Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release
Open accessAbstract
Tissue damage causes inflammation, by recruiting leukocytes and activating them to release proinflammatory mediators. We show that high-mobility group box 1 protein (HMGB1) orchestrates both processes by switching among mutually exclusive redox states. Reduced cysteines make HMGB1 a chemoattractant, whereas a disulfide bond makes it a proinflammatory cytokine and further cysteine oxidation to sulfonates by reactive oxygen species abrogates both activities. We show that leukocyte recruitment and activation can be separated. A nonoxidizable HMGB1 mutant in which serines replace all cysteines (3S-HMGB1) does not promote cytokine production, but is more effective than wild-type HMGB1 in recruiting leukocytes in vivo. BoxA, a HMGB1 inhibitor, interferes with leukocyte recruitment but not with activation. We detected the different redox forms of HMGB1 ex vivo within injured muscle. HMGB1 is completely reduced at first and disulfide-bonded later. Thus, HMGB1 orchestrates both key events in sterile inflammation, leukocyte recruitment and their induction to secrete inflammatory cytokines, by adopting mutually exclusive redox states.
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HMGB1 biological activities can switch from pro-inflammatory to anti-inflammatory depending on variables including oxidation state.
“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 [918]
The disulfide form of HMGB1 mediates its proinflammatory effects by signaling through TLR4.
“The disulfide form mediates the proinflammatory effects of HMGB1 by signaling through TLR4, whereas the reduced form mediates the chemotactic properties of HMGB1 by forming a complex with the chemokine CXCL12 and signaling through CXCR4.”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
HMGB1 can function either as a chemotactic or proinflammatory mediator depending on the redox state of three critical cysteines.
“HMGB1 can function either as a chemotactic or proinflammatory mediator depending on the redox state of three critical cysteines (Venereau et al, 2012).”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
The reduced form of HMGB1 mediates its chemotactic properties by forming a complex with CXCL12 and signaling through CXCR4.
“The disulfide form mediates the proinflammatory effects of HMGB1 by signaling through TLR4, whereas the reduced form mediates the chemotactic properties of HMGB1 by forming a complex with the chemokine CXCL12 and signaling through CXCR4.”
From Danger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders (2017) · cites this paper as Venereau et al, 2012
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BackgroundSelf-citationSustained Oscillations of NF-κB Produce Distinct Genome Scanning and Gene Expression Profiles
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“Finally, all-cysteine–oxidized HMGB1 prevents HMGB10s cytokine or chemotactic activity (29).”
BackgroundMyeloid-Derived Suppressor Cells
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“, oxidation, reduction, citrullination) that may potentially neutralize, increase, or change their immunogenic properties (31, 32) – a process that is still incompletely understood.”
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“The C-terminal acidic tail (residues 186–215), containing aspartic acid or glutamic acid residues, may compete with DNA for binding to A-box and B-box domains of HMGB1, thus mediating autoinhibition under conditions of cellular or nuclear stress 18 .”
BackgroundInfluentialJAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation
Lü, B., Antoine, D. J., Kwan, K., Lundbäck, P., Wähämaa, H., Schierbeck, H., Robinson, M., van Zoelen, M. A. D., Yang, H., Li, J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1316925111 · Cited by 364 · see citing works
“These data indicate that the mechanisms that regulate HMGB1 release and nuclear translocation are intimately linked to the biological functions of the secreted HMGB1 (11).”
BackgroundMethodInfluentialSelf-citationHigh Mobility Group Box Protein 1 (HMGB1): The Prototypical Endogenous Danger Molecule
Yang, H., Wang, H., Chavan, S. S., & Andersson, U. (2015) · Molecular Medicine · doi:10.2119/molmed.2015.00087 · Cited by 360 · see citing works
Self-citationMetal Drugs and the Anticancer Immune Response
Englinger, B., Pirker, C., Heffeter, P., Terenzi, A., Kowol, C. R., Keppler, B. K., & Berger, W. (2019) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00396 · Cited by 355 · see citing works
The HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis
Huebener, P., Pradère, J., Hernandez, C., Gwak, G., Caviglia, J. M., Mu, X., Loike, J. D., Jenkins, R. E., Antoine, D. J., & Schwabe, R. F. (2014) · Journal of Clinical Investigation · doi:10.1172/jci76887 · Cited by 353 · see citing works
Self-citationSignaling 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 360 · see citing works
“This disulfide form of HMGB1 is capable in mediating massive inflammatory responses such as TNF-α release and NF-κB signaling by allowing binding of reduced C106 with TLR4MD2.(196,197) HMGB1 is also capable to interact on TLR2 and RAGE to elicit cytokine-like activity.”
BackgroundMultimodal 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 352 · see citing works
“As HMGB1 is an intrinsic sensor of oxidative stress,(59) the immunomodulatory properties of HMGB1 might be determined by its redox status.(60,61) Indeed, reduced HMGB1 production from dying cells was shown to trigger the immunogenic DCs, whereas oxidized HMGB1 during apoptosis fails.”
BackgroundDAMPs, MAMPs, and NAMPs in plant innate immunity
Choi, H. W., & Klessig, D. F. (2016) · BMC Plant Biology · doi:10.1186/s12870-016-0921-2 · Cited by 356 · see citing works
“Disulfide bond-containing HMGB1 specifically binds MD-2, which facilitates recognition by TLR4, leading to induction of the NF-κB-mediated transcriptional activation of pro-inflammatory cytokines [13, 15].”
BackgroundGuijarro-Muñoz, I., Compte, M., Álvarez-Cienfuegos, A., Álvarez-Vallina, L., & Sanz, L. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.521161 · Cited by 342 · see citing works
“Recombinant LPS-free HMGB1 in the redox form known to act as an inflammation mediator (20) was kindly provided by M.”
MethodThe Chemokine Receptor CXCR4 in Cell Proliferation and Tissue Regeneration
Bianchi, M. E., & Mezzapelle, R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.02109 · Cited by 339 · see citing works
“Only the reduced form of HMGB1, where the pair of cysteines in the HMG-box domain A do not form a disulfide bond, binds CXCL12 and interacts with CXCR4 (16).”
BackgroundSelf-citationBianchi, 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 327 · see citing works
Self-citationThe role of neuroimmune signaling in alcoholism
Crews, F. T., Lawrimore, C. J., Walter, T. J., & Coleman, L. G. (2017) · Neuropharmacology · doi:10.1016/j.neuropharm.2017.01.031 · Cited by 321 · see citing works
“4b) (Venereau et al., 2012; Yang et al., 2012).”
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 · see citing works
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 · see citing works
Self-citationROS-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 · see citing works
Disulfide HMGB1 derived from platelets coordinates venous thrombosis in mice
Stark, K., Philippi, V., Stockhausen, S., Busse, J., Antonelli, A., Miller, M., Schubert, I., Hoseinpour, P., Chandraratne, S., von Brühl, M.-L., et al. (2016) · Blood · doi:10.1182/blood-2016-04-710632 · Cited by 306 · see citing works
“In venous thrombosis the order of events starts with luminal accumulation of HMGB; which then (I) recruits and activates monocytes to the developing thrombus – promoting the oxidation to disulfide HMGB1 - which in turn provide TF thereby activating the extrinsic pathway of coagulation, and proinflammatory mediators li…”
BackgroundMethodInfluentialSelf-citationThe HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis
Huebener, P., Pradère, J., Hernandez, C., Gwak, G., Caviglia, J. M., Mu, X., Loike, J. D., Jenkins, R. E., Antoine, D. J., & Schwabe, R. F. (2019) · Journal of Clinical Investigation · doi:10.1172/jci126975 · Cited by 301 · see citing works
Self-citationMany 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 295 · see citing works
“The different redox states of HMGB1 could be analyzed by liquid chromatography tandem mass spectrometric analysis and by electrophoretic mobility of HMGB1 in the presence and in the absence of dithiothreitol.(4) It has also been shown that the redox state of extracellular HMGB1 critically regulates the autophagic resp…”
BackgroundHMGB1 as a therapeutic target in disease
Xue, J., Suarez, J. S., Minaai, M., Li, S., Gaudino, G., Pass, H. I., Carbone, M., & Yang, H. (2020) · Journal of Cellular Physiology · doi:10.1002/jcp.30125 · Cited by 297 · see citing works
“When these three cysteines are replaced with nonoxidizable, polarity‐similar serine residues (HMGB1‐3s), the resulting HMGB1 loses cytokine‐stimulating activity, but becomes more effective in recruiting leukocytes (Venereau et al., 2012).”
BackgroundMethodSelf-citationExtracellular HMGB1 as a therapeutic target in inflammatory diseases
Andersson, U., Yang, H., & Harris, H. E. (2018) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2018.1439924 · Cited by 287 · see citing works
Self-citationLi, 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 291 · see citing works
“These results suggest that N6F11 activates the UbcH5b-TRIM25-GPX4 ubiquitination cascade.”
BackgroundSelf-citationNeuroinflammation after surgery: from mechanisms to therapeutic targets
Yang, T., Velagapudi, R., & Terrando, N. (2020) · Nature Immunology · doi:10.1038/s41590-020-00812-1 · Cited by 277 · see citing works
van Vliet, E. A., Aronica, E., Vezzani, A., & Ravizza, T. (2017) · Neuropathology and Applied Neurobiology · doi:10.1111/nan.12444 · Cited by 260 · see citing works
Oxidative stress-mediated HMGB1 biology
Yan, Y. Q., Tang, D., & Kang, R. (2015) · Frontiers in Physiology · doi:10.3389/fphys.2015.00093 · Cited by 262 · see citing works
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 256 · see citing works
Physiological Signaling Functions of Reactive Oxygen Species in Stem Cells: From Flies to Man
Sinenko, S. A., Starkova, T. Y., Kuzmin, A. A., & Tomilin, A. N. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.714370 · Cited by 256 · see citing works
HMGB1 as biomarker and drug target
Vénéreau, E., Leo, F. D., Mezzapelle, R., Careccia, G., Musco, G., & Bianchi, M. E. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.06.031 · Cited by 240 · see citing works
Self-citationFrank, 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 · see citing works
“These effects of dsHMGB1 and frHMGB1 are consistent with observations that dsHMGB1 is pro-inflammatory, whereas frHMGB1 is chemotactic and not pro-inflammatory (Venereau et al., 2012).”
Mechanisms of neuroimmune gene induction in alcoholism
Crews, F. T., & Vetreno, R. P. (2016) · Psychopharmacology · doi:10.1007/s00213-015-3906-1 · Cited by 232 · see citing works
“2014) and also dimerizes with proinflammatory molecules (Tang et al. 2012; Venereau et al. 2012), such as IL-1β (Wahamaa et al.”
BackgroundNeutrophil extracellular trap induced by HMGB1 exacerbates damages in the ischemic brain
Kim, S.-W., Lee, H., Lee, H., Kim, I., & Lee, J.-K. (2019) · Acta Neuropathologica Communications · doi:10.1186/s40478-019-0747-x · Cited by 237 · see citing works
Mihm, S. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19103104 · Cited by 232 · see citing works
“Full oxidation of HMGB1 abrogates its chemokine and cytokine activities and associates with resolution of inflammation [23,25].”
BackgroundThe oxysterol–CXCR2 axis plays a key role in the recruitment of tumor-promoting neutrophils
Raccosta, L., Fontana, R., Maggioni, D., Lanterna, C., Villablanca, E. J., Paniccia, A., Musumeci, A. G., Chiricozzi, E., Trincavelli, M. L., Daniele, S., et al. (2013) · The Journal of Experimental Medicine · doi:10.1084/jem.20130440 · Cited by 230 · see citing works
“Recently, different mo lecular mechanisms able to modify protein structure within tumors (Nagaraj et al., 2007; Molon et al., 2011) or in dam aged tissues (Venereau et al., 2012) have been reported.”
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 228 · see citing works
Self-citationTargeting oxidative stress improves disease outcomes in a rat model of acquired epilepsy
Pauletti, A., Terrone, G., Shekh‐Ahmad, T., Salamone, A., Ravizza, T., Rizzi, M., Pastore, A., Pascente, R., Liang, L., Villa, B. R., et al. (2019) · Brain · doi:10.1093/brain/awz130 · Cited by 226 · see citing works
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 225 · see citing works
“at-HMGB1 also binds to RAGE to increase CXCL12 secretion [143, 144].”
BackgroundInfluentialDanger Signals and Inflammasomes: Stress-Evoked Sterile Inflammation in Mood Disorders
Fleshner, M., Frank, M., & Maier, S. F. (2017) · Neuropsychopharmacology · doi:10.1038/npp.2016.125 · Cited by 216 · see citing works
Weber, M. D., Frank, M. G., Tracey, K. J., Watkins, L. R., & Maier, S. F. (2015) · The Journal of Neuroscience · doi:10.1523/jneurosci.3561-14.2015 · Cited by 215 · see citing works
“Oxidation at all three cysteines abrogates both the chemotactic and proinflammatory properties of HMGB-1 (oxidized HMGB-1; Venereau et al., 2012).”
Self-citationDamage-associated molecular patterns in trauma
Relja, B., & Land, W. G. (2019) · European Journal of Trauma and Emergency Surgery · doi:10.1007/s00068-019-01235-w · Cited by 218 · see citing works
“Interestingly, while a reduction in cysteine residues makes HMGB1 rather a chemoattractant than a cytokine inducer, oxidization of the cysteine residues via reactive oxygen species abrogates both activities of HMGB1 [101].”
BackgroundHMGB1 and leukocyte migration during trauma and sterile inflammation
Vénéreau, E., Schiraldi, M., Uguccioni, M., & Bianchi, M. E. (2012) · Molecular Immunology · doi:10.1016/j.molimm.2012.10.037 · Cited by 213 · see citing works
“1, glycyrrhizin and Box A neutralize the hemoattractant activity of HMGB1 without interfering with the ytokine-inducing activity (Venereau et al., 2012, and unpubished results).”
BackgroundMethodInfluentialSelf-citationIntracellular Hmgb1 Inhibits Inflammatory Nucleosome Release and Limits Acute Pancreatitis in Mice
Kang, R., Zhang, Q., Hou, W., Yan, Z., Chen, R., Bonaroti, J. W., Bansal, P., Billiar, T. R., Tsung, A., Wang, Q., et al. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.12.015 · Cited by 212 · see citing works
Self-citationRedox Regulation of Inflammation: Old Elements, a New Story
Lei, Y., Wang, K., Deng, L., Chen, Y., Nice, E. C., & Huang, C. (2014) · Medicinal Research Reviews · doi:10.1002/med.21330 · Cited by 208 · see citing works
Retracted: Targeting oxidative stress improves disease outcomes in a rat model of acquired epilepsy
Pauletti, A., Terrone, G., Shekh‐Ahmad, T., Salamone, A., Ravizza, T., Rizzi, M., Pastore, A., Pascente, R., Liang, L.-P., Villa, B. R., et al. (2017) · Brain · doi:10.1093/brain/awx117 · Cited by 206 · see citing works
Self-citationRetractedWorkenhe, S. T., & Mossman, K. L. (2013) · Molecular Therapy · doi:10.1038/mt.2013.220 · Cited by 203 · see citing works
Inflammation balance in skeletal muscle damage and repair
Tu, H., & Li, Y. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1133355 · Cited by 212 · see citing works
Immunogenic Cell Death and Immunotherapy of Multiple Myeloma
del Valle, A. S., Anel, A., Naval, J., & Marzo, I. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00050 · Cited by 196 · see citing works
Redox Control of Skeletal Muscle Regeneration
Moal, E. L., Pialoux, V., Juban, G., Groussard, C., Zouhal, H., Chazaud, B., & Mounier, R. (2016) · Antioxidants and Redox Signaling · doi:10.1089/ars.2016.6782 · Cited by 197 · see citing works
“When cysteine residues are oxidized, HGMB1 promotes the release of proinflammatory cytokines (339).”
Cell death, clearance and immunity in the skeletal muscle
Sciorati, C., Rigamonti, E., Manfredi, A., & Rovere-Querini, P. (2016) · Cell Death and Differentiation · doi:10.1038/cdd.2015.171 · Cited by 183 · see citing works
Cicco, S., Cicco, G., Racanelli, V., & Vacca, A. (2020) · Mediators of Inflammation · doi:10.1155/2020/7527953 · Cited by 190 · see citing works
“[72, 74, 75] and its function in inflammation and sepsis.”
BackgroundHigh‐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 · see citing works
DAMPs activating innate and adaptive immune responses in COPD
Pouwels, S. D., Heijink, I. H., ten Hacken, N. H. T., Vandenabeele, P., Krysko, D. V., Nawijn, M. C., & van Oosterhout, A. J. M. (2013) · Mucosal Immunology · doi:10.1038/mi.2013.77 · Cited by 187 · see citing works
“When the three cysteine residues (C23, C45, and C106) of HMGB1 are all in a reduced form, HMGB1 has chemotactic but no immunostimulatory properties, whereas HMGB1 has no chemotactic or immunostimulatory activities at all when all three cysteine residues are present in their oxidized form.(95) Finally, when C106 is red…”
BackgroundYanai, H., Matsuda, A., An, J., Koshiba, R., Nishio, J., Negishi, H., Ikushima, H., Onoe, T., Ohdan, H., Yoshida, N., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1320808110 · Cited by 181 · see citing works
Cell Death and DAMPs in Acute Pancreatitis
Kang, R., Lotze, M. T., Zeh, H. J., Billiar, T. R., & Tang, D. (2014) · Molecular Medicine · doi:10.2119/molmed.2014.00117 · Cited by 178 · see citing works
Agalave, N. M., Larsson, M., Abdelmoaty, S., Su, J., Baharpoor, A., Lundbäck, P., Palmblad, K., Andersson, U., Harris, H. E., & Svensson, C. I. (2014) · Pain · doi:10.1016/j.pain.2014.06.007 · Cited by 179 · see citing works
“Indeed, it has been shown in models of hepatic inflammation and muscle injury that released HMGB1 may change its redox state from a reduced to first a partially and then a fully oxidized form [43,45].”
BackgroundMethodInfluentialSelf-citationHubert, P., Roncarati, P., Demoulin, S., Pilard, C., Ancion, M., Reynders, C., Lerho, T., Bruyère, D., Lebeau, A., Radermecker, C., et al. (2021) · Journal for ImmunoTherapy of Cancer · doi:10.1136/jitc-2020-001966 · Cited by 186 · see citing works
“11–14 As a result, three redox forms of HMGB1 have been described: reduced, disulfide (Cys-23 and Cys-45 forming an intramolecular bond) and oxidized HMGB1.”
How is inflammation initiated? Individual influences of IL-1, IL-18 and HMGB1
Keyel, P. A. (2014) · Cytokine · doi:10.1016/j.cyto.2014.03.007 · Cited by 175 · see citing works
NETosis in Alzheimer’s Disease
Pietronigro, E. C., Bianca, V. D., Zenaro, E., & Constantin, G. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00211 · Cited by 176 · see citing works
“HMGB1 is a damage-associated molecular pattern (DAMP) released during apoptosis and is involved in leukocyte recruitment and local activation (86).”
BackgroundPaudel, Y. N., Angelopoulou, E., Piperi, C., Balasubramaniam, V. R. M. T., Othman, I., & Shaikh, M. F. (2019) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2019.172487 · Cited by 178 · see citing works
Innate Immune Regulations and Liver Ischemia-Reperfusion Injury
Lü, L., Zhou, H., Ni, M., Wang, X., Busuttil, R. W., Kupiec‐Weglinski, J. W., & Zhai, Y. (2016) · Transplantation · doi:10.1097/tp.0000000000001411 · Cited by 173 · see citing works
Divergent Roles of Inflammation in Skeletal Muscle Recovery From Injury
Howard, E. E., Pasiakos, S. M., Blesso, C. N., Fussell, M. A., & Rodriguez, N. R. (2020) · Frontiers in Physiology · doi:10.3389/fphys.2020.00087 · Cited by 176 · see citing works
“Secretion of the chemoattractants CXC-chemokine ligand 1 (CXCL1) and CC-chemokine ligand 2 (CCL2) as well as damage-associated molecular patterns (DAMPs) such as high-mobility group box 1 protein (HMGB1) from muscle-resident macrophages also facilitates immune cell activation and infiltration following injury (Brigitt…”
BackgroundHMGB1: The Central Cytokine for All Lymphoid Cells
Li, G., Liang, X., & Lotze, M. T. (2013) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00068 · Cited by 167 · see citing works
“…promotes TNF/IL6 production (cytokine activity), it is quite likely that the molecule secreted by activated cells, endowed with autocrine and paracrine actions, differs biochemically and functionally from the molecule released as a consequence of cell and tissue necrosis (Venereau et al., 2012).”
BackgroundDaiber, A., & Chłopicki, S. (2020) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2020.02.026 · Cited by 169 · see citing works
Redox Modulation of HMGB1-Related Signaling
Janko, C., Filipović, M. R., Munoz, L. E., Schorn, C., Schett, G. A., Ivanović‐Burmazović, I., & i, M. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5179 · Cited by 167 · see citing works
“Recently, Venereau et al. confirmed the findings by Yang et al. and additionally described the influence of redox mod-ifications on the chemotactic activity (86).”
Kim, S., Kim, S. Y., Pribis, J. P., Lotze, M. T., Mollen, K. P., Shapiro, R. A., Loughran, P., Scott, M. J., & Billiar, T. R. (2013) · Molecular Medicine · doi:10.2119/molmed.2012.00306 · Cited by 164 · see citing works
“If all of these cysteines are in the thiol state, HMGB1 stimulates the production of and interacts directly with CXCL12 to activate the chemokine receptor CXCR4 (15).”
BackgroundPotential protective mechanisms of green tea polyphenol EGCG against COVID-19
Zhang, Z., Zhang, X., Bi, K., He, Y., Yan, W., Yang, C. S., & Zhang, J. (2021) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2021.05.023 · Cited by 171 · see citing works
Balosso, S., Liu, J., Bianchi, M. E., & Vezzani, A. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2013.5349 · Cited by 161 · see citing works
“Recent evidence demonstrates that the redox state of HMGB1 is pivotal for determining which receptor is activated and its functional effects (55, 61, 69).”
InfluentialSelf-citationRegulation of HMGB1 release by inflammasomes
Lü, B., Wang, H., Andersson, U., & Tracey, K. J. (2013) · Protein & Cell · doi:10.1007/s13238-012-2118-2 · Cited by 160 · see citing works
Self-citationPrognostic and predictive value of DAMPs and DAMP-associated processes in cancer
Fucikova, J., Moserova, I., Urbanova, L., Bezu, L., Kepp, O., Cremer, I., Salek, C., Strnad, P., Kroemer, G., Galluzzi, L., et al. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00402 · Cited by 159 · see citing works
“Indeed, while reduced HMGB1 efficiently dimerizes with CXCL12 and mediate potent chemotactic functions upon binding to chemokine (C–X–C motif) receptor 4 (CXCR4) (164, 165), its oxidized counterpart fails to do so (162).”
Background
- Authors
- Venereau, E., Casalgrandi, M., Schiraldi, M., Antoine, D. J., Cattaneo, A., De Marchis, F., Liu, J., Antonelli, A., Preti, A., Raeli, L., Shams, S. S., Yang, H., Varani, L., Andersson, U., Tracey, K. J., Bachi, A., Uguccioni, M., & Bianchi, M. E.
- Affiliations
- Division of Genetics and Cell Biology, San Raffaele Scientific Institute, 20132 Milan, Italy 1
- HMGBiotech Srl, 20133 Milan, Italy 2
- Institute for Research in Biomedicine (CH)
- University of Liverpool (GB)
- IRCCS Ospedale San Raffaele (IT)
- Vita-Salute San Raffaele University (IT)
- Feinstein Institute for Medical Research (US)
- Karolinska University Hospital (SE)
- Corresponding author
- Bianchi, Marco E.
- ORCID
- Venue
- Journal of Experimental Medicine
- Publisher
- Rockefeller University Press
- Published
- 2012-08-06
- Volume
- 209
- Issue
- 9
- Pages
- 1519-1528
- ISSN
- 0022-1007 (ISSN-L)
- 1540-9538
- PMC
- PMC3428943
- OpenAlex
- W2141438911
- Semantic Scholar
- 17d0978fd742005f41f9a10b50083eec9ce6ff3d
- Cited by
- 720
- References
- 29
- Citations by year
- 2026: 48 · 2025: 38 · 2024: 54 · 2023: 46 · 2022: 38 · 2021: 44 · 2020: 56 · 2019: 40 · 2018: 60 · 2017: 58 · 2016: 52 · 2015: 64 · 2014: 66 · 2013: 46 · 2012: 10
- FWCI
- 38.20
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- The Journal of Experimental Medicine (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-sa)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- reroDoc Digital Library (submittedVersion)
- Funders
- European Commission (281608, 280873)
- National Institute of General Medical Sciences (R01GM062508)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Clinical Biochemistry › Advanced Glycation End Products research
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Keywords
- HMGB1, high mobility group box 1, redox regulation, cysteine oxidation, disulfide bonds, leukocyte recruitment, sterile inflammation, tissue damage, muscle damage, reactive oxygen species, chemoattractants, leukocyte activation
- MeSH terms
- Animals, Antibodies, Monoclonal, Cell Movement, Chemotactic Factors, Cysteine, Disulfides, Inflammation, Leukocytes, Male, Mice, Inbred C57BL, Mutation, Recombinant Proteins, Cytokines, Reactive Oxygen Species, Muscle, Skeletal, HMGB1 Protein, Mice, Rats
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