The activation of autophagy protects neurons and astrocytes against bilirubin-induced cytotoxicity
Abstract
Unconjugated bilirubin (UCB) neurotoxicity involves oxidative stress, calcium signaling and ER-stress. The same insults can also induce autophagy, a process of "self-eating", with both a pro-survival or a pro-apoptotic role. Our aim was to study the outcome of autophagy activation by UCB in the highly sensitive neuronal SH-SY5Y cells and in the resistant astrocytoma U87 cells. Upon treatment with a toxic dose of UCB, the conversion of LC3-I to LC3-II was detected in both cell lines. Inhibition of autophagy by E64d before UCB treatment increased SH-SY5Y cell mortality and made U87 cells sensitive to UCB. In SH-SY5Y autophagy related genes ATG8 (5 folds), ATG18 (5 folds), p62 (3 folds) and FAM 129A (4.5 folds) were induced 8h after UCB treatment while DDIT4 upregulation (13 folds) started at 4h. mTORC1 inactivation by UCB was confirmed by phosphorylation of 4EBP1. UCB induced LC3-II conversion was completely prevented by pretreating cells with the calcium chelator BAPTA and reduced by 65% using the ER-stress inhibitor 4-PBA. Pretreatment with the PKC inhibitor reduced LC3 mRNA by 70% as compared to cells exposed to UCB alone. Finally, autophagy induction by Trifluoroperazine (TFP) increased the cell viability of rat hippocampal primary neurons upon UCB treatment from 60% to 80%. In SH-SY5Y cells, TFP pretreatment blocked the UCB-induced cleaved caspase-3 protein expression, decreased LDH release from 50% to 23%, reduced the UCB-induction of HO1, CHOP and IL-8 mRNAs by 85%, 70% and 97%. Collectively these data indicate that the activation of autophagy protects neuronal cells from UCB cytotoxicity. The mechanisms of autophagy activation by UCB involves mTOR/ER-stress/PKC/calcium signaling.
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Autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by canonical aggrephagy.
“While autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by the canonical autophagic process of aggrephagy (Frake et al., 2015; Menzies et al., 2017; Qaisiya et al., 2017; Sarkar et al., 2007; Sarkar et al., 2009; Webb et al., 2003; Yamamoto and Simonsen, 2011), effects in microglia of the CNS are more likely due to LANDO.”
From LC3-Associated Endocytosis Facilitates β-Amyloid Clearance and Mitigates Neurodegeneration in Murine Alzheimer’s Disease (2019) · cites this paper as Qaisiya et al., 2017
Cites
Mosmann, T. (1983) · Journal of Immunological Methods · doi:10.1016/0022-1759(83)90303-4 · Cited by 56,104 · see citing works
mTOR Signaling in Growth Control and Disease
Laplante, M., & Sabatini, D. M. (2012) · Cell · doi:10.1016/j.cell.2012.03.017 · Cited by 8,509 · see citing works
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578 · see citing works
Methods in Mammalian Autophagy Research
Mizushima, N., Yoshimori, T., & Levine, B. (2010) · Cell · doi:10.1016/j.cell.2010.01.028 · Cited by 4,497 · see citing works
Regulation mechanisms and signaling pathways of autophagy
He, C., & Klionsky, D. J. (2009) · Annual Review of Genetics · doi:10.1146/annurev-genet-102808-114910 · Cited by 3,609 · see citing works
How to Interpret LC3 Immunoblotting
Mizushima, N., & Yoshimori, T. (2007) · Autophagy · doi:10.4161/auto.4600 · Cited by 2,595 · see citing works
Tanida, I., Ueno, T., & Kominami, E. (2008) · Methods in Molecular Biology™ · doi:10.1007/978-1-59745-157-4_4 · Cited by 1,785 · see citing works
Autophagy, mitochondria and oxidative stress: cross-talk and redox signalling.
Lee, J., Giordano, S., & Zhang, J. (2012) · Biochemical Journal · doi:10.1042/bj20111451 · Cited by 1,438 · see citing works
The autophagosome: origins unknown, biogenesis complex
Lamb, C. A., Yoshimori, T., & Tooze, S. A. (2013) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3696 · Cited by 1,307 · see citing works
UPR, autophagy, and mitochondria crosstalk underlies the ER stress response
Senft, D., & Ronai, Z. A. (2015) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2015.01.002 · Cited by 1,121 · see citing works
Autophagy and signaling: their role in cell survival and cell death
Codogno, P., & Meijer, A. J. (2005) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401751 · Cited by 1,092 · see citing works
Autophagy Counterbalances Endoplasmic Reticulum Expansion during the Unfolded Protein Response
Bernales, S., McDonald, K. L., & Walter, P. (2006) · PLoS Biology · doi:10.1371/journal.pbio.0040423 · Cited by 1,009 · see citing works
Autophagy: assays and artifacts
Barth, S., Glick, D. R., & Macleod, K. F. (2010) · The Journal of Pathology · doi:10.1002/path.2694 · Cited by 794 · see citing works
Crosstalk between autophagy and inflammatory signalling pathways: balancing defence and homeostasis
Cadwell, K. (2016) · Nature reviews. Immunology · doi:10.1038/nri.2016.100 · Cited by 479 · see citing works
Bilirubin-Induced Neurologic Damage — Mechanisms and Management Approaches
Watchko, J. F., & Tiribelli, C. (2013) · New England Journal of Medicine · doi:10.1056/nejmra1308124 · Cited by 395 · see citing works
Self-citationTsvetkov, A. S., Miller, J., Arrasate, M., Wong, J. S., Pleiss, M. A., & Finkbeiner, S. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1004498107 · Cited by 266 · see citing works
Interplay of endoplasmic reticulum stress and autophagy in neurodegenerative disorders
Cai, Y. C., Arikkath, J., Yang, L., Guo, M., Periyasamy, P., & Buch, S. J. (2016) · Autophagy · doi:10.1080/15548627.2015.1121360 · Cited by 258 · see citing works
Kapitulnik, J. (2004) · Molecular Pharmacology · doi:10.1124/mol.104.002832 · Cited by 239 · see citing works
mTOR: on target for novel therapeutic strategies in the nervous system
Maiese, K., Chong, Z. Z., Shang, Y., & Wang, S. (2012) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2012.11.001 · Cited by 226 · see citing works
Regulation of Autophagy by Kinases
Sridharan, S., Jain, K., & Basu, A. (2011) · Cancers · doi:10.3390/cancers3022630 · Cited by 182 · see citing works
Protein Kinase Cθ Is Required for Autophagy in Response to Stress in the Endoplasmic Reticulum
Sakaki, K., Wu, J., & Kaufman, R. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m710209200 · Cited by 179 · see citing works
Bridges between mitochondrial oxidative stress, ER stress and mTOR signaling in pancreatic β cells
Wang, J., Yang, X., & Zhang, J. (2016) · Cellular Signalling · doi:10.1016/j.cellsig.2016.05.007 · Cited by 178 · see citing works
Integration of autophagy, proteasomal degradation, unfolded protein response and apoptosis.
Benbrook, D. M., & Long, A. (2012) · PubMed · Cited by 173 · see citing works
Autophagy as a pro‐death pathway
Denton, D., Xu, T., & Kumar, S. (2015) · Immunology and Cell Biology · doi:10.1038/icb.2014.85 · Cited by 168 · see citing works
Autophagy regulates endoplasmic reticulum stress in ischemic preconditioning
Sheng, R., Liu, X.-Q., Zhang, L.-S., Gao, B., Han, R., Wu, Y.-Q., Zhang, X., & Qin, Z. (2012) · Autophagy · doi:10.4161/auto.18673 · Cited by 155 · see citing works
New concepts in bilirubin encephalopathy
Ostrow, J. D., Pascolo, L., Shapiro, S. M., & Tiribelli, C. (2003) · European Journal of Clinical Investigation · doi:10.1046/j.1365-2362.2003.01261.x · Cited by 153 · see citing works
Self-citationUnbound (Free) Bilirubin: Improving the Paradigm for Evaluating Neonatal Jaundice
Ahlfors, C. E., Wennberg, R. P., Ostrow, J. D., & Tiribelli, C. (2009) · Clinical Chemistry · doi:10.1373/clinchem.2008.121269 · Cited by 150 · see citing works
Self-citationKernicterus and the Molecular Mechanisms of Bilirubin-Induced CNS Injury in Newborns
Watchko, J. F. (2006) · NeuroMolecular Medicine · doi:10.1385/nmm:8:4:513 · Cited by 150 · see citing works
Zucker, S. D., Goessling, W., & Hoppin, A. G. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.16.10852 · Cited by 146 · see citing works
Bilirubin mediated oxidative stress involves antioxidant response activation via Nrf2 pathway
Qaisiya, M., Zabetta, C. D. C., Bellarosa, C., & Tiribelli, C. (2013) · Cellular Signalling · doi:10.1016/j.cellsig.2013.11.029 · Cited by 138 · see citing works
Self-citationOstrow, D. J., Pascolo, L., & Tiribelli, C. (2003) · Pediatric Research · doi:10.1203/01.pdr.0000067486.79854.d5 · Cited by 111 · see citing works
Self-citationJin, H., Seo, S., Woo, S., Kim, E. S., Lee, H., Yoo, D., An, S., Choe, T., Lee, S., Hong, S., et al. (2009) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2009.01.015 · Cited by 110 · see citing works
Chen, Y., Azad, M. B., & Gibson, S. B. (2010) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y10-010 · Cited by 108 · see citing works
The role of dimensionality in neuronal network dynamics
Severino, F. P. U., Ban, J., Song, Q., Tang, M., Ginestra Bianconi, A., Cheng, G., & Torre, V. (2016) · Scientific Reports · doi:10.1038/srep29640 · Cited by 101 · see citing works
Falcão, A. S., Fernandes, A. M. A., Brito, M. A., Silva, R. F. M., & Brites, D. M. T. O. (2006) · Acta Neuropathologica · doi:10.1007/s00401-006-0078-4 · Cited by 94 · see citing works
Roca, L., Calligaris, S. D., Wennberg, R. P., Ahlfors, C. E., Malik, S. G., Ostrow, J. D., & Tiribelli, C. (2006) · Pediatric Research · doi:10.1203/01.pdr.0000245992.89965.94 · Cited by 75 · see citing works
Self-citationThe Pro-Survival Role of Autophagy Depends on Bcl-2 Under Nutrition Stress Conditions
Xu, H., Wu, D., Gu, J., Ge, J., Wu, J., Han, R., Liang, Z., & Qin, Z. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063232 · Cited by 69 · see citing works
Anđjus, P. R., Stević-Marinković, Z., & Cherubim, E. (1997) · The Journal of Physiology · doi:10.1111/j.1469-7793.1997.103bf.x · Cited by 66 · see citing works
Unconjugated bilirubin differentially affects the redox status of neuronal and astroglial cells
Brito, M. A., Rosa, A. I., Falcão, A. S., Fernandes, A. M. A., Silva, R. F. M., Butterfield, D. A., & Brites, D. M. T. O. (2007) · Neurobiology of Disease · doi:10.1016/j.nbd.2007.07.023 · Cited by 64 · see citing works
Palmela, I., Sasaki, H., Cardoso, F. L., Moutinho, M., Kim, K., Brites, D. M. T. O., & Brito, M. A. (2012) · Frontiers in Cellular Neuroscience · doi:10.3389/fncel.2012.00022 · Cited by 63 · see citing works
Sun, G. D., Kobayashi, T., Abe, M., Tada, N., Adachi, H., Shiota, A., Totsuka, Y., & Hino, O. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.06.021 · Cited by 55 · see citing works
Bilirubin-induced ER stress contributes to the inflammatory response and apoptosis in neuronal cells
Qaisiya, M., Brischetto, C., Jašprová, J., Vı́tek, L., Tiribelli, C., & Bellarosa, C. (2016) · Archives of Toxicology · doi:10.1007/s00204-016-1835-3 · Cited by 50 · see citing works
Self-citationVodret, S., Bortolussi, G., Jašprová, J., Vı́tek, L., & Muro, A. F. (2017) · Journal of Neuroinflammation · doi:10.1186/s12974-017-0838-1 · Cited by 50 · see citing works
Gazzin, S., Strazielle, N., Tiribelli, C., & Ghersi‐Egea, J. (2012) · Frontiers in Pharmacology · doi:10.3389/fphar.2012.00089 · Cited by 46 · see citing works
Self-citationIncreased mTORC1 Signaling UPRegulates Stress
Reiling, J. H., & Sabatini, D. M. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.02.011 · Cited by 36 · see citing works
Calligaris, R., Bellarosa, C., Foti, R., Roncaglia, P., Giraudi, P. J., Krmac, H., Tiribelli, C., & Gustincich, S. (2009) · BMC Genomics · doi:10.1186/1471-2164-10-543 · Cited by 32 · see citing works
Self-citation
Flagged first, then by citations
1 of the 47 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Klionsky, D. J., Abdel-Aziz, A. K., Abdelfatah, S., Abdellatif, M., Abdoli, A., Abel, S., Abeliovich, H., Abildgaard, M. H., Abudu, Y. P., Acevedo-Arozena, A., et al. (2021) · Autophagy · doi:10.1080/15548627.2020.1797280 · Cited by 2,622 · see citing works
Self-citationHeckmann, B. L., Teubner, B. J. W., Tummers, B., Boada-Romero, E., Harris, L., Yang, M., Guy, C. S., Zakharenko, S. S., & Green, D. R. (2019) · Cell · doi:10.1016/j.cell.2019.05.056 · Cited by 503 · see citing works
“While autophagy proteins have been shown to impact the clearance of protein aggregates in neurons, most likely by the canonical autophagic process of aggrephagy (Frake et al., 2015; Menzies et al., 2017; Qaisiya et al., 2017; Sarkar et al., 2007; Sarkar et al., 2009; Webb et al., 2003; Yamamoto and Simonsen, 2011), ef…”
Astrocytes autophagy in aging and neurodegenerative disorders
Wang, J., & Xu, C. (2019) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2019.109691 · Cited by 87 · see citing works
Lysosomal Functions in Glia Associated with Neurodegeneration
Kreher, C., Favret, J., Maulik, M., & Shin, D. (2021) · Biomolecules · doi:10.3390/biom11030400 · Cited by 38 · see citing works
Molecular pathophysiology of human MICU1 deficiency
Kohlschmidt, N., Elbracht, M., Czech, A., Häusler, M., Phan, V., Töpf, A., Huang, K., Bartók, Á., Eggermann, K., Zippel, S., et al. (2021) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12694 · Cited by 32 · see citing works
The role of microbiota in neonatal hyperbilirubinemia.
Chen, K., & Yuan, T. (2020) · PubMed Central · Cited by 31 · see citing works
Lysosome exocytosis is involved in astrocyte ATP release after oxidative stress induced by H2O2
Li, Z., Gu, Y., Wen, R., Shen, F., Tian, H., Yang, G., & Zhang, Z. (2019) · Neuroscience Letters · doi:10.1016/j.neulet.2019.03.046 · Cited by 28 · see citing works
NIBAN1, Exploring its Roles in Cell Survival Under Stress Context
Diana, P., & Carvalheira, G. M. G. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.867003 · Cited by 26 · see citing works
Autophagy in brain tumors: molecular mechanisms, challenges, and therapeutic opportunities
Zhang, J., Jinan, Z., & Chen, Y. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-024-06063-0 · Cited by 22 · see citing works
Models of bilirubin neurological damage: lessons learned and new challenges
Gazzin, S., Jayanti, S. D., & Tiribelli, C. (2022) · Pediatric Research · doi:10.1038/s41390-022-02351-x · Cited by 20 · see citing works
Self-citationGarcía‐Juan, M., Ordóñez‐Gutiérrez, L., & Wandosell, F. G. (2023) · Glia · doi:10.1002/glia.24492 · Cited by 20 · see citing works
Translational Approach to the Protective Effect of Bilirubin in Diabetic Kidney Disease
Bianco, A., Tiribelli, C., & Bellarosa, C. (2022) · Biomedicines · doi:10.3390/biomedicines10030696 · Cited by 20 · see citing works
Self-citationZhuang, D., Wang, S., Deng, H., Shi, Y., Liu, C. X., Leng, X., Zhang, Q., Bai, F., Zheng, B., Guo, J., et al. (2024) · International Journal of Oral Science · doi:10.1038/s41368-024-00297-w · Cited by 18 · see citing works
Shaikh, S., Ahmad, K., Ahmad, S. S., Lee, E. J., Lim, J. H., Beg, M. M. A., Verma, A. K., & Choi, I. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/6347792 · Cited by 19 · see citing works
Experimental models assessing bilirubin neurotoxicity
Bortolussi, G., & Muro, A. F. (2019) · Pediatric Research · doi:10.1038/s41390-019-0570-x · Cited by 18 · see citing works
Chen, K.-Y., Cheng, C.-J., Cheng, C.-C., Jhan, K.-Y., Chen, Y., & Wang, L.-C. (2020) · PLoS neglected tropical diseases · doi:10.1371/journal.pntd.0008290 · Cited by 16 · see citing works
Syndecan 4 contributes to osteoclast differentiation induced by RANKL through enhancing autophagy
Li, J., Sun, Z., Lin, Y., Yan, Y., Yan, H., Jing, B., & Han, Z. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2020.107275 · Cited by 15 · see citing works
Niban protein regulates apoptosis in HK-2 cells via caspase-dependent pathway
Tang, S., Wang, J., Liu, J., Huang, Y., Zhou, Y., Yang, S., Zhang, W., Yang, M., & Zhang, H. (2019) · Renal Failure · doi:10.1080/0886022x.2019.1619582 · Cited by 14 · see citing works
Molecular events in brain bilirubin toxicity revisited
Gazzin, S., Bellarosa, C., & Tiribelli, C. (2024) · Pediatric Research · doi:10.1038/s41390-024-03084-9 · Cited by 13 · see citing works
Self-citationNeuroinflammation in Bilirubin Neurotoxicity
Zhang, F., Chen, L., & Jiang, K. (2023) · Journal of Integrative Neuroscience · doi:10.31083/j.jin2201009 · Cited by 13 · see citing works
Ferroptosis contributes to hemolytic hyperbilirubinemia‑induced brain damage in vivo and in vitro
Zhou, J., Lin, X., Liao, S., Li, G., Tang, J., Luo, J., Zhang, C., Wu, S., Xu, L., & Li, H. (2023) · Molecular Medicine Reports · doi:10.3892/mmr.2023.13123 · Cited by 12 · see citing works
Liao, P., Wang, X., Dong, H. Y., Chai, D., Yue, Z., & Lyu, L. (2023) · Shock · doi:10.1097/shk.0000000000002160 · Cited by 11 · see citing works
Zhou, J., Liao, S., Zhang, C., Luo, J., Li, G., & Li, H. (2023) · Molecular Biology Reports · doi:10.1007/s11033-023-08576-1 · Cited by 5 · see citing works
Maternal linoleic acid-rich diet ameliorates bilirubin neurotoxicity in offspring mice
Ding, Y., Wu, X., Chen, X., Wang, J., Ge, F., Wu, J., Wu, J., Zhang, N., Xiao, M., Wu, X., et al. (2024) · Cell Death Discovery · doi:10.1038/s41420-024-02099-9 · Cited by 5 · see citing works
Comprehensive metabolomics study on the pathogenesis of anaplastic astrocytoma via UPLC-Q/TOF-MS
Du, C., Huang, Z., Wei, B., & Li, M. (2022) · Medicine · doi:10.1097/md.0000000000029594 · Cited by 5 · see citing works
Shi, S., Cui, Q., Xu, J., Tang, Z., Shi, B., & Liu, Z. (2020) · Medical Science Monitor · doi:10.12659/msm.926441 · Cited by 5 · see citing works
Dugan, G., Akula, N., Marenco, S., Auluck, P. K., Raznahan, A., Liu, S., DeCasien, A. R., Xu, Q., Feng, N., Kolachana, B. S., et al. (2024) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2024.09.19.613680 · Cited by 3 · see citing works
Qi, X., Deng, M., Li, M., Ma, W., & Zhou, Y. (2025) · Human Cell · doi:10.1007/s13577-025-01298-5 · Cited by 2 · see citing works
Parthenolide ameliorates bilirubin-induced neuronal cell injury by mediating autophagy
Liu, J., Zhang, C., Hu, Y., & Zheng, Z. (2026) · Experimental Brain Research · doi:10.1007/s00221-026-07235-8 · Cited by 1 · see citing works
The Role of ER Stress in Bilirubin Neurotoxicity: A Complex Molecular Network
Qaisiya, M., Tiribelli, C., & Bellarosa, C. (2026) · Antioxidants · doi:10.3390/antiox15040451 · Cited by 1 · see citing works
Self-citationMolecular mechanisms of neonatal bilirubin neurotoxicity: The Subcellular Cascade
Adhikari, A. (2026) · Seminars in Perinatology · doi:10.1016/j.semperi.2026.152306 · Cited by 1 · see citing works
Dimitrijević, M., Žižić, M. V., Jelača, S., Maksimović‐Ivanić, D., Sánchez, D. F., Grolimund, D., Mroginski, M. A., & Spasojević, I. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110466
Exploring Bilirubin’s Impact on Autophagy and Apoptosis in Diabetic Kidney Disease
Maleki, M. H., Dashti, Z. J. S., Monsef, A., Siri, M., Jamali, H., Naiebi, R., Omidi, F., Dehghanian, A., & Shafiee, S. M. (2026) · BioMed Research International · doi:10.1155/bmri/3801742
ALKBH5-mediated autophagic flux impairment is involved in bilirubin neurotoxicity
Zhou, J., Liao, S., Zhang, C., Li, G., Zheng, F., Yu, G., Hu, H., Shao, W., Guo, Z., Wu, S., et al. (2026) · Chemico-Biological Interactions · doi:10.1016/j.cbi.2026.111940
Bilirubin in Parkinson’s disease: pathogenic mechanisms and therapeutic potentials
Wan, Y., Xie, C., Wang, Q., & Wang, X. (2026) · Frontiers in Neuroscience · doi:10.3389/fnins.2026.1806875
- Authors
- Qaisiya, M., Mardešić, P., Pastore, B., Tiribelli, C., & Bellarosa, C.
- Affiliations
- Hebron University (PS)
- Fondazione Italiana Fegato (IT)
- Scuola Internazionale Superiore di Studi Avanzati (IT)
- Corresponding author
- Bellarosa, Cristina
- Venue
- Neuroscience Letters
- Publisher
- Elsevier BV
- Published
- 2017-11
- Volume
- 661
- Pages
- 96-103
- ISSN
- 0304-3940 (ISSN-L)
- OpenAlex
- W2758629344
- Cited by
- 35
- References
- 47
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 4 · 2023: 5 · 2022: 4 · 2021: 4 · 2020: 4 · 2019: 5
- FWCI
- 1.94
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Neuroscience Letters (publishedVersion)
- PubMed (publishedVersion)
- Funders
- AREA Science Park
- Fondazione Italiana Fegato, ONLUS
- Topics
- Health Sciences › Medicine › Epidemiology › Autophagy in Disease and Therapy
- Health Sciences › Medicine › Pediatrics, Perinatology and Child Health › Neonatal Health and Biochemistry
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Keywords
- autophagy, unconjugated bilirubin, bilirubin neurotoxicity, neuroprotection, astrocytes, LC3 conversion, mTOR signaling, endoplasmic reticulum stress, calcium signaling, protein kinase C, oxidative stress, apoptosis, caspase-3, SH-SY5Y cells, U87 cells, hippocampal neurons, DDIT4, CHOP, interleukin-8, hepatorenal syndrome
- MeSH terms
- Astrocytes, Autophagy, Bilirubin, Cell Survival, Humans, Neurons, Signal Transduction, Apoptosis, Cell Line, Tumor, TOR Serine-Threonine Kinases
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