Molecular mechanism and therapeutic modulation of high mobility group box 1 release and action: an updated review

References

• Andersson U, Tracey KJ. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu Rev Immunol 2011;29:139-62
   PubMed Web of Science ®Google Scholar
• Yanai H, Matsuda A, An J, et al. Conditional ablation of HMGB1 in mice reveals its protective function against endotoxemia and bacterial infection. Proc Natl Acad Sci USA 2013;110:20699-704
   PubMed Web of Science ®Google Scholar
• Huang H, Nace GW, McDonald KA, et al. Hepatocyte specific HMGB1 deletion worsens the injury in liver ischemia/reperfusion: a role for intracellular HMGB1 in cellular protection. Hepatology 2014; In press
   Google Scholar
• Kang R, Zhang Q, Hou W, et al. Intracellular Hmgb1 inhibits inflammatory nucleosome release and limits acute pancreatitis in mice. Gastroenterology 2014; 46:1097-107
   Google Scholar
• Wang H, Bloom O, Zhang M, et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science 1999;285:248-51
   PubMed Web of Science ®Google Scholar
• Ivanov S, Dragoi AM, Wang X, et al. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood 2007;110:1970-81
   PubMed Web of Science ®Google Scholar
• Rendon-Mitchell B, Ochani M, Li J, et al. IFN-gamma Induces High Mobility Group Box 1 Protein Release Partly Through a TNF-Dependent Mechanism. J Immunol 2003;170:3890-7
   PubMed Web of Science ®Google Scholar
• Kim JH, Kim SJ, Lee IS, et al. Bacterial endotoxin induces the release of high mobility group box 1 via the IFN-beta signaling pathway. J Immunol 2009;182:2458-66
   PubMedGoogle Scholar
• Lu B, Antoine DJ, Kwan K, et al. JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation. Proc Natl Acad Sci USA 2014; 111:3068-73
   Google Scholar
• Hao N, Budnik BA, Gunawardena J, et al. Tunable signal processing through modular control of transcription factor translocation. Science 2013;339:460-4
   PubMedGoogle Scholar
• Bonaldi T, Talamo F, Scaffidi P, et al. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J 2003;22:5551-60
   PubMed Web of Science ®Google Scholar
• Gardella S, Andrei C, Ferrera D, et al. The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep 2002;3:955-1001
   Google Scholar
• Evankovich J, Cho SW, Zhang R, et al. High mobility group box 1 release from hepatocytes during ischemia and reperfusion injury is mediated by decreased histone deacetylase activity. J Biol Chem 2010;285:39888-97
   PubMed Web of Science ®Google Scholar
• Kang R, Livesey KM, Zeh HJ, et al. HMGB1: a novel Beclin 1-binding protein active in autophagy. Autophagy 2010;6:1209-11
   PubMed Web of Science ®Google Scholar
• O’Shea JJ, Plenge R. JAK and STAT signaling molecules in immunoregulation and immune-mediated disease. Immunity 2012;36:542-50
   PubMed Web of Science ®Google Scholar
• Yanai H, Ban T, Wang Z, et al. HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses. Nature 2009;462:99-103
   PubMed Web of Science ®Google Scholar
• Youn JH, Shin JS. Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation that redirects it toward secretion. J Immunol 2006;177:7889-97
   PubMed Web of Science ®Google Scholar
• Zhang X, Wheeler D, Tang Y, et al. Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages. J Immunol 2008;181:5015-23
   Google Scholar
• Ito I, Fukazawa J, Yoshida M. Post-translational methylation of high mobility group box 1 (HMGB1) causes its cytoplasmic localization in neutrophils. J Biol Chem 2007;282:16336-44
   PubMed Web of Science ®Google Scholar
• Qin S, Wang H, Yuan R, et al. Role of HMGB1 in apoptosis-mediated sepsis lethality. J Exp Med 2006;203:1637-42
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Sarkar A, Vande WL, et al. Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia. J Immunol 2010;185:4385-92
   PubMed Web of Science ®Google Scholar
• Strowig T, Henao-Mejia J, Elinav E, et al. Inflammasomes in health and disease. Nature 2012;481:278-86
   PubMed Web of Science ®Google Scholar
• Kayagaki N, Warming S, Lamkanfi M, et al. Non-canonical inflammasome activation targets caspase-11. Nature 2011;479:117-21
   PubMed Web of Science ®Google Scholar
• Kayagaki N, Wong MT, Stowe IB, et al. Noncanonical inflammasome activation by intracellular LPS independent of TLR4. Science 2013;341:1246-9
   PubMed Web of Science ®Google Scholar
• Lu B, Nakamura T, Inouye K, et al. Novel role of PKR in inflammasome activation and HMGB1 release. Nature 2012;488:670-4
   PubMed Web of Science ®Google Scholar
• Li W, Li J, Sama AE, et al. Carbenoxolone Blocks Endotoxin-Induced Protein Kinase R (PKR) Activation and High Mobility Group Box 1 (HMGB1) Release. Mol Med 2013;19:203-11
   Google Scholar
• Hett EC, Slater LH, Mark KG, et al. Chemical genetics reveals a kinase-independent role for protein kinase R in pyroptosis. Nat Chem Biol 2013;9:398-405
   Google Scholar
• Keller M, Ruegg A, Werner S, et al. Active caspase-1 is a regulator of unconventional protein secretion. Cell 2008;132:818-31
   PubMed Web of Science ®Google Scholar
• Scaffidi P, Misteli T, Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 2002;418:191-5
   PubMed Web of Science ®Google Scholar
• Tsung A, Sahai R, Tanaka H, et al. The nuclear factor HMGB1 mediates hepatic injury after murine liver ischemia-reperfusion. J Exp Med 2005;201:1135-43
   PubMed Web of Science ®Google Scholar
• Andrassy M, Volz HC, Igwe JC, et al. High-mobility group box-1 in ischemia-reperfusion injury of the heart. Circulation 2008;117:3216-26
   PubMed Web of Science ®Google Scholar
• Cohen MJ, Brohi K, Calfee CS, et al. Early release of high mobility group box nuclear protein 1 after severe trauma in humans: role of injury severity and tissue hypoperfusion. Crit Care 2009;13:R174
   PubMedGoogle Scholar
• Peltz ED, Moore EE, Eckels PC, et al. HMGB1 is markedly elevated within 6 hours of mechanical trauma in humans. Shock 2009;32:17-22
   PubMed Web of Science ®Google Scholar
• Zhou RR, Liu HB, Peng JP, et al. High mobility group box chromosomal protein 1 in acute-on-chronic liver failure patients and mice with ConA-induced acute liver injury. Exp Mol Pathol 2012;93:213-19
   Google Scholar
• Antoine DJ, Dear JW, Lewis PS, et al. Mechanistic biomarkers provide early and sensitive detection of acetaminophen-induced acute liver injury at first presentation to hospital. Hepatology 2013;58:777-87
   PubMed Web of Science ®Google Scholar
• Seo YS, Kwon JH, Yaqoob U, et al. HMGB1 recruits hepatic stellate cells and liver endothelial cells to sites of ethanol induced parenchymal cell injury. Am J Physiol Gastrointest Liver Physiol 2013;305(11):G838-48
   Google Scholar
• Zhu S, Li W, Ward MF, et al. High mobility group box 1 protein as a potential drug target for infection- and injury-elicited inflammation. Inflamm Allergy Drug Targets 2010;9:60-72
   Google Scholar
• Vincent JL, Opal SM, Marshall JC, et al. Sepsis definitions: time for change. Lancet 2013;381:774-5
   PubMed Web of Science ®Google Scholar
• Cho YS, Challa S, Moquin D, et al. Phosphorylation-driven assembly of the RIP1-RIP3 complex regulates programmed necrosis and virus-induced inflammation. Cell 2009;137:1112-23
   PubMed Web of Science ®Google Scholar
• Thapa RJ, Nogusa S, Chen P, et al. Interferon-induced RIP1/RIP3-mediated necrosis requires PKR and is licensed by FADD and caspases. Proc Natl Acad Sci USA 2013;110:E3109-18
   PubMed Web of Science ®Google Scholar
• Chen LC, Yeh TM, Wu HN, et al. Dengue virus infection induces passive release of high mobility group box 1 protein by epithelial cells. J Infect 2008;56:143-50
   Google Scholar
• Alleva LM, Budd AC, Clark IA. Systemic release of high mobility group box 1 protein during severe murine influenza. J Immunol 2008;181:1454-9
   PubMed Web of Science ®Google Scholar
• Whilding LM, Archibald KM, Kulbe H, et al. Vaccinia Virus Induces Programmed Necrosis in Ovarian Cancer Cells. Mol Ther 2013;21(11):2074-86
   PubMed Web of Science ®Google Scholar
• Wang H, Ward MF, Fan XG, et al. Potential role of high mobility group box 1 in viral infectious diseases. Viral Immunol 2006;19:3-9
   Google Scholar
• Gunther C, Martini E, Wittkopf N, et al. Caspase-8 regulates TNF-alpha-induced epithelial necroptosis and terminal ileitis. Nature 2011;477:335-9
   PubMed Web of Science ®Google Scholar
• Zhang Q, Raoof M, Chen Y, et al. Circulating mitochondrial DAMPs cause inflammatory responses to injury. Nature 2010;464:104-7
   PubMed Web of Science ®Google Scholar
• Qiang X, Yang WL, Wu R, et al. Cold-inducible RNA-binding protein (CIRP) triggers inflammatory responses in hemorrhagic shock and sepsis. Nat Med 2013;19:1489-95
   PubMed Web of Science ®Google Scholar
• Tian J, Avalos AM, Mao SY, et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol 2007;8:487-96
   PubMed Web of Science ®Google Scholar
• Yang D, Chen Q, Yang H, et al. High mobility group box-1 protein induces the migration and activation of human dendritic cells and acts as an alarmin. J Leukoc Biol 2007;81:59-66
   PubMed Web of Science ®Google Scholar
• Dumitriu IE, Bianchi ME, Bacci M, et al. The secretion of HMGB1 is required for the migration of maturing dendritic cells. J Leukoc Biol 2007;81:84-91
   PubMed Web of Science ®Google Scholar
• Orlova VV, Choi EY, Xie C, et al. A novel pathway of HMGB1-mediated inflammatory cell recruitment that requires Mac-1-integrin. EMBO J 2007;26:1129-39
   PubMed Web of Science ®Google Scholar
• Degryse B, Bonaldi T, Scaffidi P, et al. The high mobility group (HMG) boxes of the nuclear protein HMG1 induce chemotaxis and cytoskeleton reorganization in rat smooth muscle cells. J Cell Biol 2001;152:1197-206
   PubMed Web of Science ®Google Scholar
• Yu M, Wang H, Ding A, et al. HMGB1 signals through toll-Like receptor (TLR) 4 AND TLR2. Shock 2006;26:174-9
   PubMed Web of Science ®Google Scholar
• Chen GY, Tang J, Zheng P, et al. CD24 and Siglec-10 selectively repress tissue damage-induced immune responses. Science 2009;323:1722-5
   PubMed Web of Science ®Google Scholar
• Abeyama K, Stern DM, Ito Y, et al. The N-terminal domain of thrombomodulin sequesters high-mobility group-B1 protein, a novel antiinflammatory mechanism. J Clin Invest 2005;115:1267-74
   PubMed Web of Science ®Google Scholar
• Salmivirta M, Rauvala H, Elenius K, et al. Neurite growth-promoting protein (amphoterin, p30) binds syndecan. Exp Cell Res 1992;200:444-51
   PubMed Web of Science ®Google Scholar
• Zhu S, Ashok M, Li J, et al. Spermine protects mice against lethal sepsis partly by attenuating surrogate inflammatory markers. Mol Med 2009;15:275-82
   Google Scholar
• Fiuza C, Bustin M, Talwar S, et al. Inflammation-promoting activity of HMGB1 on human microvascular endothelial cells. Blood 2003;101:2652-60
   PubMed Web of Science ®Google Scholar
• Kazama H, Ricci JE, Herndon JM, et al. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein. Immunity 2008;29:21-32
   PubMed Web of Science ®Google Scholar
• Venereau E, Casalgrandi M, Schiraldi M, et al. Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J Exp Med 2012;209:1519-28
   PubMed Web of Science ®Google Scholar
• Liu A, Fang H, Dirsch O, et al. Oxidation of HMGB1 causes attenuation of its pro-inflammatory activity and occurs during liver ischemia and reperfusion. PLoS One 2012;7:e35379
   Google Scholar
• Antoine DJ, Harris HE, Andersson U, et al. A systematic nomenclature for the redox states of high mobility group box (HMGB) proteins. Mol Med 2014; In press
   Google Scholar
• Schiraldi M, Raucci A, Munoz LM, et al. HMGB1 promotes recruitment of inflammatory cells to damaged tissues by forming a complex with CXCL12 and signaling via CXCR4. J Exp Med 2012;209:551-63
   PubMed Web of Science ®Google Scholar
• Yang H, Lundback P, Ottosson L, et al. Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Mol Med 2012;18:250-9
   PubMed Web of Science ®Google Scholar
• Nystrom S, Antoine DJ, Lundback P, et al. TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. EMBO J 2013;32:86-99
   PubMed Web of Science ®Google Scholar
• Zhou R, Yazdi AS, Menu P, et al. A role for mitochondria in NLRP3 inflammasome activation. Nature 2011;469:221-5
   PubMed Web of Science ®Google Scholar
• Allen IC, Scull MA, Moore CB, et al. The NLRP3 inflammasome mediates in vivo innate immunity to influenza A virus through recognition of viral RNA. Immunity 2009;30:556-65
   PubMed Web of Science ®Google Scholar
• Miao EA, Leaf IA, Treuting PM, et al. Caspase-1-induced pyroptosis is an innate immune effector mechanism against intracellular bacteria. Nat Immunol 2010;11:1136-42
   PubMed Web of Science ®Google Scholar
• Wang H, Zhu S, Zhou R, et al. Therapeutic potential of HMGB1-targeting agents in sepsis. Expert Rev Mol Med 2008;10:e32
   PubMedGoogle Scholar
• Poltorak A, He X, Smirnova I, et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 1998;282:2085-8
   PubMed Web of Science ®Google Scholar
• Nagai Y, Akashi S, Nagafuku M, et al. Essential role of MD-2 in LPS responsiveness and TLR4 distribution. Nat Immunol 2002;3:667-72
   PubMed Web of Science ®Google Scholar
• Kim S, Kim SY, Pribis JP, et al. Signaling of high mobility group box 1 (HMGB1) through toll-like receptor 4 in macrophages requires CD14. Mol Med 2013;19:88-98
   PubMed Web of Science ®Google Scholar
• Hsu LC, Enzler T, Seita J, et al. IL-1beta-driven neutrophilia preserves antibacterial defense in the absence of the kinase IKKbeta. Nat Immunol 2011;12:144-50
   PubMed Web of Science ®Google Scholar
• Yang H, Ochani M, Li J, et al. Reversing established sepsis with antagonists of endogenous high-mobility group box 1. Proc Natl Acad Sci USA 2004;101:296-301
   PubMed Web of Science ®Google Scholar
• Wang H, Yang H, Czura CJ, et al. HMGB1 as a Late Mediator of Lethal Systemic Inflammation. Am J Respir Crit Care Med 2001;164:1768-73
   PubMed Web of Science ®Google Scholar
• Ye C, Choi JG, Abraham S, et al. Human macrophage and dendritic cell-specific silencing of high-mobility group protein B1 ameliorates sepsis in a humanized mouse model. Proc Natl Acad Sci USA 2012;109:21052-7
   Google Scholar
• Wu H, Ma J, Wang P, et al. HMGB1 contributes to kidney ischemia reperfusion injury. J Am Soc Nephrol 2010;21:1878-90
   PubMed Web of Science ®Google Scholar
• Qiu J, Nishimura M, Wang Y, et al. Early release of HMGB-1 from neurons after the onset of brain ischemia. J Cereb Blood Flow Metab 2008;28:927-38
   PubMed Web of Science ®Google Scholar
• Okuma Y, Liu K, Wake H, et al. Anti-high mobility group box-1 antibody therapy for traumatic brain injury. Ann Neurol 2012;72:373-84
   PubMed Web of Science ®Google Scholar
• Shimazaki J, Matsumoto N, Ogura H, et al. Systemic involvement of high-mobility group box 1 protein and therapeutic effect of anti-high-mobility group box 1 protein antibody in a rat model of crush injury. Shock 2012;37:634-8
   PubMed Web of Science ®Google Scholar
• Yang R, Zhang S, Cotoia A, et al. High mobility group B1 impairs hepatocyte regeneration in acetaminophen hepatotoxicity. BMC Gastroenterol 2012;12:45
   Google Scholar
• Nadatani Y, Watanabe T, Tanigawa T, et al. High mobility group box 1 promotes small intestinal damage induced by nonsteroidal anti-inflammatory drugs through Toll-like receptor 4. Am J Pathol 2012;181:98-110
   PubMed Web of Science ®Google Scholar
• Hirata Y, Kurobe H, Higashida M, et al. HMGB1 plays a critical role in vascular inflammation and lesion formation via toll-like receptor 9. Atherosclerosis 2013;231:227-33
   PubMed Web of Science ®Google Scholar
• Nadatani Y, Watanabe T, Tanigawa T, et al. High-mobility group box 1 inhibits gastric ulcer healing through toll-like receptor 4 and receptor for advanced glycation end products. PLoS One 2013;8:e80130
   Google Scholar
• Patel VS, Sitapara RA, Gore A, et al. High Mobility Group Box-1 mediates hyperoxia-induced impairment of Pseudomonas aeruginosa clearance and inflammatory lung injury in mice. Am J Respir Cell Mol Biol 2013;48:280-7
   PubMed Web of Science ®Google Scholar
• Harris HE, Andersson U, Pisetsky DS. HMGB1: a multifunctional alarmin driving autoimmune and inflammatory disease. Nat Rev Rheumatol 2012;8:195-202
   PubMed Web of Science ®Google Scholar
• Schaper F, Westra J, Bijl M. Recent developments on the role of high mobility group box 1 in systemic lupus erythematosus. Mol Med 2014; In press
   Google Scholar
• Yu SL, Wong CK, Tam LS. The alarmin functions of high-mobility group box-1 and IL-33 in the pathogenesis of systemic lupus erythematosus. Expert Rev Clin Immunol 2013;9:739-49
   Web of Science ®Google Scholar
• Andersson U, Harris HE. The role of HMGB1 in the pathogenesis of rheumatic disease. Biochim Biophys Acta 2010;1799:141-8
   PubMed Web of Science ®Google Scholar
• Liu G, Wang J, Park YJ, et al. High Mobility Group Protein-1 Inhibits Phagocytosis of Apoptotic Neutrophils through Binding to Phosphatidylserine. J Immunol 2008;181:4240-6
   PubMed Web of Science ®Google Scholar
• Urbonaviciute V, Furnrohr BG, Meister S, et al. Induction of inflammatory and immune responses by HMGB1-nucleosome complexes: implications for the pathogenesis of SLE. J Exp Med 2008;205:3007-18
   PubMed Web of Science ®Google Scholar
• Popovic K, Ek M, Espinosa A, et al. Increased expression of the novel proinflammatory cytokine high mobility group box chromosomal protein 1 in skin lesions of patients with lupus erythematosus. Arthritis Rheum 2005;52:3639-45
   PubMed Web of Science ®Google Scholar
• Barkauskaite V, Ek M, Popovic K, et al. Translocation of the novel cytokine HMGB1 to the cytoplasm and extracellular space coincides with the peak of clinical activity in experimentally UV-induced lesions of cutaneous lupus erythematosus. Lupus 2007;16:794-802
   Google Scholar
• Abdulahad DA, Westra J, Reefman E, et al. High mobility group box1 (HMGB1) in relation to cutaneous inflammation in systemic lupus erythematosus (SLE). Lupus 2013;22:597-606
   Google Scholar
• Bald T, Quast T, Landsberg J, et al. Ultraviolet-radiation-induced inflammation promotes angiotropism and metastasis in melanoma. Nature 2014;507:109-13
   PubMed Web of Science ®Google Scholar
• Zhang C, Li C, Jia S, et al. High mobility group box 1 inhibition alleviates lupus-like disease in BXSB mice. Scand J Immunol 2014; In press
   Google Scholar
• Kokkola R, Li J, Sundberg E, et al. Successful treatment of collagen-induced arthritis in mice and rats by targeting extracellular high mobility group box chromosomal protein 1 activity. Arthritis Rheum 2003;48:2052-8
   PubMed Web of Science ®Google Scholar
• Schierbeck H, Lundback P, Palmblad K, et al. Monoclonal anti-HMGB1 (high mobility group box chromosomal protein 1) antibody protection in two experimental arthritis models. Mol Med 2011;17:1039-44
   PubMed Web of Science ®Google Scholar
• Ostberg T, Kawane K, Nagata S, et al. Protective targeting of high mobility group box chromosomal protein 1 in a spontaneous arthritis model. Arthritis Rheum 2010;62:2963-72
   Google Scholar
• Rosas-Ballina M, Olofsson PS, Ochani M, et al. Acetylcholine-synthesizing T cells relay neural signals in a vagus nerve circuit. Science 2011;334:98-101
   PubMed Web of Science ®Google Scholar
• Borovikova LV, Ivanova S, Zhang M, et al. Vagus nerve stimulation attenuates the systemic inflammatory response to endotoxin. Nature 2000;405:458-62
   PubMed Web of Science ®Google Scholar
• Wang H, Yu M, Ochani M, et al. Nicotinic acetylcholine receptor alpha7 subunit is an essential regulator of inflammation. Nature 2000;421:384-8
   Google Scholar
• Wang H, Liao H, Ochani M, et al. Cholinergic agonists inhibit HMGB1 release and improve survival in experimental sepsis. Nat Med 2004;10:1216-21
   PubMed Web of Science ®Google Scholar
• Zhang M, Caragine T, Wang H, et al. Spermine inhibits proinflammatory cytokine synthesis in human mononuclear cells: a counterregulatory mechanism that restrains the immune response. J Exp Med 1997;185:1759-68
   PubMed Web of Science ®Google Scholar
• Zhang M, Borovikova LV, Wang H, et al. Spermine inhibition of monocyte activation and inflammation. Mol Med 1999;5:595-605
   PubMed Web of Science ®Google Scholar
• Wang H, Zhang M, Bianchi M, et al. Fetuin (alpha2-HS-glycoprotein) opsonizes cationic macrophage deactivating molecules. Proc Natl Acad Sci USA 1998;95:14429-34
   Google Scholar
• Zhang M, Wang H, Tracey KJ. Regulation of macrophage activation and inflammation by spermine: a new chapter in an old story. Crit Care Med 2000;28:N60-6
   PubMed Web of Science ®Google Scholar
• Li W, Zhu S, Li J, et al. A hepatic protein, fetuin-A, occupies a protective role in lethal systemic inflammation. PLoS One 2011;6:e16945
   PubMed Web of Science ®Google Scholar
• Wang H, Li W, Zhu S, et al. Peripheral administration of fetuin-A attenuates early cerebral ischemic injury in rats. J Cereb Blood Flow Metab 2010;30:493-504
   PubMed Web of Science ®Google Scholar
• Hagiwara S, Iwasaka H, Hasegawa A, et al. High-dose intravenous immunoglobulin G improves systemic inflammation in a rat model of CLP-induced sepsis. Intensive Care Med 2008;34:1812-19
   Google Scholar
• Hagiwara S, Iwasaka H, Matsumoto S, et al. High dose antithrombin III inhibits HMGB1 and improves endotoxin-induced acute lung injury in rats. Intensive Care Med 2008;34:361-7
   PubMed Web of Science ®Google Scholar
• Chorny A, Delgado M. Neuropeptides rescue mice from lethal sepsis by down-regulating secretion of the late-acting inflammatory mediator high mobility group box 1. Am J Pathol 2008;172:1297-307
   Google Scholar
• Chorny A, Anderson P, Gonzalez-Rey E, et al. Ghrelin Protects against Experimental Sepsis by Inhibiting High-Mobility Group Box 1 Release and by Killing Bacteria. J Immunol 2008;180:8369-77
   PubMed Web of Science ®Google Scholar
• Favreau F, Thuillier R, Cau J, et al. Anti-thrombin therapy during warm ischemia and cold preservation prevents chronic kidney graft fibrosis in a DCD model. Am J Transplant 2010;10:30-9
   Google Scholar
• Herzog C, Lorenz A, Gillmann HJ, et al. Thrombomodulin’s lectin-like domain reduces myocardial damage by interfering with HMGB1-mediated TLR2 signalling. Cardiovasc Res 2014; 101:400-10
   Google Scholar
• Jiang W, Tang W, Geng Q, et al. Inhibition of Toll-like receptor 4 with vasoactive intestinal peptide attenuates liver ischemia-reperfusion injury. Transplant Proc 2011;43:1462-7
   Google Scholar
• Zhang H, Cui Z, Luo G, et al. Ghrelin attenuates intestinal ischemia/reperfusion injury in mice by activating the mTOR signaling pathway. Int J Mol Med 2013;32:851-9
   Google Scholar
• Fann DY, Lee SY, Manzanero S, et al. Intravenous immunoglobulin suppresses NLRP1 and NLRP3 inflammasome-mediated neuronal death in ischemic stroke. Cell Death Dis 2013;4:e790
   PubMed Web of Science ®Google Scholar
• Mohri T, Tanaka H, Tajima G, et al. Synergistic effects of recombinant human soluble thrombomodulin and fluid-volume resuscitation in a rat lethal crush injury model. Shock 2006;26:581-6
   Google Scholar
• Wang XQ, Hayes MT, Kempf M, et al. Fetuin-A: a major fetal serum protein that promotes “wound closure” and scarless healing. J Invest Dermatol 2008;128:753-7
   Google Scholar
• Luo Q, Wang Y, Feng D, et al. Vasoactive intestinal peptide attenuates concanavalin A-mediated liver injury. Eur J Pharmacol 2009;607:226-33
   Google Scholar
• Imazu Y, Yanagi S, Miyoshi K, et al. Ghrelin ameliorates bleomycin-induced acute lung injury by protecting alveolar epithelial cells and suppressing lung inflammation. Eur J Pharmacol 2011;672:153-8
   PubMed Web of Science ®Google Scholar
• Yang D, Liu Z, Zhang H, et al. Ghrelin protects human pulmonary artery endothelial cells against hypoxia-induced injury via PI3-kinase/Akt. Peptides 2013;42:112-17
   PubMed Web of Science ®Google Scholar
• Jacob A, Shah KG, Wu R, et al. Ghrelin as a novel therapy for radiation combined injury. Mol Med 2010;16:137-43
   PubMed Web of Science ®Google Scholar
• Wang H, Li W, Li J, et al. The aqueous extract of a popular herbal nutrient supplement, Angelica sinensis, protects mice against lethal endotoxemia and sepsis. J Nutr 2006;136:360-5
   Google Scholar
• Zhu S, Li W, Li J, et al. It Is Not Just Folklore: the Aqueous Extract of Mung Bean Coat Is Protective against Sepsis. Evid Based Complement Alternat Med 2012;2012:498467
   Google Scholar
• Jun MS, Kim HS, Kim YM, et al. Ethanol extract of Prunella vulgaris var. lilacina inhibits HMGB1 release by induction of heme oxygenase-1 in LPS-activated RAW 264.7 cells and CLP-induced septic mice. Phytother Res 2012;26:605-12
   PubMed Web of Science ®Google Scholar
• Xie CH, Zhang MS, Zhou YF, et al. Chinese medicine Angelica sinensis suppresses radiation-induced expression of TNF-alpha and TGF-beta1 in mice. Oncol Rep 2006;15:1429-36
   PubMed Web of Science ®Google Scholar
• Mohd AN, Mohd YH, Long K, et al. Antioxidant and hepatoprotective effect of aqueous extract of germinated and fermented mung bean on ethanol-mediated liver damage. Biomed Res Int 2013;2013:693613
   Google Scholar
• Li W, Ashok M, Li J, et al. A major ingredient of green tea rescues mice from lethal sepsis partly by inhibiting HMGB1. PLoS One 2007;2:e1153
   PubMed Web of Science ®Google Scholar
• Li W, Li J, Ashok M, et al. A cardiovascular drug rescues mice from lethal sepsis by selectively attenuating a late-acting proinflammatory mediator, high mobility group box 1. J Immunol 2007;178:3856-64
   Google Scholar
• Wang W, Zhao F, Fang Y, et al. Glycyrrhizin protects against porcine endotoxemia through modulation of systemic inflammatory response. Crit Care 2013;17:R44
   Google Scholar
• Lee CH, Yoon SJ, Lee SM. Chlorogenic acid attenuates high mobility group box 1 (HMGB1) and enhances host defense mechanisms in murine sepsis. Mol Med 2013;18:1437-48
   Google Scholar
• Lee W, Ku SK, Kim TH, et al. Emodin-6-O-beta-D-glucoside inhibits HMGB1-induced inflammatory responses in vitro and in vivo. Food Chem Toxicol 2013;52:97-104
   PubMed Web of Science ®Google Scholar
• Yang EJ, Ku SK, Lee W, et al. Barrier protective effects of rosmarinic acid on HMGB1-induced inflammatory responses in vitro and in vivo. J Cell Physiol 2013;228:975-82
   PubMed Web of Science ®Google Scholar
• Kim TH, Ku SK, Bae JS. Anti-inflammatory activities of isorhamnetin-3-O-galactoside against HMGB1-induced inflammatory responses in both HUVECs and CLP-induced septic mice. J Cell Biochem 2013;114:336-45
   PubMed Web of Science ®Google Scholar
• Kim TH, Ku SK, Bae JS. Persicarin is anti-inflammatory mediator against HMGB1-induced inflammatory responses in HUVECs and in CLP-induced sepsis mice. J Cell Physiol 2013;228:696-703
   Google Scholar
• Jiang WL, Yong X, Zhang SP, et al. Forsythoside B protects against experimental sepsis by modulating inflammatory factors. Phytother Res 2012;26:981-7
   PubMed Web of Science ®Google Scholar
• Yang M, Cao L, Xie M, et al. Chloroquine inhibits HMGB1 inflammatory signaling and protects mice from lethal sepsis. Biochem Pharmacol 2013;86(3):410-18
   PubMed Web of Science ®Google Scholar
• Seo ES, Oh BK, Pak JH, et al. Acteoside improves survival in cecal ligation and puncture-induced septic mice via blocking of high mobility group box 1 release. Mol Cells 2013;35:348-54
   Google Scholar
• Li W, Zhu S, Li J, et al. EGCG stimulates autophagy and reduces cytoplasmic HMGB1 levels in endotoxin-stimulated macrophages. Biochem Pharmacol 2011;81:1152-63
   PubMed Web of Science ®Google Scholar
• Thorburn J, Horita H, Redzic J, et al. Autophagy regulates selective HMGB1 release in tumor cells that are destined to die. Cell Death Differ 2009;16:175-83
   PubMed Web of Science ®Google Scholar
• Tang D, Kang R, Livesey KM, et al. Endogenous HMGB1 regulates autophagy. J Cell Biol 2010;190:881-92
   PubMed Web of Science ®Google Scholar
• Tang D, Kang R, Cheh CW, et al. HMGB1 release and redox regulates autophagy and apoptosis in cancer cells. Oncogene 2010;29:5299-310
   PubMed Web of Science ®Google Scholar
• Huebener P, Gwak GY, Pradere JP, et al. High-mobility group box 1 is dispensable for autophagy, mitochondrial quality control, and organ function in vivo. Cell Metab 2014;19:539-47
   Google Scholar
• Zhang Y, Li W, Zhu S, et al. Tanshinone IIA sodium sulfonate facilitates endocytic HMGB1 uptake. Biochem Pharmacol 2012;84:1492-500
   Google Scholar
• Zhao L, Li W, Zhu S, et al. Green tea catechins quench the fluorescence of bacteria-conjugated Alexa fluor dyes. Inflamm Allergy Drug Targets 2013;12:308-14
   Google Scholar
• Wang JG, Bondy SC, Zhou L, et al. protective effect of tanshinone IIA against infarct size and increased HMGB1, NFkappaB, GFAP and apoptosis consequent to transient middle cerebral artery occlusion. Neurochem Res 2014;39:295-304
   Google Scholar
• Giakoustidis AE, Giakoustidis DE, Iliadis S, et al. Attenuation of intestinal ischemia/reperfusion induced liver and lung injury by intraperitoneal administration of (-)-epigallocatechin-3-gallate. Free Radic Res 2006;40:103-10
   PubMed Web of Science ®Google Scholar
• Tamura K, Alessandri B, Heimann A, et al. The effect of a gap-junction blocker, carbenoxolone, on ischemic brain injury and cortical spreading depression. Neuroscience 2011;194:262-71
   Google Scholar
• Zhai CL, Zhang MQ, Zhang Y, et al. Glycyrrhizin protects rat heart against ischemia-reperfusion injury through blockade of HMGB1-dependent phospho-JNK/Bax pathway. Acta Pharmacol Sin 2012;33:1477-87
   PubMed Web of Science ®Google Scholar
• Ogiku M, Kono H, Hara M, et al. Glycyrrhizin prevents liver injury by inhibition of high-mobility group box 1 production by Kupffer cells after ischemia-reperfusion in rats. J Pharmacol Exp Ther 2011;339:93-8
   PubMed Web of Science ®Google Scholar
• Fang H, Liu A, Dahmen U, et al. Dual role of chloroquine in liver ischemia reperfusion injury: reduction of liver damage in early phase, but aggravation in late phase. Cell Death Dis 2013;4:e694
   PubMed Web of Science ®Google Scholar
• Yun N, Kang JW, Lee SM. Protective effects of chlorogenic acid against ischemia/reperfusion injury in rat liver: molecular evidence of its antioxidant and anti-inflammatory properties. J Nutr Biochem 2012;23:1249-55
   PubMed Web of Science ®Google Scholar
• Jiang WL, Tian JW, Fu FH, et al. Neuroprotective efficacy and therapeutic window of Forsythoside B: in a rat model of cerebral ischemia and reperfusion injury. Eur J Pharmacol 2010;640:75-81
   Google Scholar
• Yin X, Yin Y, Cao FL, et al. Tanshinone IIA attenuates the inflammatory response and apoptosis after traumatic injury of the spinal cord in adult rats. PLoS One 2012;7:e38381
   PubMed Web of Science ®Google Scholar
• Hellmich HL, Rojo DR, Micci MA, et al. Pathway analysis reveals common pro-survival mechanisms of metyrapone and carbenoxolone after traumatic brain injury. PLoS One 2013;8:e53230
   Google Scholar
• Renno WM, Al Maghrebi M, Alshammari A, et al. (-)-Epigallocatechin-3-gallate (EGCG) attenuates peripheral nerve degeneration in rat sciatic nerve crush injury. Neurochem Int 2013;62:221-31
   PubMed Web of Science ®Google Scholar
• Ohnishi M, Katsuki H, Fukutomi C, et al. HMGB1 inhibitor glycyrrhizin attenuates intracerebral hemorrhage-induced injury in rats. Neuropharmacology 2011;61:975-80
   PubMed Web of Science ®Google Scholar
• Lim Y, Hedayati M, Merchant AA, et al. Chloroquine improves survival and hematopoietic recovery after lethal low-dose-rate radiation. Int J Radiat Oncol Biol Phys 2012;84:800-6
   PubMed Web of Science ®Google Scholar
• Sanchez-Campillo M, Gabaldon JA, Castillo J, et al. Rosmarinic acid, a photo-protective agent against UV and other ionizing radiations. Food Chem Toxicol 2009;7:386-92
   Google Scholar
• Lee KJ, Woo ER, Choi CY, et al. Protective effect of acteoside on carbon tetrachloride-induced hepatotoxicity. Life Sci 2004;74:1051-64
   PubMed Web of Science ®Google Scholar
• Kim DW, Cho HI, Kim KM, et al. Isorhamnetin-3-O-galactoside Protects against CCl4-Induced Hepatic Injury in Mice. Biomol Ther (Seoul) 2012;20:406-12
   PubMed Web of Science ®Google Scholar
• Wang H, Ward MF, Sama AE. Targeting HMGB1 in the treatment of sepsis. Expert Opin Ther Targets 2014; 18:257-68
   Google Scholar
• Valdes-Ferrer SI, Rosas-Ballina M, Olofsson PS, et al. High-mobility group box 1 mediates persistent splenocyte priming in sepsis survivors: evidence from a murine model. Shock 2013;40:492-5
   Google Scholar
• Sursal T, Stearns-Kurosawa DJ, Itagaki K, et al. Plasma bacterial and mitochondrial DNA distinguish bacterial sepsis from sterile systemic inflammatory response syndrome and quantify inflammatory tissue injury in nonhuman primates. Shock 2013;39:55-62
   PubMed Web of Science ®Google Scholar
• Ziegler EJ, Fisher CJ Jr, Sprung CL, et al. Treatment of gram-negative bacteremia and septic shock with HA-1A human monoclonal antibody against endotoxin. A randomized, double-blind, placebo-controlled trial. The HA-1A Sepsis Study Group. N Engl J Med 1991;324:429-36
   PubMed Web of Science ®Google Scholar
• Opal SM, Laterre PF, Francois B, et al. Effect of eritoran, an antagonist of MD2-TLR4, on mortality in patients with severe sepsis: the ACCESS randomized trial. JAMA 2013;309:1154-62
   PubMed Web of Science ®Google Scholar
• Feldmann M, Maini RN. Anti-TNF alpha therapy of rheumatoid arthritis: what have we learned? Annu Rev Immunol 2001;19:163-96
   PubMed Web of Science ®Google Scholar
• Abraham E, Wunderink R, Silverman H, et al. Efficacy and safety of monoclonal antibody to human tumor necrosis factor alpha in patients with sepsis syndrome. A randomized, controlled, double-blind, multicenter clinical trial. TNF-alpha MAb Sepsis Study Group. JAMA 1995;273:934-41
   PubMed Web of Science ®Google Scholar