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Induction of Immunological Tolerance by Apoptotic Cells Requires Caspase-Dependent Oxidation of High-Mobility Group Box-1 Protein
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The mammalian immune system discriminates between modes of cell death; necrosis often results in inflammation and adaptive immunity, whereas apoptosis tends to be anti-inflammatory and promote immune tolerance. We have examined apoptosis for the features responsible for tolerance; specifically, we looked at the roles of caspases and mitochondria. Our results show that caspase activation targeted the mitochondria to produce reactive oxygen species (ROS), which were critical to tolerance induction by apoptotic cells. ROS oxidized the potential danger signal high-mobility group box-1 protein (HMGB1) released from dying cells and thereby neutralized its stimulatory activity. Apoptotic cells failed to induce tolerance and instead stimulated immune responses by scavenging or by mutating a mitochondrial caspase target protein when ROS activity was prohibited. Similarly, blocking sites of oxidation in HMGB1 prevented tolerance induction by apoptotic cells. These results suggest that caspase-orchestrated mitochondrial events determine the impact of apoptotic cells on the immune response.
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“Potential immunogenic signals emanating from dying cells include proteins that appear at the surface of stressed and dying cells (such as calreticulin and heat shock proteins, HSPs), lipid moieties that flip from the inner plasma membrane leaflet to the outer leaflet (such as phosphatidylserine) 38,60, proteins that are released into the supernatant of cells (such as HMGB1) 51, as well as nucleic”
From Immunogenic and tolerogenic cell death (2009) · cites this paper as [51]
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“That said, it should be noted that biological activities of HMGB1 may flip from pro-inflammatory to anti-inflammatory depending on multiple variables including its oxidation state [917–923].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [921]
In the citing paper
“The inhibition of caspases affects the exposure of find-me signals 40, eat-me signals 40 (Box 4), and the secretion of DAMPs51 from dying cells, as well as the exposure of CRT on anthracyclin-treated cancer cells60.”
From Immunogenic and tolerogenic cell death (2009) · cites this paper as [51]
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“Thus, HMGB1 may act on the receptor for advanced glycated endproducts (RAGEs) and possibly the toll-like receptors (TLRs) including TLR2 and TLR4 51,52, although the latter are controversial 53.”
From Immunogenic and tolerogenic cell death (2009) · cites this paper as [51]
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Citations
Cites
Release of chromatin protein HMGB1 by necrotic cells triggers inflammation
Scaffidi, P., Misteli, T., & Bianchi, M. E. (2002) · Nature · doi:10.1038/nature00858 · Cited by 4,221
The Danger Model: A Renewed Sense of Self
Matzinger, P. (2002) · Science · doi:10.1126/science.1071059 · Cited by 4,205
HMG-1 as a Late Mediator of Endotoxin Lethality in Mice
Wang, H., Bloom, O., Zhang, M., Vishnubhakat, J. M., Ombrellino, M., Che, J., Frazier, A., Yang, H., Ivanova, S., Borovikova, L. V., et al. (1999) · Science · doi:10.1126/science.285.5425.248 · Cited by 3,386
Yang, Y., Li, S., Yang, Q., Shi, Y., Zheng, M., Liu, Y., Chen, F., Song, G., Xu, H., Wan, T., et al. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000358696 · Cited by 3,263
Calreticulin exposure dictates the immunogenicity of cancer cell death
Obeid, M., Tesniere, A., Ghiringhelli, F., Fimia, G. M., Apetoh, L., Perfettini, J.-L., Castedo, M., Mignot, G., Panaretakis, T., Casares, N., et al. (2007) · Nature Medicine · doi:10.1038/nm1523 · Cited by 3,216
Fadok, V. A., Bratton, D. L., Konowal, A., Freed, P. W., Westcott, J. Y., & Henson, P. M. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1112 · Cited by 3,166 · cited 4×
“Although these mediators can stimulate immunity, apoptotic cells can inhibit inflammatory and immunological responses driven by macrophages and DCs (Fadok et al., 1998).”
BackgroundInfluentialSteinman, R. M., Hawiger, D., & Nussenzweig, M. C. (2003) · Annual Review of Immunology · doi:10.1146/annurev.immunol.21.120601.141040 · Cited by 3,162
Apoptosis: controlled demolition at the cellular level
Taylor, R. C., Cullen, S. P., & Martin, S. J. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2312 · Cited by 2,708
Mitochondria, oxidative stress and cell death
Ott, M., Gogvadze, V. G., Orrenius, S., & Zhivotovsky, B. (2007) · APOPTOSIS · doi:10.1007/s10495-007-0756-2 · Cited by 2,020
Kamata, H., Honda, S.-I., Maeda, S., Chang, L., Hirata, H., & Karin, M. (2005) · Cell · doi:10.1016/j.cell.2004.12.041 · Cited by 1,792
Cited by
Sorted by citations
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationImmunogenic Cell Death in Cancer Therapy
Kroemer, G., Galluzzi, L., Kepp, O., & Zitvogel, L. (2013) · Annual Review of Immunology · doi:10.1146/annurev-immunol-032712-100008 · Cited by 3,303
Immunogenic cell death and DAMPs in cancer therapy
Krysko, D. V., Garg, A. D., Kaczmarek, A., Krysko, O., Agostinis, P., & Vandenabeele, P. (2012) · Nature Reviews Cancer · doi:10.1038/nrc3380 · Cited by 3,223
Mitochondria and cell death: outer membrane permeabilization and beyond
Tait, S. W. G., & Green, D. R. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2952 · Cited by 2,593
Self-citationThe molecular machinery of regulated cell death
Tang, D., Kang, R., Berghe, T. V., Vandenabeele, P., & Kroemer, G. (2019) · Cell Research · doi:10.1038/s41422-019-0164-5 · Cited by 2,675
Necroptosis and its role in inflammation
Pasparakis, M., & Vandenabeele, P. (2015) · Nature · doi:10.1038/nature14191 · Cited by 2,148
ROS and the DNA damage response in cancer
Srinivas, U. S., Tan, B. W. Q., Vellayappan, B. A., & Jeyasekharan, A. D. (2019) · Redox Biology · doi:10.1016/j.redox.2018.101084 · Cited by 2,144
“cells has however been reported to also mediate immunological tolerance [125], although the relevance of this finding to ICD after chemotherapy is unclear.”
BackgroundHMGB1 is a therapeutic target for sterile inflammation and infection
Andersson, U., & Tracey, K. J. (2011) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101323 · Cited by 1,437
HMGB1 and RAGE in Inflammation and Cancer
Sims, G. P., Rowe, D. C., Rietdijk, S. T., Herbst, R., & Coyle, A. J. (2010) · Annual Review of Immunology · doi:10.1146/annurev.immunol.021908.132603 · Cited by 1,436
Necroptosis: The Release of Damage-Associated Molecular Patterns and Its Physiological Relevance
Kaczmarek, A., Vandenabeele, P., & Krysko, D. V. (2013) · Immunity · doi:10.1016/j.immuni.2013.02.003 · Cited by 1,411
PAMP s and DAMP s: signal 0s that spur autophagy and immunity
Tang, D., Kang, R., Coyne, C. B., Zeh, H. J., & Lotze, M. T. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01146.x · Cited by 1,327
Immunogenic and tolerogenic cell death
Green, D. R., Ferguson, T., Zitvogel, L., & Kroemer, G. (2009) · Nature Reviews Immunology · doi:10.1038/nri2545 · Cited by 1,176
Self-citationDisease-associated functions of IL-33: the new kid in the IL-1 family
Liew, F. Y., Pitman, N. I., & McInnes, I. B. (2010) · Nature reviews. Immunology · doi:10.1038/nri2692 · Cited by 1,020
Kang, R., Chen, R., Zhang, Q., Hou, W., Wu, S., Cao, L., Huang, J., Yu, Y., Fan, X.-G., Yan, Z., et al. (2014) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2014.05.001 · Cited by 956
Apoptotic Caspases Suppress mtDNA-Induced STING-Mediated Type I IFN Production
White, M. J., McArthur, K., Metcalf, D., Lane, R. M., Cambier, J. C., Herold, M. J., van Delft, M. F., Bedoui, S., Lessene, G., Ritchie, M. E., et al. (2014) · Cell · doi:10.1016/j.cell.2014.11.036 · Cited by 983
“Although apoptotic caspases have been previously reported to inactivate the DAMPs HMGB1 (Kazama et al., 2008) and IL33 (Cayrol and Girard, 2009; Lüthi et al.”
Endogenous HMGB1 regulates autophagy
Tang, D., Kang, R., Livesey, K. M., Cheh, C.-W., Farkas, A., Loughran, P., Hoppe, G., Bianchi, M. E., Tracey, K. J., Zeh, H. J., et al. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911078 · Cited by 951
Self-citationTargeting immunogenic cell death in cancer
Ahmed, A. S., & Tait, S. W. G. (2020) · Molecular Oncology · doi:10.1002/1878-0261.12851 · Cited by 964
The clearance of dead cells by efferocytosis
Boada-Romero, E., Martinez, J., Heckmann, B. L., & Green, D. R. (2020) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-020-0232-1 · Cited by 924
Self-citationZitvogel, L., Galluzzi, L., Smyth, M. J., & Kroemer, G. (2013) · Immunity · doi:10.1016/j.immuni.2013.06.014 · Cited by 901
Consensus guidelines for the detection of immunogenic cell death
Kepp, O., Senovilla, L., Vitale, I., Vacchelli, E., Adjemian, S., Agostinis, P., Apetoh, L., Aranda, F., Barnaba, V., Bloy, N., et al. (2014) · OncoImmunology · doi:10.4161/21624011.2014.955691 · Cited by 832
Self-citationYang, H., Hreggvidsdottir, H. S., Palmblad, K., Wang, H., Ochani, M., Li, J., Lü, B., Chavan, S. S., Rosas‐Ballina, M., Al‐Abed, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1003893107 · Cited by 812
Pattern Recognition Receptors and the Host Cell Death Molecular Machinery
Amarante-Mendes, G. P., Adjemian, S., Branco, L. M., Zanetti, L. C., Weinlich, R., & Bortoluci, K. R. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02379 · Cited by 802
The role of oxidative stress during inflammatory processes
Lugrin, J., Rosenblatt‐Velin, N., Parapanov, R., & Liaudet, L. (2013) · Biological Chemistry · doi:10.1515/hsz-2013-0241 · Cited by 766
Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J., Cattaneo, A., De Marchis, F., Liu, J., Antonelli, A., Preti, A., Raeli, L., et al. (2012) · Journal of Experimental Medicine · doi:10.1084/jem.20120189 · Cited by 720
“High ROS levels produced during apoptosis cause terminal oxidation of HMGB1, redirecting its ability to activate acquired immune responses toward tolerance (Kazama et al., 2008).”
BackgroundEmerging role of damage-associated molecular patterns derived from mitochondria in inflammation
Krysko, D. V., Agostinis, P., Krysko, O., Garg, A. D., Bachert, C., Lambrecht, B. N., & Vandenabeele, P. (2011) · Trends in Immunology · doi:10.1016/j.it.2011.01.005 · Cited by 680
HMGB1: A multifunctional alarmin driving autoimmune and inflammatory disease
Harris, H. E., Andersson, U., & Pisetsky, D. S. (2012) · Nature Reviews Rheumatology · doi:10.1038/nrrheum.2011.222 · Cited by 689
HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses
Yanai, H., Ban, T., Wang, Z., Choi, M. K., Kawamura, T., Negishi, H., Nakasato, M., Lu, Y., Hangai, S., Koshiba, R., et al. (2009) · Nature · doi:10.1038/nature08512 · Cited by 708
Immune escape to PD-L1/PD-1 blockade: seven steps to success (or failure)
Kim, J. M., & Chen, D. S. (2016) · Annals of Oncology · doi:10.1093/annonc/mdw217 · Cited by 648
The Sedoheptulose Kinase CARKL Directs Macrophage Polarization through Control of Glucose Metabolism
Haschemi, A., Kosma, P., Gille, L., Evans, C. R., Burant, C. F., Starkl, P., Knapp, B., Haas, R., Schmid, J. A., Jandl, C., et al. (2012) · Cell Metabolism · doi:10.1016/j.cmet.2012.04.023 · Cited by 635
RIPK1 and NF-κB signaling in dying cells determines cross-priming of CD8 + T cells
Yatim, N., Jusforgues-Saklani, H., Orozco, S. L., Schulz, O., da Silva, R. B., Sousa, C. R. E., Green, D. R., Oberst, A., & Albert, M. L. (2015) · Science · doi:10.1126/science.aad0395 · Cited by 643
Self-citationConrad, M., & Sato, H. (2011) · Amino Acids · doi:10.1007/s00726-011-0867-5 · Cited by 621
The Endotoxin Delivery Protein HMGB1 Mediates Caspase-11-Dependent Lethality in Sepsis
Deng, M., Tang, Y., Li, W., Wang, X., Zhang, R., Zhang, X., Zhao, X. S., Liu, J., Tang, C. W., Liu, Z., et al. (2018) · Immunity · doi:10.1016/j.immuni.2018.08.016 · Cited by 596
Linking oxidative stress to inflammation: Toll-like receptors
Gill, R., Tsung, A., & Billiar, T. (2010) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2010.01.006 · Cited by 553
Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features
Berghe, T. V., Vanlangenakker, N., Parthoens, E., Deckers, W., Devos, M., Festjens, N., Guerin, C. J., Brunk, U. T., Declercq, W., & Vandenabeele, P. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.184 · Cited by 639
IL-1α and IL-1β Recruit Different Myeloid Cells and Promote Different Stages of Sterile Inflammation
Rider, P., Carmi, Y., Guttman, O., Braiman, A., Cohen, I., Voronov, E., White, M. R., Dinarello, C. A., & Apte, R. N. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1102048 · Cited by 546
High-mobility group box 1 and cancer
Tang, D., Kang, R., Zeh, H. J., & Lotze, M. T. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.11.014 · Cited by 518
Immunogenic cell death, DAMPs and anticancer therapeutics: An emerging amalgamation
Garg, A. D., Nowis, D., Gołąb, J., Vandenabeele, P., Krysko, D. V., & Agostinis, P. (2009) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2009.08.003 · Cited by 517
Decoding Cell Death Signals in Inflammation and Immunity
Zitvogel, L., Kepp, O., & Kroemer, G. (2010) · Cell · doi:10.1016/j.cell.2010.02.015 · Cited by 558
HMGB1 in Cancer: Good, Bad, or Both?
Kang, R., Zhang, Q., Zeh, H. J., Lotze, M. T., & Tang, D. (2013) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-0495 · Cited by 505
Acetaminophen hepatotoxicity and repair: the role of sterile inflammation and innate immunity
Jaeschke, H., Williams, C. D., Ramachandran, A., & Bajt, M. L. (2011) · Liver International · doi:10.1111/j.1478-3231.2011.02501.x · Cited by 478
High-Mobility Group Box 1, Oxidative Stress, and Disease
Tang, D., Kang, R., Zeh, H. J., & Lotze, M. T. (2010) · Antioxidants and Redox Signaling · doi:10.1089/ars.2010.3356 · Cited by 475
HMGB1 release and redox regulates autophagy and apoptosis in cancer cells
Tang, D., Kang, R., Cheh, C.-W., Livesey, K. M., Liang, X., Schapiro, N. E., Benschop, R., Sparvero, L. J., Amoscato, A. A., Tracey, K. J., et al. (2010) · Oncogene · doi:10.1038/onc.2010.261 · Cited by 461
Dying cells actively regulate adaptive immune responses
Yatim, N., Cullen, S., & Albert, M. L. (2017) · Nature Reviews Immunology · doi:10.1038/nri.2017.9 · Cited by 442
HMGB1, IL-1α, IL-33 and S100 proteins: dual-function alarmins
Bertheloot, D., & Latz, E. (2017) · Cellular & Molecular Immunology · doi:10.1038/cmi.2016.34 · Cited by 455
Manipulation of Host Cell Death Pathways during Microbial Infections
Lamkanfi, M., & Dixit, V. M. (2010) · Cell Host & Microbe · doi:10.1016/j.chom.2010.06.007 · Cited by 472
Cell death and immunity in cancer: From danger signals to mimicry of pathogen defense responses
Garg, A. D., & Agostinis, P. (2017) · Immunological Reviews · doi:10.1111/imr.12574 · Cited by 451
Emerging inflammasome effector mechanisms
Lamkanfi, M. (2011) · Nature reviews. Immunology · doi:10.1038/nri2936 · Cited by 448
Many stimuli pull the necrotic trigger, an overview
Vanlangenakker, N., Berghe, T. V., & Vandenabeele, P. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.164 · Cited by 418
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Garg, A. D., Galluzzi, L., Apétoh, L., Baert, T., Birge, R. B., Pedro, J. M. B., Breckpot, K., Brough, D., Chaurio, R. A., Cirone, M., et al. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00588 · Cited by 420
Self-citationYang, H., Lundbäck, P., Ottosson, L., Erlandsson-Harris, H., Venereau, E., Bianchi, M. E., Al-Abed, Y., Andersson, U., Tracey, K. J., & Antoine, D. J. (2012) · Molecular Medicine · doi:10.2119/molmed.2011.00389 · Cited by 407
RetractedParainflammation, Chronic Inflammation and Age-Related Macular Degeneration
Chen, M., & Xu, H. (2015) · Journal of Leukocyte Biology · doi:10.1189/jlb.3ri0615-239r · Cited by 381
The multifunctional protein HMGB1: 50 years of discovery
Tang, D., Kang, R., Zeh, H. J., & Lotze, M. T. (2023) · Nature reviews. Immunology · doi:10.1038/s41577-023-00894-6 · Cited by 405
Redox control of inflammation in macrophages
Brüne, B., Dehne, N., Grossmann, N., Jung, M., Namgaladze, D., Schmid, T., von Knethen, A., & Weigert, A. (2013) · Antioxidants & Redox Signaling · doi:10.1089/ars.2012.4785 · Cited by 377
Snyder, A. G., Hubbard, N., Messmer, M. N., Kofman, S. B., Hagan, C. E., Orozco, S. L., Chiang, K., Daniels, B. P., Baker, D. A., & Oberst, A. (2019) · Science Immunology · doi:10.1126/sciimmunol.aaw2004 · Cited by 382
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Self-citationAutophagy in immunity and cell‐autonomous defense against intracellular microbes
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Molecular mechanisms of late apoptotic/necrotic cell clearance
Poon, I. K. H., Hulett, M. D., & Parish, C. R. (2009) · Cell Death and Differentiation · doi:10.1038/cdd.2009.195 · Cited by 369
Signaling pathways and intervention therapies in sepsis
Zhang, Y., & Ning, B. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00816-9 · Cited by 369
Targeting HMGB1 in inflammation
Yang, H., & Tracey, K. J. (2010) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2009.11.019 · Cited by 351
Multimodal immunogenic cancer cell death as a consequence of anticancer cytotoxic treatments
Inoue, H., & Tani, K. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.84 · Cited by 362
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Chen, M., Luo, C., Zhao, J., Devarajan, G., & Xu, H. (2019) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2018.10.003 · Cited by 305
IL‐33‐activated dendritic cells are critical for allergic airway inflammation
Besnard, A., Togbe, D., Guillou, N., Erard, F., Quesniaux, V. F. J., & Ryffel, B. (2011) · European Journal of Immunology · doi:10.1002/eji.201041033 · Cited by 341
Bianchi, M. E., Crippa, M. P., Manfredi, A. A., Mezzapelle, R., Rovere, P. Q., & Vénéreau, E. (2017) · Immunological Reviews · doi:10.1111/imr.12601 · Cited by 328
The Role of HMGB1 in the Pathogenesis of Inflammatory and Autoimmune Diseases
Magna, M., & Pisetsky, D. S. (2014) · Molecular Medicine · doi:10.2119/molmed.2013.00164 · Cited by 358
Cancer and Inflammation: Promise for Biologic Therapy
Demaria, S., Pikarsky, E., Karin, M., Coussens, L. M., Chen, Y., El-Omar, E. M., Trinchieri, G., Dubinett, S. M., Mao, J. T., Szabo, E. M., et al. (2010) · Journal of Immunotherapy · doi:10.1097/cji.0b013e3181d32e74 · Cited by 336
High-mobility group box 1 protein (HMGB1) operates as an alarmin outside as well as inside cells
Andersson, U., Yang, H., & Harris, H. (2018) · Seminars in Immunology · doi:10.1016/j.smim.2018.02.011 · Cited by 309
ROS-induced autophagy in cancer cells assists in evasion from determinants of immunogenic cell death
Garg, A. D., Dudek, A. M., Ferreira, G. B., Verfaillie, T., Vandenabeele, P., Krysko, D. V., Mathieu, C., & Agostinis, P. (2013) · Autophagy · doi:10.4161/auto.25399 · Cited by 305
Interleukin-33 – cytokine of dual function or novel alarmin?
Haraldsen, G., Balogh, J., Pollheimer, J., Sponheim, J., & Küchler, A. M. (2009) · Trends in Immunology · doi:10.1016/j.it.2009.03.003 · Cited by 319
Antoine, D. J., Jenkins, R. E., Dear, J. W., Williams, D. P., McGill, M. R., Sharpe, M. R., Craig, D. G. N., Simpson, K. J., Jaeschke, H., & Park, B. K. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2011.12.019 · Cited by 307
RetractedPhotodynamic therapy: illuminating the road from cell death towards anti-tumour immunity
Garg, A. D., Nowis, D., Golab, J., & Agostinis, P. (2010) · Apoptosis · doi:10.1007/s10495-010-0479-7 · Cited by 297
Many faces of DAMPs in cancer therapy
Krysko, O., Aaes, T. L., Bachert, C., Vandenabeele, P., & Krysko, D. V. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.156 · Cited by 309
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Aboelella, N. S., Brandle, C., Kim, T., Ding, Z., & Zhou, G. (2021) · Cancers · doi:10.3390/cancers13050986 · Cited by 303
Li, J., Liu, J., Zhou, Z., Wu, R., Chen, X., Yu, C., Stockwell, B. R., Kroemer, G., Kang, R., & Tang, D. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.adg3049 · Cited by 305
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Nam, G., Choi, Y., Kim, G. B., Kim, S., Kim, S. A., & Kim, I. (2020) · Advanced Materials · doi:10.1002/adma.202002440 · Cited by 270
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Yan, Y. Q., Tang, D., & Kang, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00093 · Cited by 268
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Singh, S., Ornatowski, W., Vergne, I., Naylor, J., Delgado, M. A., Roberts, E. A., Ponpuak, M., Master, S. S., Pilli, M., White, E., et al. (2010) · Nature Cell Biology · doi:10.1038/ncb2119 · Cited by 268
Zhao, X. L., Yang, K., Zhao, R., Ji, T., Wang, X., Yang, X., Zhang, Y., Cheng, K., Liu, S., Hao, J., et al. (2016) · Biomaterials · doi:10.1016/j.biomaterials.2016.06.032 · Cited by 259
Switching from Apoptosis to Pyroptosis: Gasdermin-Elicited Inflammation and Antitumor Immunity
Tsuchiya, K. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms22010426 · Cited by 258
Induction of regulatory T cells by macrophages is dependent on production of reactive oxygen species
Kraaij, M. D., Savage, N. D. L., van der Kooij, S. W., Koekkoek, K. M., Wang, J., van den Berg, J. M., Ottenhoff, T. H. M., Kuijpers, T. W., Holmdahl, R., van Kooten, C., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1012016107 · Cited by 259
Apoptosis in cancer: Key molecular signaling pathways and therapy targets
Burz, C. C., Berindan‐Neagoe, I., Bălăcescu, O., & Irimie, A. (2009) · Acta Oncologica · doi:10.1080/02841860902974175 · Cited by 244
Tamai, K., Yamazaki, T., Chino, T., Ishii, M., Otsuru, S., Kikuchi, Y., Iinuma, S., Saga, K., Nimura, K., Shimbo, T., et al. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016753108 · Cited by 248
Targeted scavenging of extracellular ROS relieves suppressive immunogenic cell death
Deng, H., Yang, W., Zhou, Z., Tian, R., Lin, L., Ma, Y., Song, J., & Chen, X. S. (2020) · Nature Communications · doi:10.1038/s41467-020-18745-6 · Cited by 246
Frank, M. G., Weber, M. D., Watkins, L. R., & Maier, S. F. (2015) · Brain, Behavior, and Immunity · doi:10.1016/j.bbi.2015.03.010 · Cited by 237
Qin, Y., Dai, S., Tang, G., Zhang, J., Ren, D., Wang, Z., & Shen, Q. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0900390 · Cited by 228
High mobility group box 1 (HMGB1): a pivotal regulator of hematopoietic malignancies
Yuan, S., Liu, Z., Xu, Z., Liu, J., & Zhang, J. (2020) · Journal of Hematology & Oncology · doi:10.1186/s13045-020-00920-3 · Cited by 232
Indirect regulation of HMGB1 release by gasdermin D
Volchuk, A., Ye, A. A., Chi, L., Steinberg, B. E., & Goldenberg, N. M. (2020) · Nature Communications · doi:10.1038/s41467-020-18443-3 · Cited by 232
The origin and properties of extracellular DNA: From PAMP to DAMP
Pisetsky, D. S. (2012) · Clinical Immunology · doi:10.1016/j.clim.2012.04.006 · Cited by 231
Regulation of Tumor Progression by Programmed Necrosis
Lee, S. Y., Ju, M. K., Jeon, H. M., Jeong, E. K., Lee, Y. J., Kim, C. H., Park, H. G., Han, S. I., & Kang, H. S. (2018) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2018/3537471 · Cited by 238
Biomarkers of liver cell death
Eguchi, A., Wree, A., & Feldstein, A. E. (2014) · Journal of Hepatology · doi:10.1016/j.jhep.2013.12.026 · Cited by 220
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Lei, Y., Wang, K., Deng, L., Chen, Y., Nice, E. C., & Huang, C. (2014) · Medicinal Research Reviews · doi:10.1002/med.21330 · Cited by 210
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Martin, S. J., Henry, C. M., & Cullen, S. P. (2012) · Molecular Cell · doi:10.1016/j.molcel.2012.04.026 · Cited by 206
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Lau, A. N., Wang, S., Jiang, J., Haig, A. R., Pavlosky, A., Linkermann, A., Zhang, Z.-X., & Jevnikar, A. M. (2013) · American Journal of Transplantation · doi:10.1111/ajt.12447 · Cited by 204
Immunogenic cell death modalities and their impact on cancer treatment
Kepp, O., Tesnière, A., Schlemmer, F., Michaud, M., Senovilla, L., Zitvogel, L., & Kroemer, G. (2009) · APOPTOSIS · doi:10.1007/s10495-008-0303-9 · Cited by 210
Anti-inflammatory Mechanisms Triggered by Apoptotic Cells during Their Clearance
Szondy, Z., Sarang, Z., Kiss, B., Garabuczi, É., & Köröskényi, K. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00909 · Cited by 201
HMGB1: The jack‐of‐all‐trades protein is a master DNA repair mechanic
Lange, S. S., & Vásquez, K. M. (2009) · Molecular Carcinogenesis · doi:10.1002/mc.20544 · Cited by 196
Strange attractors: DAMPs and autophagy link tumor cell death and immunity
Hou, W., Zhang, Q., Yan, Z., Chen, R., Zeh, H. J., Kang, R., Lotze, M. T., & Tang, D. (2013) · Cell Death and Disease · doi:10.1038/cddis.2013.493 · Cited by 199
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Linkermann, A., Hackl, M. J., Kunzendorf, U., Walczak, H., Krautwald, S., & Jevnikar, A. M. (2013) · American Journal of Transplantation · doi:10.1111/ajt.12448 · Cited by 193
High‐mobility group box‐1 in sterile inflammation
Tsung, A., Tohme, S., & Billiar, T. R. (2014) · Journal of Internal Medicine · doi:10.1111/joim.12276 · Cited by 187
Rider, P., Voronov, E., Dinarello, C. A., Apte, R. N., & Cohen, I. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1601342 · Cited by 186
Metadata
- Authors
- Kazama, H., Ricci, J.-E., Herndon, J. M., Hoppe, G., Green, D. R., & Ferguson, T. A.
- Affiliations
- Washington University in St. Louis (US)
- Université Côte d'Azur (FR)
- Cleveland Clinic (US)
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Ferguson, Thomas A.
- Venue
- Immunity
- Publisher
- Elsevier BV
- Published
- 2008-07
- Volume
- 29
- Issue
- 1
- Pages
- 21-32
- ISSN
- 1074-7613 (ISSN-L)
- PMC
- PMC2704496
- OpenAlex
- W2084623259
- Cited by
- 627
- References
- 60
- Citations by year
- 2026: 24 · 2025: 23 · 2024: 33 · 2023: 35 · 2022: 24 · 2021: 38 · 2020: 32 · 2019: 26 · 2018: 33 · 2017: 31 · 2016: 20 · 2015: 44 · 2014: 47 · 2013: 43 · 2012: 34
- FWCI
- 19.04
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Immunity (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Research to Prevent Blindness (EY02687)
- National Institutes of Health (AI44848, EY02687, EY06765)
- National Eye Institute (EY 02687, P30EY002687, EY 015570, F32EY006765, EY06765, R01EY015570, R01EY006765)
- National Institute of Allergy and Infectious Diseases (AI44848, R01AI044828, R01AI040646)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Phagocytosis and Immune Regulation
- Keywords
- immune tolerance, apoptotic cells, caspases, HMGB1, high mobility group box 1 protein, reactive oxygen species, oxidative modification, damage-associated molecular patterns, necrosis, tolerance induction
- MeSH terms
- Animals, Dendritic Cells, HeLa Cells, Humans, Immune Tolerance, Mice, Inbred C57BL, Mitochondria, Oxidation-Reduction, Immunoblotting, Apoptosis, Reactive Oxygen Species, Caspases, HMGB1 Protein, Mice
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