP1B after rat spinal cord injury. Inflammation 38, 1891-1902. DOI |
29 | Chung, J., Kim, K.H., Lee, S.C., An, S.H., and Kwon, K. (2015). Ursodeoxycholic acid (UDCA) exerts anti-atherogenic effects by inhibiting endoplasmic reticulum (ER) stress induced by disturbed flow. Mol. Cells 38, 851-858. DOI |
30 | Cui, W., Bai, Y., Luo, P., Miao, L., and Cai, L. (2013). Preventive and therapeutic effects of MG132 by activating Nrf2-ARE signaling pathway on oxidative stress-induced cardiovascular and renal injury. Oxid. Med. Cell. Longev. 2013, 306073. |
31 | Day, B.J., Patel, M., Calavetta, L., Chang, L.Y., and Stamler, J.S. (1999). A mechanism of paraquat toxicity involving nitric oxide synthase. Proc. Natl. Acad. Sci. USA 96, 12760-12765. DOI |
32 | Hakim, F., Wang, Y., Carreras, A., Hirotsu, C., Zhang, J., Peris, E., and Gozal, D. (2015). Chronic sleep fragmentation during the sleep period induces hypothalamic endoplasmic reticulum stress and PTP1b-mediated leptin resistance in male mice. Sleep 38, 31-40. DOI |
33 | Foufelle, F., and Fromenty, B. (2016). Role of endoplasmic reticulum stress in drug-induced toxicity. Pharmacol. Res. Perspect. 4, e00211. DOI |
34 | Goswami, P., Gupta, S., Biswas, J., Joshi, N., Swarnkar, S., Nath, C., and Singh, S. (2016). Endoplasmic reticulum stress plays a key role in rotenone-induced apoptotic death of neurons. Mol. Neurobiol. 53, 285-298. DOI |
35 | Gu, F., Nguyen, D.T., Stuible, M., Dube, N., Tremblay, M.L., and Chevet, E. (2004). Protein-tyrosine phosphatase 1B potentiates IRE1 signaling during endoplasmic reticulum stress. J. Biol. Chem. 279, 49689-49693. DOI |
36 | Kim, H.J., Raphael, A.R., LaDow, E.S., McGurk, L., Weber, R.A., Trojanowski, J.Q., Lee, V.M., Finkbeiner, S., Gitler, A.D., and Bonini, N.M. (2014). Therapeutic modulation of phosphorylation rescues TDP-43 toxicity in amyotrophic lateral sclerosis disease models. Nat. Genet. 46, 152-160. DOI |
37 | Hardie, R.A., van Dam, E., Cowley, M., Han, T.L., Balaban, S., Pajic, M., Pinese, M., Iconomou, M., Shearer, R.F., McKenna, J., et al. (2017). Mitochondrial mutations and metabolic adaptation in pancreatic cancer. Cancer Metab. 5, 2. DOI |
38 | Hotamisligil, G.S. (2010). Endoplasmic reticulum stress and the inflammatory basis of metabolic disease. Cell 140, 900-917. DOI |
39 | Kapeta, S., Chondrogianni, N., and Gonos, E.S. (2010). Nuclear erythroid factor 2-mediated proteasome activation delays senescence in human fibroblasts. J. Biol. Chem. 285, 8171-8184. DOI |
40 | Kwak, M.K., Wakabayashi, N., Greenlaw, J.L., Yamamoto, M., and Kensler, T.W. (2003a). Antioxidants enhance mammalian proteasome expression through the Keap1-Nrf2 signaling pathway. Mol. Cell. Biol. 23, 8786-8794. DOI |
41 | Kwak, M.K., Wakabayashi, N., Itoh, K., Motohashi, H., Yamamoto, M., and Kensler, T.W. (2003b). Modulation of gene expression by cancer chemopreventive dithiolethiones through the Keap1-Nrf2 pathway. Identification of novel gene clusters for cell survival. J. Biol. Chem. 278, 8135-8145. DOI |
42 | Mobasher, M.A., Gonzalez-Rodriguez, A., Santamaria, B., Ramos, S., Martin, M.A., Goya, L., and Valverde, A.M. (2013). Protein tyrosine phosphatase 1B modulates GSK3beta/Nrf2 and IGFIR signaling pathways in acetaminophen-induced hepatotoxicity. Cell Death Dis. 4, e626. DOI |
43 | Oslowski, C.M., and Urano, F. (2011). Measuring ER stress and the unfolded protein response using mammalian tissue culture system. Methods Enzymol. 490, 71-92. |
44 | Moreno, J.A., Halliday, M., Molloy, C., Radford, H., Verity, N., Axten, J.M., Ortori, C.A., Willis, A.E., Fischer, P.M., Barrett, D.A., et al. (2013). Oral treatment targeting the unfolded protein response prevents neurodegeneration and clinical disease in prion-infected mice. Sci. Transl. Med. 5, 206ra138. |
45 | Nakajima, S., Kato, H., Takahashi, S., Johno, H., and Kitamura, M. (2011). Inhibition of NF-kappaB by MG132 through ER stressmediated induction of LAP and LIP. FEBS Lett. 585, 2249-2254. DOI |
46 | Nandipati, S., and Litvan, I. (2016). Environmental Exposures and Parkinson's Disease. Int. J. Environ. Res. Public Health 13, 881. DOI |
47 | Pal, R., Monroe, T.O., Palmieri, M., Sardiello, M., and Rodney, G.G. (2014). Rotenone induces neurotoxicity through Rac1-dependent activation of NADPH oxidase in SHSY-5Y cells. FEBS Lett. 588, 472-481. DOI |
48 | Ozcan, L., and Tabas, I. (2012). Role of endoplasmic reticulum stress in metabolic disease and other disorders. Annu. Rev. Med. 63, 317-328. DOI |
49 | Ozek, C., Kanoski, S.E., Zhang, Z.Y., Grill, H.J., and Bence, K.K. (2014). Protein-tyrosine phosphatase 1B (PTP1B) is a novel regulator of central brain-derived neurotrophic factor and tropomyosin receptor kinase B (TrkB) signaling. J. Biol. Chem. 289, 31682-31692. DOI |
50 | Pajares, M., Cuadrado, A., and Rojo, A.I. (2017). Modulation of proteostasis by transcription factor NRF2 and impact in neurodegenerative diseases. Redox Biol. 11, 543-553. DOI |
51 | Panzhinskiy, E., Ren, J., and Nair, S. (2013a). Protein tyrosine phosphatase 1B and insulin resistance: role of endoplasmic reticulum stress/reactive oxygen species/nuclear factor kappa B axis. PLoS One 8, e77228. DOI |