High-mobility group box 1, oxidative stress, and disease.
Journal: 2011/June - Antioxidants and Redox Signaling
ISSN: 1557-7716
Abstract:
Oxidative stress and associated reactive oxygen species can modify lipids, proteins, carbohydrates, and nucleic acids, and induce the mitochondrial permeability transition, providing a signal leading to the induction of autophagy, apoptosis, and necrosis. High-mobility group box 1 (HMGB1) protein, a chromatin-binding nuclear protein and damage-associated molecular pattern molecule, is integral to oxidative stress and downstream apoptosis or survival. Accumulation of HMGB1 at sites of oxidative DNA damage can lead to repair of the DNA. As a redox-sensitive protein, HMGB1 contains three cysteines (Cys23, 45, and 106). In the setting of oxidative stress, it can form a Cys23-Cys45 disulfide bond; a role for oxidative homo- or heterodimerization through the Cys106 has been suggested for some of its biologic activities. HMGB1 causes activation of nicotinamide adenine dinucleotide phosphate oxidase and increased reactive oxygen species production in neutrophils. Reduced and oxidized HMGB1 have different roles in extracellular signaling and regulation of immune responses, mediated by signaling through the receptor for advanced glycation end products and/or Toll-like receptors. Antioxidants such as ethyl pyruvate, quercetin, green tea, N-acetylcysteine, and curcumin are protective in the setting of experimental infection/sepsis and injury including ischemia-reperfusion, partly through attenuating HMGB1 release and systemic accumulation.
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Antioxid Redox Signal 14(7): 1315-1335

High-Mobility Group Box 1, Oxidative Stress, and Disease

The DAMP Laboratory, Department of Surgery, G.27 Hillman Cancer Center, University of Pittsburgh Cancer Institute, Pittsburgh, Pennsylvania.
Corresponding author.
Address correspondence to: Dr. Daolin Tang, The DAMP Laboratory, Department of Surgery, G.21 Hillman Cancer Center, Pittsburgh, PA 15213. E-mail:ude.cmpu@2dgnat
Prof. Michael T. Lotze, The DAMP Laboratory, Department of Surgery, G.27A Hillman Cancer Center, Pittsburgh, PA 15213. E-mail:ude.cmpu@tmeztol
Address correspondence to: Dr. Daolin Tang, The DAMP Laboratory, Department of Surgery, G.21 Hillman Cancer Center, Pittsburgh, PA 15213. E-mail:ude.cmpu@2dgnatProf. Michael T. Lotze, The DAMP Laboratory, Department of Surgery, G.27A Hillman Cancer Center, Pittsburgh, PA 15213. E-mail:ude.cmpu@tmeztol
Received 2010 Jun 4; Revised 2010 Sep 20; Accepted 2010 Oct 24.

Abstract

Oxidative stress and associated reactive oxygen species can modify lipids, proteins, carbohydrates, and nucleic acids, and induce the mitochondrial permeability transition, providing a signal leading to the induction of autophagy, apoptosis, and necrosis. High-mobility group box 1 (HMGB1) protein, a chromatin-binding nuclear protein and damage-associated molecular pattern molecule, is integral to oxidative stress and downstream apoptosis or survival. Accumulation of HMGB1 at sites of oxidative DNA damage can lead to repair of the DNA. As a redox-sensitive protein, HMGB1 contains three cysteines (Cys23, 45, and 106). In the setting of oxidative stress, it can form a Cys23-Cys45 disulfide bond; a role for oxidative homo- or heterodimerization through the Cys106 has been suggested for some of its biologic activities. HMGB1 causes activation of nicotinamide adenine dinucleotide phosphate oxidase and increased reactive oxygen species production in neutrophils. Reduced and oxidized HMGB1 have different roles in extracellular signaling and regulation of immune responses, mediated by signaling through the receptor for advanced glycation end products and/or Toll-like receptors. Antioxidants such as ethyl pyruvate, quercetin, green tea, N-acetylcysteine, and curcumin are protective in the setting of experimental infection/sepsis and injury including ischemia-reperfusion, partly through attenuating HMGB1 release and systemic accumulation. Antioxid. Redox Signal. 14, 1315–1335.

Abstract

Abbreviations Used

AAamino acid
AGEadvanced glycation end product
APE1apurinic/apyrimidinic endonuclease 1/redox factor-1
ATGautophagy-related gene
CMAchaperone-mediated autophagy
CRM1chromosome region maintenance 1
Cyscysteines
Cyt ccytochrome c
DAMPdamage-associated molecular pattern molecule
DCsdendritic cells
DDSBDNA double-strand break
EGCGepigallocatechin gallate
ERendoplasmic reticulum
ERKextracellular signal-regulated kinase
HDAC1histone deacetylase-1
HMGB1high-mobility group box 1 protein
H2O2hydrogen peroxide
HSPheat shock protein
HS/Rhemorrhagic shock/resuscitation
ICAM-1intercellular adhesion molecule 1
ILinterleukin
I/Rischemia reperfusion
IRAK4interleukin-1 receptor-associated kinase 4
LAMP-2Alysosome-associated membrane protein type-2A
LDLlow-density lipoprotein
LDL-oxoxidized low-density lipoprotein
LPSlipopolysaccharide
MAPKsmitogen-activated protein kinases
MCP-1monocyte chemotactic protein-1
METCmitochondrial electron transport chain
MPTmitochondrial permeability transition
MyD88myeloid differentiation factor 88
NACN-acetylcysteine
NADPHnicotinamide adenine dinucleotide phosphate
NF-κBnuclear factor-κB
Nixnip3-like protein X
NKnatural killer
NOnitric oxide
O2•−superoxide anion
O2singlet oxygen
OHhydroxyl radical
ONOO•peroxynitrite
PAI-1plasminogen activator inhibitor 1
PKCprotein kinase C
PMNprimes circulating neutrophils
PTKstyrosine kinases
PTPsprotein tyrosine phosphatases
PUMAp53-upregulated mediator of apoptosis
RAGEreceptor for advanced glycation end products
ROSreactive oxygen species
R-SNOS-nitrosothiol
R-SOHsulphenic acid
R-S-S-Rdisulphide
-SHthiol side-chain
SMCsmooth muscle cells
SODsuperoxide dismutase
TLRToll-like receptor
TNFtumor necrosis factor
tPAtissue plasminogen activator
TREM-1triggering receptor expressed on myeloid cells-1
TRIFTIR-domain-containing adapter-inducing interferon-β
Trx1thiol-disulfide oxidoreductase thioredoxin-1
VCAM-1vascular cell adhesion molecule 1
Abbreviations Used

References

  • 1. Abd El-Gawad HM. Khalifa AE. Quercetin, coenzyme Q10, and L-canavanine as protective agents against lipid peroxidation and nitric oxide generation in endotoxin-induced shock in rat brain. Pharmacol Res. 2001;43:257–263.[PubMed]
  • 2. Abraham E. Arcaroli J. Carmody A. Wang H. Tracey KJ. HMG-1 as a mediator of acute lung inflammation. J Immunol. 2000;165:2950–2954.[PubMed]
  • 3. Agresti A. Lupo R. Bianchi ME. Muller S. HMGB1 interacts differentially with members of the Rel family of transcription factors. Biochem Biophys Res Commun. 2003;302:421–426.[PubMed]
  • 4. Andersson U. Wang H. Palmblad K. Aveberger AC. Bloom O. Erlandsson-Harris H. Janson A. Kokkola R. Zhang M. Yang H. Tracey KJ. High mobility group 1 protein (HMG-1) stimulates proinflammatory cytokine synthesis in human monocytes. J Exp Med. 2000;192:565–570.
  • 5. Andrassy M. Volz HC. Igwe JC. Funke B. Eichberger SN. Kaya Z. Buss S. Autschbach F. Pleger ST. Lukic IK. Bea F. Hardt SE. Humpert PM. Bianchi ME. Mairbaurl H. Nawroth PP. Remppis A. Katus HA. Bierhaus A. High-mobility group box-1 in ischemia-reperfusion injury of the heart. Circulation. 2008;117:3216–3226.[PubMed]
  • 6. Apel K. Hirt H. Reactive oxygen species: metabolism, oxidative stress, and signal transduction. Annu Rev Plant Biol. 2004;55:373–399.[PubMed]
  • 7. Apetoh L. Ghiringhelli F. Tesniere A. Criollo A. Ortiz C. Lidereau R. Mariette C. Chaput N. Mira JP. Delaloge S. Andre F. Tursz T. Kroemer G. Zitvogel L. The interaction between HMGB1 and TLR4 dictates the outcome of anticancer chemotherapy and radiotherapy. Immunol Rev. 2007;220:47–59.[PubMed]
  • 8. Aragones J. Fraisl P. Baes M. Carmeliet P. Oxygen sensors at the crossroad of metabolism. Cell Metab. 2009;9:11–22.[PubMed]
  • 9. Azevedo D. Tacnet F. Delaunay A. Rodrigues-Pousada C. Toledano MB. Two redox centers within Yap1 for H2O2 and thiol-reactive chemicals signaling. Free Radic Biol Med. 2003;35:889–900.[PubMed]
  • 10. Bamboat ZM. Balachandran VP. Ocuin LM. Obaid H. Plitas G. Dematteo RP. Toll-like receptor 9 inhibition confers protection from liver ischemia-reperfusion injury. Hepatology. 2010;51:621–632.
  • 11. Banerjee S. Friggeri A. Liu G. Abraham E. The C-terminal acidic tail is responsible for the inhibitory effects of HMGB1 on efferocytosis. J Leukoc Biol. 2010;88:973–979.
  • 12. Banerjee S. Kundu TK. The acidic C-terminal domain and A-box of HMGB-1 regulates p53-mediated transcription. Nucleic Acids Res. 2003;31:3236–3247.
  • 13. Barcellos-Hoff MH. Dix TA. Redox-mediated activation of latent transforming growth factor-beta 1. Mol Endocrinol. 1996;10:1077–1083.[PubMed]
  • 14. Barnham KJ. Masters CL. Bush AI. Neurodegenerative diseases and oxidative stress. Nat Rev Drug Discov. 2004;3:205–214.[PubMed]
  • 15. Bell CW. Jiang W. Reich CF., 3rd Pisetsky DS. The extracellular release of HMGB1 during apoptotic cell death. Am J Physiol Cell Physiol. 2006;291:C1318–C1325.[PubMed]
  • 16. Benz CC. Yau C. Ageing, oxidative stress and cancer: paradigms in parallax. Nat Rev Cancer. 2008;8:875–879.
  • 17. Bianchi ME. HMGB1 loves company. J Leukoc Biol. 2009;86:573–576.[PubMed]
  • 18. Bianchi ME. Manfredi AA. High-mobility group box 1 (HMGB1) protein at the crossroads between innate and adaptive immunity. Immunol Rev. 2007;220:35–46.[PubMed]
  • 19. Biswas KK. Oyama Y. Abeyama K. Hashiguchi T. Maruyama I. Uric acid induces high mobility group box1 protein release in monocytes/macrophages through P38 MAPK, ERK1/2, JNK and AP-1 activation. ASH Annu Meet Abstr. 2004;104:1464.[PubMed]
  • 20. Blankson H. Holen I. Seglen PO. Disruption of the cytokeratin cytoskeleton and inhibition of hepatocytic autophagy by okadaic acid. Exp Cell Res. 1995;218:522–530.[PubMed]
  • 21. Bonaldi T. Talamo F. Scaffidi P. Ferrera D. Porto A. Bachi A. Rubartelli A. Agresti A. Bianchi ME. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J. 2003;22:5551–5560.
  • 22. Bonomini F. Tengattini S. Fabiano A. Bianchi R. Rezzani R. Atherosclerosis and oxidative stress. Histol Histopathol. 2008;23:381–390.[PubMed]
  • 23. Brickman JM. Adam M. Ptashne M. Interactions between an HMG-1 protein and members of the Rel family. Proc Natl Acad Sci U S A. 1999;96:10679–10683.
  • 24. Brigelius-Flohe R. Banning A. Kny M. Bol GF. Redox events in interleukin-1 signaling. Arch Biochem Biophys. 2004;423:66–73.[PubMed]
  • 25. Burdon RH. Control of cell proliferation by reactive oxygen species. Biochem Soc Trans. 1996;24:1028–1032.[PubMed]
  • 26. Bustin M. Revised nomenclature for high mobility group (HMG) chromosomal proteins. Trends Biochem Sci. 2001;26:152–153.[PubMed]
  • 27. Calogero S. Grassi F. Aguzzi A. Voigtlander T. Ferrier P. Ferrari S. Bianchi ME. The lack of chromosomal protein Hmg1 does not disrupt cell growth but causes lethal hypoglycaemia in newborn mice. Nat Genet. 1999;22:276–280.[PubMed]
  • 28. Carta S. Castellani P. Delfino L. Tassi S. Vene R. Rubartelli A. DAMPs and inflammatory processes: the role of redox in the different outcomes. J Leukoc Biol. 2009;86:549–555.[PubMed]
  • 29. Case J. Ingram DA. Haneline LS. Oxidative stress impairs endothelial progenitor cell function. Antioxid Redox Signal. 2008;10:1895–1907.
  • 30. Chen GY. Tang J. Zheng P. Liu Y. CD24 and Siglec-10 selectively repress tissue damage-induced immune responses. Science. 2009;323:1722–1725.
  • 31. Chiang HL. Terlecky SR. Plant CP. Dice JF. A role for a 70-kilodalton heat shock protein in lysosomal degradation of intracellular proteins. Science. 1989;246:382–385.[PubMed]
  • 32. Choi JJ. Reich CF., 3rd Pisetsky DS. Release of DNA from dead and dying lymphocyte and monocyte cell lines in vitro. Scand J Immunol. 2004;60:159–166.[PubMed]
  • 33. Chung KY. Park JJ. Kim YS. The role of high-mobility group box-1 in renal ischemia and reperfusion injury and the effect of ethyl pyruvate. Transplant Proc. 2008;40:2136–2138.[PubMed]
  • 34. Connor KM. Subbaram S. Regan KJ. Nelson KK. Mazurkiewicz JE. Bartholomew PJ. Aplin AE. Tai YT. Aguirre-Ghiso J. Flores SC. Melendez JA. Mitochondrial H2O2 regulates the angiogenic phenotype via PTEN oxidation. J Biol Chem. 2005;280:16916–16924.[PubMed]
  • 35. Coughlan MT. Cooper ME. Forbes JM. Renal microvascular injury in diabetes: RAGE and redox signaling. Antioxid Redox Signal. 2007;9:331–342.[PubMed]
  • 36. Cowan KJ. Diamond MI. Welch WJ. Polyglutamine protein aggregation and toxicity are linked to the cellular stress response. Hum Mol Genet. 2003;12:1377–1391.[PubMed]
  • 37. Cuervo AM. Dice JF. A receptor for the selective uptake and degradation of proteins by lysosomes. Science. 1996;273:501–503.[PubMed]
  • 38. Das D. Peterson RC. Scovell WM. High mobility group B proteins facilitate strong estrogen receptor binding to classical and half-site estrogen response elements and relax binding selectivity. Mol Endocrinol. 2004;18:2616–2632.[PubMed]
  • 39. Das UN. Pyruvate is an endogenous anti-inflammatory and anti-oxidant molecule. Med Sci Monit. 2006;12:RA79–RA84.[PubMed]
  • 40. Dave SH. Tilstra JS. Matsuoka K. Li F. DeMarco RA. Beer-Stolz D. Sepulveda AR. Fink MP. Lotze MT. Plevy SE. Ethyl pyruvate decreases HMGB1 release and ameliorates murine colitis. J Leukoc Biol. 2009;86:633–643.
  • 41. Degryse B. Bonaldi T. Scaffidi P. Muller S. Resnati M. Sanvito F. Arrigoni G. Bianchi ME. 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;152:1197–1206.
  • 42. De Mori R. Straino S. Di Carlo A. Mangoni A. Pompilio G. Palumbo R. Bianchi ME. Capogrossi MC. Germani A. Multiple effects of high mobility group box protein 1 in skeletal muscle regeneration. Arterioscler Thromb Vasc Biol. 2007;27:2377–2383.[PubMed]
  • 43. Demple B. Amabile-Cuevas CF. Redox redux: the control of oxidative stress responses. Cell. 1991;67:837–839.[PubMed]
  • 44. Dias AS. Porawski M. Alonso M. Marroni N. Collado PS. Gonzalez-Gallego J. Quercetin decreases oxidative stress, NF-kappaB activation, and iNOS overexpression in liver of streptozotocin-induced diabetic rats. J Nutr. 2005;135:2299–2304.[PubMed]
  • 45. Dintilhac A. Bernues J. HMGB1 interacts with many apparently unrelated proteins by recognizing short amino acid sequences. J Biol Chem. 2002;277:7021–7028.[PubMed]
  • 46. Dong XD. Ito N. Lotze MT. Demarco RA. Popovic P. Shand SH. Watkins S. Winikoff S. Brown CK. Bartlett DL. Zeh HJ., 3rd High mobility group box I (HMGB1) release from tumor cells after treatment: implications for development of targeted chemoimmunotherapy. J Immunother. 2007;30:596–606.[PubMed]
  • 47. Dumitriu IE. Baruah P. Bianchi ME. Manfredi AA. Rovere-Querini P. Requirement of HMGB1 and RAGE for the maturation of human plasmacytoid dendritic cells. Eur J Immunol. 2005;35:2184–2190.[PubMed]
  • 48. Dumitriu IE. Bianchi ME. Bacci M. Manfredi AA. Rovere-Querini P. The secretion of HMGB1 is required for the migration of maturing dendritic cells. J Leukoc Biol. 2007;81:84–91.[PubMed]
  • 49. Ellerman JE. Brown CK. de Vera M. Zeh HJ. Billiar T. Rubartelli A. Lotze MT. Masquerader: high mobility group box-1 and cancer. Clin Cancer Res. 2007;13:2836–2848.[PubMed]
  • 50. Ellis S. Killender M. Anderson RL. Heat-induced alterations in the localization of HSP72 and HSP73 as measured by indirect immunohistochemistry and immunogold electron microscopy. J Histochem Cytochem. 2000;48:321–332.[PubMed]
  • 51. El Marzouk S. Gahattamaneni R. Joshi SR. Scovell WM. The plasticity of estrogen receptor-DNA complexes: binding affinity and specificity of estrogen receptors to estrogen response element half-sites separated by variant spacers. J Steroid Biochem Mol Biol. 2008;110:186–195.[PubMed]
  • 52. El Mezayen R. El Gazzar M. Seeds MC. McCall CE. Dreskin SC. Nicolls MR. Endogenous signals released from necrotic cells augment inflammatory responses to bacterial endotoxin. Immunol Lett. 2007;111:36–44.
  • 53. Enokido Y. Yoshitake A. Ito H. Okazawa H. Age-dependent change of HMGB1 and DNA double-strand break accumulation in mouse brain. Biochem Biophys Res Commun. 2008;376:128–133.[PubMed]
  • 54. Fages C. Nolo R. Huttunen HJ. Eskelinen E. Rauvala H. Regulation of cell migration by amphoterin. J Cell Sci. 2000;113(Pt 4):611–620.[PubMed]
  • 55. Fan J. Li Y. Levy RM. Fan JJ. Hackam DJ. Vodovotz Y. Yang H. Tracey KJ. Billiar TR. Wilson MA. Hemorrhagic shock induces NAD(P)H oxidase activation in neutrophils: role of HMGB1-TLR4 signaling. J Immunol. 2007;178:6573–6580.[PubMed]
  • 56. Fink MP. Ethyl pyruvate. Curr Opin Anaesthesiol. 2008;21:160–167.[PubMed]
  • 57. Fink MP. Ethyl pyruvate: a novel treatment for sepsis. Novartis Found Symp. 2007;280:147–156. discussion 156–164. [[PubMed]
  • 58. Finkel T. Holbrook NJ. Oxidants, oxidative stress and the biology of ageing. Nature. 2000;408:239–247.[PubMed]
  • 59. Gardella S. Andrei C. Ferrera D. Lotti LV. Torrisi MR. Bianchi ME. Rubartelli A. The nuclear protein HMGB1 is secreted by monocytes via a non-classical, vesicle-mediated secretory pathway. EMBO Rep. 2002;3:995–1001.
  • 60. Garrido C. Schmitt E. Cande C. Vahsen N. Parcellier A. Kroemer G. HSP27 and HSP70: potentially oncogenic apoptosis inhibitors. Cell Cycle. 2003;2:579–584.[PubMed]
  • 61. Germani A. Limana F. Capogrossi MC. Pivotal advances: high-mobility group box 1 protein—a cytokine with a role in cardiac repair. J Leukoc Biol. 2007;81:41–45.[PubMed]
  • 62. Goodwin GH. Johns EW. The isolation and purification of the high mobility group (HMG) nonhistone chromosomal proteins. Methods Cell Biol. 1977;16:257–267.[PubMed]
  • 63. Goula AV. Berquist BR. Wilson DM., 3rd Wheeler VC. Trottier Y. Merienne K. Stoichiometry of base excision repair proteins correlates with increased somatic CAG instability in striatum over cerebellum in Huntington's disease transgenic mice. PLoS Genet. 2009;5:e1000749.
  • 64. Gourlay CW. Carpp LN. Timpson P. Winder SJ. Ayscough KR. A role for the actin cytoskeleton in cell death and aging in yeast. J Cell Biol. 2004;164:803–809.
  • 65. Green J. Paget MS. Bacterial redox sensors. Nat Rev Microbiol. 2004;2:954–966.[PubMed]
  • 66. Griendling KK. Alexander RW. Oxidative stress and cardiovascular disease. Circulation. 1997;96:3264–3265.[PubMed]
  • 67. Grover A. Taylor J. Troudt J. Keyser A. Sommersted K. Schenkel A. Izzo AA. Mycobacterial infection induces the secretion of high-mobility group box 1 protein. Cell Microbiol. 2008;10:1390–1404.[PubMed]
  • 68. Hanspal M. Hanspal JS. The association of erythroblasts with macrophages promotes erythroid proliferation and maturation: a 30-kD heparin-binding protein is involved in this contact. Blood. 1994;84:3494–3504.[PubMed]
  • 69. Harja E. Bu DX. Hudson BI. Chang JS. Shen X. Hallam K. Kalea AZ. Lu Y. Rosario RH. Oruganti S. Nikolla Z. Belov D. Lalla E. Ramasamy R. Yan SF. Schmidt AM. Vascular and inflammatory stresses mediate atherosclerosis via RAGE and its ligands in apoE-/- mice. J Clin Invest. 2008;118:183–194.
  • 70. Harrison CA. Raftery MJ. Walsh J. Alewood P. Iismaa SE. Thliveris S. Geczy CL. Oxidation regulates the inflammatory properties of the murine S100 protein S100A8. J Biol Chem. 1999;274:8561–8569.[PubMed]
  • 71. Hartl FU. Molecular chaperones in cellular protein folding. Nature. 1996;381:571–579.[PubMed]
  • 72. Hayakawa K. Mishima K. Irie K. Hazekawa M. Mishima S. Fujioka M. Orito K. Egashira N. Katsurabayashi S. Takasaki K. Iwasaki K. Fujiwara M. Cannabidiol prevents a post-ischemic injury progressively induced by cerebral ischemia via a high-mobility group box1-inhibiting mechanism. Neuropharmacology. 2008;55:1280–1286.[PubMed]
  • 73. Hidalgo C. Donoso P. Crosstalk between calcium and redox signaling: from molecular mechanisms to health implications. Antioxid Redox Signal. 2008;10:1275–1312.[PubMed]
  • 74. Higdon JV. Frei B. Tea catechins and polyphenols: health effects, metabolism, and antioxidant functions. Crit Rev Food Sci Nutr. 2003;43:89–143.[PubMed]
  • 75. Hightower LE. Heat shock, stress proteins, chaperones, and proteotoxicity. Cell. 1991;66:191–197.[PubMed]
  • 76. Hofner P. Seprenyi G. Miczak A. Buzas K. Gyulai Z. Medzihradszky KF. Rouhiainen A. Rauvala H. Mandi Y. High mobility group box 1 protein induction by Mycobacterium bovis BCG. Mediators Inflamm. 2007;2007:53805.
  • 77. Hoppe G. Talcott KE. Bhattacharya SK. Crabb JW. Sears JE. Molecular basis for the redox control of nuclear transport of the structural chromatin protein Hmgb1. Exp Cell Res. 2006;312:3526–3538.[PubMed]
  • 78. Hu J. Dong L. Outten CE. The redox environment in the mitochondrial intermembrane space is maintained separately from the cytosol and matrix. J Biol Chem. 2008;283:29126–29134.
  • 79. Huttunen HJ. Fages C. Kuja-Panula J. Ridley AJ. Rauvala H. Receptor for advanced glycation end products-binding COOH-terminal motif of amphoterin inhibits invasive migration and metastasis. Cancer Res. 2002;62:4805–4811.[PubMed]
  • 80. Ilmakunnas M. Tukiainen EM. Rouhiainen A. Rauvala H. Arola J. Nordin A. Makisalo H. Hockerstedt K. Isoniemi H. High mobility group box 1 protein as a marker of hepatocellular injury in human liver transplantation. Liver Transpl. 2008;14:1517–1525.[PubMed]
  • 81. Ilzecka J. Serum-soluble receptor for advanced glycation end product levels in patients with amyotrophic lateral sclerosis. Acta Neurol Scand. 2009;120:119–122.[PubMed]
  • 82. Inoue K. Kawahara K. Biswas KK. Ando K. Mitsudo K. Nobuyoshi M. Maruyama I. HMGB1 expression by activated vascular smooth muscle cells in advanced human atherosclerosis plaques. Cardiovasc Pathol. 2007;16:136–143.[PubMed]
  • 83. Ito N. Demarco RA. Mailliard RB. Han J. Rabinowich H. Kalinski P. Stolz DB. Zeh HJ., 3rd Lotze MT. Cytolytic cells induce HMGB1 release from melanoma cell lines. J Leukoc Biol. 2007;81:75–83.[PubMed]
  • 84. Ivanov S. Dragoi AM. Wang X. Dallacosta C. Louten J. Musco G. Sitia G. Yap GS. Wan Y. Biron CA. Bianchi ME. Wang H. Chu WM. A novel role for HMGB1 in TLR9-mediated inflammatory responses to CpG-DNA. Blood. 2007;110:1970–1981.
  • 85. Izuishi K. Tsung A. Jeyabalan G. Critchlow ND. Li J. Tracey KJ. Demarco RA. Lotze MT. Fink MP. Geller DA. Billiar TR. Cutting edge: high-mobility group box 1 preconditioning protects against liver ischemia-reperfusion injury. J Immunol. 2006;176:7154–7158.[PubMed]
  • 86. Jalilian C. Gallant EM. Board PG. Dulhunty AF. Redox potential and the response of cardiac ryanodine receptors to CLIC-2, a member of the glutathione S-transferase structural family. Antioxid Redox Signal. 2008;10:1675–1686.[PubMed]
  • 87. Jantzen HM. Admon A. Bell SP. Tjian R. Nucleolar transcription factor hUBF contains a DNA-binding motif with homology to HMG proteins. Nature. 1990;344:830–836.[PubMed]
  • 88. Jaulmes A. Thierry S. Janvier B. Raymondjean M. Marechal V. Activation of sPLA2-IIA and PGE2 production by high mobility group protein B1 in vascular smooth muscle cells sensitized by IL-1beta. FASEB J. 2006;20:1727–1729.[PubMed]
  • 89. Jayaraman L. Moorthy NC. Murthy KG. Manley JL. Bustin M. Prives C. High mobility group protein-1 (HMG-1) is a unique activator of p53. Genes Dev. 1998;12:462–472.
  • 90. Jiao Y. Wang HC. Fan SJ. Growth suppression and radiosensitivity increase by HMGB1 in breast cancer. Acta Pharmacol Sin. 2007;28:1957–1967.[PubMed]
  • 91. Jin X. Wang L. Wu HS. Zhang L. Wang CY. Tian Y. Zhang JH. N-acetylcysteine inhibits activation of toll-like receptor 2 and 4 gene expression in the liver and lung after partial hepatic ischemia-reperfusion injury in mice. Hepatobiliary Pancreat Dis Int. 2007;6:284–289.[PubMed]
  • 92. Kaczorowski DJ. Nakao A. Vallabhaneni R. Mollen KP. Sugimoto R. Kohmoto J. Zuckerbraun BS. McCurry KR. Billiar TR. Mechanisms of Toll-like receptor 4 (TLR4)-mediated inflammation after cold ischemia/reperfusion in the heart. Transplantation. 2009;87:1455–1463.
  • 93. Kalinina N. Agrotis A. Antropova Y. DiVitto G. Kanellakis P. Kostolias G. Ilyinskaya O. Tararak E. Bobik A. Increased expression of the DNA-binding cytokine HMGB1 in human atherosclerotic lesions: role of activated macrophages and cytokines. Arterioscler Thromb Vasc Biol. 2004;24:2320–2325.[PubMed]
  • 94. Kaneto H. Katakami N. Kawamori D. Miyatsuka T. Sakamoto K. Matsuoka TA. Matsuhisa M. Yamasaki Y. Involvement of oxidative stress in the pathogenesis of diabetes. Antioxid Redox Signal. 2007;9:355–366.[PubMed]
  • 95. Kang R. Tang D. Schapiro NE. Livesey KM. Farkas A. Loughran P. Bierhaus A. Lotze MT. Zeh HJ. The receptor for advanced glycation end products (RAGE) sustains autophagy and limits apoptosis, promoting pancreatic tumor cell survival. Cell Death Differ. 2010;17:666–676.
  • 96. Kang R. Tang D. Yu Y. Wang Z. Hu T. Wang H. Cao L. WAVE1 regulates Bcl-2 localization and phosphorylation in leukemia cells. Leukemia. 2010;24:177–186.
  • 97. Kanki T. Wang K. Cao Y. Baba M. Klionsky DJ. Atg32 is a mitochondrial protein that confers selectivity during mitophagy. Dev Cell. 2009;17:98–109.
  • 98. Karabeyoglu M. Unal B. Bozkurt B. Dolapci I. Bilgihan A. Karabeyoglu I. Cengiz O. The effect of ethyl pyruvate on oxidative stress in intestine and bacterial translocation after thermal injury. J Surg Res. 2008;144:59–63.[PubMed]
  • 99. Kaushik S. Cuervo AM. Autophagy as a cell-repair mechanism: activation of chaperone-mediated autophagy during oxidative stress. Mol Aspects Med. 2006;27:444–454.
  • 100. Kazama H. Ricci JE. Herndon JM. Hoppe G. Green DR. Ferguson TA. Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein. Immunity. 2008;29:21–32.
  • 101. Khan BV. Harrison DG. Olbrych MT. Alexander RW. Medford RM. Nitric oxide regulates vascular cell adhesion molecule 1 gene expression and redox-sensitive transcriptional events in human vascular endothelial cells. Proc Natl Acad Sci U S A. 1996;93:9114–9119.
  • 102. Kiffin R. Bandyopadhyay U. Cuervo AM. Oxidative stress and autophagy. Antioxid Redox Signal. 2006;8:152–162.[PubMed]
  • 103. Kiffin R. Christian C. Knecht E. Cuervo AM. Activation of chaperone-mediated autophagy during oxidative stress. Mol Biol Cell. 2004;15:4829–4840.
  • 104. Kim HS. Cho IH. Kim JE. Shin YJ. Jeon JH. Kim Y. Yang YM. Lee KH. Lee JW. Lee WJ. Ye SK. Chung MH. Ethyl pyruvate has an anti-inflammatory effect by inhibiting ROS-dependent STAT signaling in activated microglia. Free Radic Biol Med. 2008;45:950–963.[PubMed]
  • 105. Kim JB. Lim CM. Yu YM. Lee JK. Induction and subcellular localization of high-mobility group box-1 (HMGB1) in the postischemic rat brain. J Neurosci Res. 2008;86:1125–1131.[PubMed]
  • 106. Klionsky DJ. Emr SD. Autophagy as a regulated pathway of cellular degradation. Science. 2000;290:1717–1721.
  • 107. Knapp S. Muller S. Digilio G. Bonaldi T. Bianchi ME. Musco G. The long acidic tail of high mobility group box 1 (HMGB1) protein forms an extended and flexible structure that interacts with specific residues within and between the HMG boxes. Biochemistry. 2004;43:11992–11997.[PubMed]
  • 108. Kregel KC. Zhang HJ. An integrated view of oxidative stress in aging: basic mechanisms, functional effects, and pathological considerations. Am J Physiol Regul Integr Comp Physiol. 2007;292:R18–R36.[PubMed]
  • 109. Kruger B. Krick S. Dhillon N. Lerner SM. Ames S. Bromberg JS. Lin M. Walsh L. Vella J. Fischereder M. Kramer BK. Colvin RB. Heeger PS. Murphy BT. Schroppel B. Donor Toll-like receptor 4 contributes to ischemia and reperfusion injury following human kidney transplantation. Proc Natl Acad Sci U S A. 2009;106:3390–3395.
  • 110. Krynetski EY. Krynetskaia NF. Bianchi ME. Evans WE. A nuclear protein complex containing high mobility group proteins B1 and B2, heat shock cognate protein 70, ERp60, and glyceraldehyde-3-phosphate dehydrogenase is involved in the cytotoxic response to DNA modified by incorporation of anticancer nucleoside analogues. Cancer Res. 2003;63:100–106.[PubMed]
  • 111. Kusume A. Sasahira T. Luo Y. Isobe M. Nakagawa N. Tatsumoto N. Fujii K. Ohmori H. Kuniyasu H. Suppression of dendritic cells by HMGB1 is associated with lymph node metastasis of human colon cancer. Pathobiology. 2009;76:155–162.[PubMed]
  • 112. Lange SS. Mitchell DL. Vasquez KM. High mobility group protein B1 enhances DNA repair and chromatin modification after DNA damage. Proc Natl Acad Sci U S A. 2008;105:10320–10325.
  • 113. Lange SS. Vasquez KM. HMGB1: the jack-of-all-trades protein is a master DNA repair mechanic. Mol Carcinog. 2009;48:571–580.
  • 114. Levy RM. Mollen KP. Prince JM. Kaczorowski DJ. Vallabhaneni R. Liu S. Tracey KJ. Lotze MT. Hackam DJ. Fink MP. Vodovotz Y. Billiar TR. Systemic inflammation and remote organ injury following trauma require HMGB1. Am J Physiol Regul Integr Comp Physiol. 2007;293:R1538–R1544.[PubMed]
  • 115. Li CY. Lee JS. Ko YG. Kim JI. Seo JS. Heat shock protein 70 inhibits apoptosis downstream of cytochrome c release and upstream of caspase-3 activation. J Biol Chem. 2000;275:25665–25671.[PubMed]
  • 116. Li J. Kokkola R. Tabibzadeh S. Yang R. Ochani M. Qiang X. Harris HE. Czura CJ. Wang H. Ulloa L. Warren HS. Moldawer LL. Fink MP. Andersson U. Tracey KJ. Yang H. Structural basis for the proinflammatory cytokine activity of high mobility group box 1. Mol Med. 2003;9:37–45.
  • 117. Li W. Ashok M. Li J. Yang H. Sama AE. Wang H. A major ingredient of green tea rescues mice from lethal sepsis partly by inhibiting HMGB1. PLoS ONE. 2007;2:e1153.
  • 118. Li W. Febbraio M. Reddy SP. Yu DY. Yamamoto M. Silverstein RL. CD36 participates in a signaling pathway that regulates ROS formation in murine VSMCs. J Clin Invest. 2010;120:3996–4006.
  • 119. Li W. Sama AE. Wang H. Role of HMGB1 in cardiovascular diseases. Curr Opin Pharmacol. 2006;6:130–135.
  • 120. Liang X. Chavez AR. Schapiro NE. Loughran P. Thorne SH. Amoscato AA. Zeh HJ. Beer-Stolz D. Lotze MT. de Vera ME. Ethyl pyruvate administration inhibits hepatic tumor growth. J Leukoc Biol. 2009;86:599–607.[PubMed]
  • 121. Lim JH. Kwon TK. Curcumin inhibits phorbol myristate acetate (PMA)-induced MCP-1 expression by inhibiting ERK and NF-kappaB transcriptional activity. Food Chem Toxicol. 2010;48:47–52.[PubMed]
  • 122. Limana F. Germani A. Zacheo A. Kajstura J. Di Carlo A. Borsellino G. Leoni O. Palumbo R. Battistini L. Rastaldo R. Muller S. Pompilio G. Anversa P. Bianchi ME. Capogrossi MC. Exogenous high-mobility group box 1 protein induces myocardial regeneration after infarction via enhanced cardiac C-kit+ cell proliferation and differentiation. Circ Res. 2005;97:e73–e83.[PubMed]
  • 123. Lin MT. Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature. 2006;443:787–795.[PubMed]
  • 124. Lindersson EK. Hojrup P. Gai WP. Locker D. Martin D. Jensen PH. Alpha-Synuclein filaments bind the transcriptional regulator HMGB-1. Neuroreport. 2004;15:2735–2739.[PubMed]
  • 125. Liu G. Wang J. Park YJ. Tsuruta Y. Lorne EF. Zhao X. Abraham E. High mobility group protein-1 inhibits phagocytosis of apoptotic neutrophils through binding to phosphatidylserine. J Immunol. 2008;181:4240–4246.
  • 126. Liu JJ. Song CW. Yue Y. Duan CG. Yang J. He T. He YZ. Quercetin inhibits LPS-induced delay in spontaneous apoptosis and activation of neutrophils. Inflamm Res. 2005;54:500–507.[PubMed]
  • 127. Liu Y. Prasad R. Beard WA. Hou EW. Horton JK. McMurray CT. Wilson SH. Coordination between polymerase beta and FEN1 can modulate CAG repeat expansion. J Biol Chem. 2009;284:28352–28366.
  • 128. Liu Y. Prasad R. Wilson SH. HMGB1: roles in base excision repair and related function. Biochim Biophys Acta. 2010;1799:119–130.
  • 129. Livesey KM. Tang D. Zeh HJ. Lotze MT. Autophagy inhibition in combination cancer treatment. Curr Opin Investig Drugs. 2009;10:1269–1279.[PubMed]
  • 130. Livesey KM. Tang D. Zeh HJ. Lotze MT. Not just nuclear proteins: “novel” autophagy cancer treatment targets—p53 and HMGB1. Curr Opin Investig Drugs. 2008;9:1259–1263.[PubMed]
  • 131. Lotze MT. Deisseroth A. Rubartelli A. Damage associated molecular pattern molecules. Clin Immunol. 2007;124:1–4.
  • 132. Lotze MT. DeMarco RA. Dealing with death: HMGB1 as a novel target for cancer therapy. Curr Opin Investig Drugs. 2003;4:1405–1409.[PubMed]
  • 133. Lotze MT. Tracey KJ. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat Rev Immunol. 2005;5:331–342.[PubMed]
  • 134. Lotze MT. Zeh HJ. Rubartelli A. Sparvero LJ. Amoscato AA. Washburn NR. Devera ME. Liang X. Tor M. Billiar T. The grateful dead: damage-associated molecular pattern molecules and reduction/oxidation regulate immunity. Immunol Rev. 2007;220:60–81.[PubMed]
  • 135. Manfredi AA. Capobianco A. Esposito A. De Cobelli F. Canu T. Monno A. Raucci A. Sanvito F. Doglioni C. Nawroth PP. Bierhaus A. Bianchi ME. Rovere-Querini P. Del Maschio A. Maturing dendritic cells depend on RAGE for in vivo homing to lymph nodes. J Immunol. 2008;180:2270–2275.[PubMed]
  • 136. Manjeet KR. Ghosh B. Quercetin inhibits LPS-induced nitric oxide and tumor necrosis factor-alpha production in murine macrophages. Int J Immunopharmacol. 1999;21:435–443.[PubMed]
  • 137. Maret W. Zinc coordination environments in proteins as redox sensors and signal transducers. Antioxid Redox Signal. 2006;8:1419–1441.[PubMed]
  • 138. Maroso M. Balosso S. Ravizza T. Liu J. Aronica E. Iyer AM. Rossetti C. Molteni M. Casalgrandi M. Manfredi AA. Bianchi ME. Vezzani A. Toll-like receptor 4 and high-mobility group box-1 are involved in ictogenesis and can be targeted to reduce seizures. Nat Med. 2010;16:413–419.[PubMed]
  • 139. Massullo P. Druhan LJ. Bunnell BA. Hunter MG. Robinson JM. Marsh CB. Avalos BR. Aberrant subcellular targeting of the G185R neutrophil elastase mutant associated with severe congenital neutropenia induces premature apoptosis of differentiating promyelocytes. Blood. 2005;105:3397–3404.
  • 140. Massullo P. Sumoza-Toledo A. Bhagat H. Partida-Sanchez S. TRPM channels, calcium and redox sensors during innate immune responses. Semin Cell Dev Biol. 2006;17:654–666.[PubMed]
  • 141. Matsuoka N. Itoh T. Watarai H. Sekine-Kondo E. Nagata N. Okamoto K. Mera T. Yamamoto H. Yamada S. Maruyama I. Taniguchi M. Yasunami Y. High-mobility group box 1 is involved in the initial events of early loss of transplanted islets in mice. J Clin Invest. 2010;120:735–743.
  • 142. McKinney K. Prives C. Efficient specific DNA binding by p53 requires both its central and C-terminal domains as revealed by studies with high-mobility group 1 protein. Mol Cell Biol. 2002;22:6797–6808.
  • 143. Meissner F. Molawi K. Zychlinsky A. Superoxide dismutase 1 regulates caspase-1 and endotoxic shock. Nat Immunol. 2008;9:866–872.[PubMed]
  • 144. Melki MT. Saidi H. Dufour A. Olivo-Marin JC. Gougeon ML. Escape of HIV-1-infected dendritic cells from TRAIL-mediated NK cell cytotoxicity during NK-DC cross-talk—a pivotal role of HMGB1. PLoS Pathog. 2010;6:e1000862.
  • 145. Melloni E. Sparatore B. Patrone M. Pessino A. Passalacqua M. Pontremoli S. Extracellular release of the “differentiation enhancing factor,” a HMG1 protein type, is an early step in murine erythroleukemia cell differentiation. FEBS Lett. 1995;368:466–470.[PubMed]
  • 146. Meng X. Harken AH. The interaction between Hsp70 and TNF-alpha expression: a novel mechanism for protection of the myocardium against post-injury depression. Shock. 2002;17:345–353.[PubMed]
  • 147. Messmer D. Yang H. Telusma G. Knoll F. Li J. Messmer B. Tracey KJ. Chiorazzi N. High mobility group box protein 1: an endogenous signal for dendritic cell maturation and Th1 polarization. J Immunol. 2004;173:307–313.[PubMed]
  • 148. Mittal D. Saccheri F. Venereau E. Pusterla T. Bianchi ME. Rescigno M. TLR4-mediated skin carcinogenesis is dependent on immune and radioresistant cells. EMBO J. 2010;29:2242–2252.
  • 149. Monastyrska I. Rieter E. Klionsky DJ. Reggiori F. Multiple roles of the cytoskeleton in autophagy. Biol Rev Camb Philos Soc. 2009;84:431–448.
  • 150. Muller S. Scaffidi P. Degryse B. Bonaldi T. Ronfani L. Agresti A. Beltrame M. Bianchi ME. New EMBO members' review: the double life of HMGB1 chromatin protein: architectural factor and extracellular signal. EMBO J. 2001;20:4337–4340.
  • 151. Nicholas SA. Sumbayev VV. The role of redox-dependent mechanisms in the downregulation of ligand-induced Toll-like receptors 7, 8 and 4-mediated HIF-1alpha prolyl hydroxylation. Immunol Cell Biol. 2010;88:180–186.[PubMed]
  • 152. Noble CG. Dong JM. Manser E. Song H. Bcl-xL and UVRAG cause a monomer-dimer switch in Beclin1. J Biol Chem. 2008;283:26274–26282.
  • 153. Ohndorf UM. Rould MA. He Q. Pabo CO. Lippard SJ. Basis for recognition of cisplatin-modified DNA by high-mobility-group proteins. Nature. 1999;399:708–712.[PubMed]
  • 154. Oozawa S. Mori S. Kanke T. Takahashi H. Liu K. Tomono Y. Asanuma M. Miyazaki I. Nishibori M. Sano S. Effects of HMGB1 on ischemia-reperfusion injury in the rat heart. Circ J. 2008;72:1178–1184.[PubMed]
  • 155. Orlova VV. Choi EY. Xie C. Chavakis E. Bierhaus A. Ihanus E. Ballantyne CM. Gahmberg CG. Bianchi ME. Nawroth PP. Chavakis T. A novel pathway of HMGB1-mediated inflammatory cell recruitment that requires Mac-1-integrin. EMBO J. 2007;26:1129–1139.
  • 156. Outten FW. Theil EC. Iron-based redox switches in biology. Antioxid Redox Signal. 2009;11:1029–1046.
  • 157. Palumbo R. De Marchis F. Pusterla T. Conti A. Alessio M. Bianchi ME. Src family kinases are necessary for cell migration induced by extracellular HMGB1. J Leukoc Biol. 2009;86:617–623.[PubMed]
  • 158. Palumbo R. Galvez BG. Pusterla T. De Marchis F. Cossu G. Marcu KB. Bianchi ME. Cells migrating to sites of tissue damage in response to the danger signal HMGB1 require NF-{kappa}B activation. J Cell Biol. 2007;179:33–40.
  • 159. Palumbo R. Sampaolesi M. De Marchis F. Tonlorenzi R. Colombetti S. Mondino A. Cossu G. Bianchi ME. Extracellular HMGB1, a signal of tissue damage, induces mesoangioblast migration and proliferation. J Cell Biol. 2004;164:441–449.
  • 160. Pardo M. Budick-Harmelin N. Tirosh B. Tirosh O. Antioxidant defense in hepatic ischemia-reperfusion injury is regulated by damage-associated molecular pattern signal molecules. Free Radic Biol Med. 2008;45:1073–1083.[PubMed]
  • 161. Park HS. Kim SR. Lee YC. Impact of oxidative stress on lung diseases. Respirology. 2009;14:27–38.[PubMed]
  • 162. Passalacqua M. Patrone M. Picotti GB. Del Rio M. Sparatore B. Melloni E. Pontremoli S. Stimulated astrocytes release high-mobility group 1 protein, an inducer of LAN-5 neuroblastoma cell differentiation. Neuroscience. 1998;82:1021–1028.[PubMed]
  • 163. Pattingre S. Tassa A. Qu X. Garuti R. Liang XH. Mizushima N. Packer M. Schneider MD. Levine B. Bcl-2 antiapoptotic proteins inhibit Beclin 1-dependent autophagy. Cell. 2005;122:927–939.[PubMed]
  • 164. Peter ME. ROS eliminate danger. Immunity. 2008;29:1–2.[PubMed]
  • 165. Popovic PJ. DeMarco R. Lotze MT. Winikoff SE. Bartlett DL. Krieg AM. Guo ZS. Brown CK. Tracey KJ. Zeh HJ., 3rd High mobility group B1 protein suppresses the human plasmacytoid dendritic cell response to TLR9 agonists. J Immunol. 2006;177:8701–8707.[PubMed]
  • 166. Porto A. Palumbo R. Pieroni M. Aprigliano G. Chiesa R. Sanvito F. Maseri A. Bianchi ME. Smooth muscle cells in human atherosclerotic plaques secrete and proliferate in response to high mobility group box 1 protein. FASEB J. 2006;20:2565–2566.[PubMed]
  • 167. Prasad R. Liu Y. Deterding LJ. Poltoratsky VP. Kedar PS. Horton JK. Kanno S. Asagoshi K. Hou EW. Khodyreva SN. Lavrik OI. Tomer KB. Yasui A. Wilson SH. HMGB1 is a cofactor in mammalian base excision repair. Mol Cell. 2007;27:829–841.
  • 168. Qi ML. Tagawa K. Enokido Y. Yoshimura N. Wada Y. Watase K. Ishiura S. Kanazawa I. Botas J. Saitoe M. Wanker EE. Okazawa H. Proteome analysis of soluble nuclear proteins reveals that HMGB1/2 suppress genotoxic stress in polyglutamine diseases. Nat Cell Biol. 2007;9:402–414.[PubMed]
  • 169. Qin S. Wang H. Yuan R. Li H. Ochani M. Ochani K. Rosas-Ballina M. Czura CJ. Huston JM. Miller E. Lin X. Sherry B. Kumar A. Larosa G. Newman W. Tracey KJ. Yang H. Role of HMGB1 in apoptosis-mediated sepsis lethality. J Exp Med. 2006;203:1637–1642.
  • 170. Qiu J. Nishimura M. Wang Y. Sims JR. Qiu S. Savitz SI. Salomone S. Moskowitz MA. Early release of HMGB-1 from neurons after the onset of brain ischemia. J Cereb Blood Flow Metab. 2008;28:927–938.[PubMed]
  • 171. Qiu J. Xu J. Zheng Y. Wei Y. Zhu X. Lo EH. Moskowitz MA. Sims JR. High-mobility group box 1 promotes metalloproteinase-9 upregulation through Toll-like receptor 4 after cerebral ischemia. Stroke. 2010;41:2077–2082.
  • 172. Raucci A. Palumbo R. Bianchi ME. HMGB1: a signal of necrosis. Autoimmunity. 2007;40:285–289.[PubMed]
  • 173. Rauvala H. Rouhiainen A. RAGE as a receptor of HMGB1 (Amphoterin): roles in health and disease. Curr Mol Med. 2007;7:725–734.[PubMed]
  • 174. Reggiori F. Monastyrska I. Shintani T. Klionsky DJ. The actin cytoskeleton is required for selective types of autophagy, but not nonspecific autophagy, in the yeast Saccharomyces cerevisiae. Mol Biol Cell. 2005;16:5843–5856.
  • 175. Rendon-Mitchell B. Ochani M. Li J. Han J. Wang H. Yang H. Susarla S. Czura C. Mitchell RA. Chen G. Sama AE. Tracey KJ. IFN-gamma induces high mobility group box 1 protein release partly through a TNF-dependent mechanism. J Immunol. 2003;170:3890–3897.[PubMed]
  • 176. Riuzzi F. Sorci G. Donato R. The amphoterin (HMGB1)/receptor for advanced glycation end products (RAGE) pair modulates myoblast proliferation, apoptosis, adhesiveness, migration, and invasiveness. Functional inactivation of RAGE in L6 myoblasts results in tumor formation in vivo. J Biol Chem. 2006;281:8242–8253.[PubMed]
  • 177. Riuzzi F. Sorci G. Donato R. RAGE expression in rhabdomyosarcoma cells results in myogenic differentiation and reduced proliferation, migration, invasiveness, and tumor growth. Am J Pathol. 2007;171:947–961.
  • 178. Rocksen D. Lilliehook B. Larsson R. Johansson T. Bucht A. Differential anti-inflammatory and anti-oxidative effects of dexamethasone and N-acetylcysteine in endotoxin-induced lung inflammation. Clin Exp Immunol. 2000;122:249–256.
  • 179. Rong Y. Distelhorst CW. Bcl-2 protein family members: versatile regulators of calcium signaling in cell survival and apoptosis. Annu Rev Physiol. 2008;70:73–91.[PubMed]
  • 180. Rossini A. Zacheo A. Mocini D. Totta P. Facchiano A. Castoldi R. Sordini P. Pompilio G. Abeni D. Capogrossi MC. Germani A. HMGB1-stimulated human primary cardiac fibroblasts exert a paracrine action on human and murine cardiac stem cells. J Mol Cell Cardiol. 2008;44:683–693.[PubMed]
  • 181. Rouhiainen A. Kuja-Panula J. Wilkman E. Pakkanen J. Stenfors J. Tuominen RK. Lepantalo M. Carpen O. Parkkinen J. Rauvala H. Regulation of monocyte migration by amphoterin (HMGB1) Blood. 2004;104:1174–1182.[PubMed]
  • 182. Rovere-Querini P. Capobianco A. Scaffidi P. Valentinis B. Catalanotti F. Giazzon M. Dumitriu IE. Muller S. Iannacone M. Traversari C. Bianchi ME. Manfredi AA. HMGB1 is an endogenous immune adjuvant released by necrotic cells. EMBO Rep. 2004;5:825–830.
  • 183. Rubartelli A. Lotze MT. Inside, outside, upside down: damage-associated molecular-pattern molecules (DAMPs) and redox. Trends Immunol. 2007;28:429–436.[PubMed]
  • 184. Rubartelli A. Sitia R. Stress as an intercellular signal: the emergence of stress associated molecular patterns (SAMP) Antioxid Redox Signal. 2009;11:2621–2629.[PubMed]
  • 185. Sahu D. Debnath P. Takayama Y. Iwahara J. Redox properties of the A-domain of the HMGB1 protein. FEBS Lett. 2008;582:3973–3978.
  • 186. Samuhasaneeto S. Thong-Ngam D. Kulaputana O. Suyasunanont D. Klaikeaw N. Curcumin decreased oxidative stress, inhibited NF-kappaB activation, and improved liver pathology in ethanol-induced liver injury in rats. J Biomed Biotechnol. 2009;2009:981963.
  • 187. Sandoval H. Thiagarajan P. Dasgupta SK. Schumacher A. Prchal JT. Chen M. Wang J. Essential role for Nix in autophagic maturation of erythroid cells. Nature. 2008;454:232–235.
  • 188. Sappington PL. Yang R. Yang H. Tracey KJ. Delude RL. Fink MP. HMGB1 B box increases the permeability of Caco-2 enterocytic monolayers and impairs intestinal barrier function in mice. Gastroenterology. 2002;123:790–802.[PubMed]
  • 189. Sarsour EH. Kumar MG. Chaudhuri L. Kalen AL. Goswami PC. Redox control of the cell cycle in health and disease. Antioxid Redox Signal. 2009;11:2985–3011.
  • 190. Scaffidi P. Misteli T. Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature. 2002;418:191–195.[PubMed]
  • 191. Schafer FQ. Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med. 2001;30:1191–1212.[PubMed]
  • 192. Scherz-Shouval R. Elazar Z. ROS, mitochondria and the regulation of autophagy. Trends Cell Biol. 2007;17:422–427.[PubMed]
  • 193. Scherz-Shouval R. Shvets E. Fass E. Shorer H. Gil L. Elazar Z. Reactive oxygen species are essential for autophagy and specifically regulate the activity of Atg4. EMBO J. 2007;26:1749–1760.
  • 194. Schulze PC. Lee RT. Oxidative stress and atherosclerosis. Curr Atheroscler Rep. 2005;7:242–248.[PubMed]
  • 195. Schwertassek U. Balmer Y. Gutscher M. Weingarten L. Preuss M. Engelhard J. Winkler M. Dick TP. Selective redox regulation of cytokine receptor signaling by extracellular thioredoxin-1. EMBO J. 2007;26:3086–3097.
  • 196. Semino C. Angelini G. Poggi A. Rubartelli A. NK/iDC interaction results in IL-18 secretion by DCs at the synaptic cleft followed by NK cell activation and release of the DC maturation factor HMGB1. Blood. 2005;106:609–616.[PubMed]
  • 197. Sevier CS. Kaiser CA. Formation and transfer of disulphide bonds in living cells. Nat Rev Mol Cell Biol. 2002;3:836–847.[PubMed]
  • 198. Shaikhali J. Heiber I. Seidel T. Stroher E. Hiltscher H. Birkmann S. Dietz KJ. Baier M. The redox-sensitive transcription factor Rap2.4a controls nuclear expression of 2-Cys peroxiredoxin A and other chloroplast antioxidant enzymes. BMC Plant Biol. 2008;8:48.
  • 199. Sharma P. Chakraborty R. Wang L. Min B. Tremblay ML. Kawahara T. Lambeth JD. Haque SJ. Redox regulation of interleukin-4 signaling. Immunity. 2008;29:551–564.
  • 200. Shukla PK. Khanna VK. Khan MY. Srimal RC. Protective effect of curcumin against lead neurotoxicity in rat. Hum Exp Toxicol. 2003;22:653–658.[PubMed]
  • 201. Simon HU. Haj-Yehia A. Levi-Schaffer F. Role of reactive oxygen species (ROS) in apoptosis induction. Apoptosis. 2000;5:415–418.[PubMed]
  • 202. Soderberg A. Barral AM. Soderstrom M. Sander B. Rosen A. Redox-signaling transmitted in trans to neighboring cells by melanoma-derived TNF-containing exosomes. Free Radic Biol Med. 2007;43:90–99.[PubMed]
  • 203. Soro-Paavonen A. Watson AM. Li J. Paavonen K. Koitka A. Calkin AC. Barit D. Coughlan MT. Drew BG. Lancaster GI. Thomas M. Forbes JM. Nawroth PP. Bierhaus A. Cooper ME. Jandeleit-Dahm KA. Receptor for advanced glycation end products (RAGE) deficiency attenuates the development of atherosclerosis in diabetes. Diabetes. 2008;57:2461–2469.
  • 204. Sparatore B. Patrone M. Passalacqua M. Pedrazzi M. Gaggero D. Pontremoli S. Melloni E. Extracellular processing of amphoterin generates a peptide active on erythroleukaemia cell differentiation. Biochem J. 2001;357:569–574.
  • 205. Sparatore B. Pedrazzi M. Passalacqua M. Gaggero D. Patrone M. Pontremoli S. Melloni E. Stimulation of erythroleukaemia cell differentiation by extracellular high-mobility group-box protein 1 is independent of the receptor for advanced glycation end-products. Biochem J. 2002;363:529–535.
  • 206. Sparvero LJ. Asafu-Adjei D. Kang R. Tang D. Amin N. Im J. Rutledge R. Lin B. Amoscato AA. Zeh HJ. Lotze MT. RAGE (Receptor for Advanced Glycation Endproducts), RAGE ligands, and their role in cancer and inflammation. J Transl Med. 2009;7:17.
  • 207. Stott K. Watson M. Howe FS. Grossmann JG. Thomas JO. Tail-mediated collapse of HMGB1 is dynamic and occurs via differential binding of the acidic tail to the A and B domains. J Mol Biol. 2010;403:706–722.[PubMed]
  • 208. Stros M. Muselikova-Polanska E. Pospisilova S. Strauss F. High-affinity binding of tumor-suppressor protein p53 and HMGB1 to hemicatenated DNA loops. Biochemistry. 2004;43:7215–7225.[PubMed]
  • 209. Stros M. Ozaki T. Bacikova A. Kageyama H. Nakagawara A. HMGB1 and HMGB2 cell-specifically down-regulate the p53- and p73-dependent sequence-specific transactivation from the human Bax gene promoter. J Biol Chem. 2002;277:7157–7164.[PubMed]
  • 210. Stumbo AC. Cortez E. Rodrigues CA. Henriques MG. Porto LC. Barbosa HS. Carvalho L. Mitochondrial localization of non-histone protein HMGB1 during human endothelial cell-Toxoplasma gondii infection. Cell Biol Int. 2008;32:235–238.[PubMed]
  • 211. Sundberg E. Fasth AE. Palmblad K. Harris HE. Andersson U. High mobility group box chromosomal protein 1 acts as a proliferation signal for activated T lymphocytes. Immunobiology. 2009;214:303–309.[PubMed]
  • 212. Surh YJ. Kundu JK. Na HK. Nrf2 as a master redox switch in turning on the cellular signaling involved in the induction of cytoprotective genes by some chemopreventive phytochemicals. Planta Med. 2008;74:1526–1539.[PubMed]
  • 213. Tang D. Kang R. Cao L. Zhang G. Yu Y. Xiao W. Wang H. Xiao X. A pilot study to detect high mobility group box 1 and heat shock protein 72 in cerebrospinal fluid of pediatric patients with meningitis. Crit Care Med. 2008;36:291–295.[PubMed]
  • 214. Tang D. Kang R. Cheh CW. Livesey KM. Liang X. Schapiro NE. Benschop R. Sparvero LJ. Amoscato AA. Tracey KJ. Zeh HJ. Lotze MT. HMGB1 release and redox regulates autophagy and apoptosis in cancer cells. Oncogene. 2010;29:5299–5310.
  • 215. Tang D. Kang R. Livesey KM. Cheh C. Adam Farkas A. Loughran P. Hoppe G. Bianchi ME. Tracey KJ. Zeh HJ. Lotze MT. Endogenous HMGB1 regulates autophagy. J Cell Biol. 2010;190:881–892.
  • 216. Tang D. Kang R. Xiao W. Jiang L. Liu M. Shi Y. Wang K. Wang H. Xiao X. Nuclear heat shock protein 72 as a negative regulator of oxidative stress (hydrogen peroxide)-induced HMGB1 cytoplasmic translocation and release. J Immunol. 2007;178:7376–7384.
  • 217. Tang D. Kang R. Xiao W. Wang H. Calderwood SK. Xiao X. The anti-inflammatory effects of heat shock protein 72 involve inhibition of high-mobility-group box 1 release and proinflammatory function in macrophages. J Immunol. 2007;179:1236–1244.
  • 218. Tang D. Kang R. Xiao W. Zhang H. Lotze MT. Wang H. Xiao X. Quercetin prevents lipopolysaccharide-induced HMGB1 release and proinflammatory function. Am J Respir Cell Mol Biol. 2009;41:651–660.
  • 219. Tang D. Kang R. Zeh HJ., 3rd Lotze MT. High-mobility group box 1 and cancer. Biochim Biophys Acta. 2010;1799:131–140.
  • 220. Tang D. Lotze MT. Zeh HJ., 3rd Kang R. The redox protein HMGB1 regulates cell death and survival in cancer treatment. Autophagy. 2010;6:1181–1183.[PubMed]
  • 221. Tang D. Shi Y. Jang L. Wang K. Xiao W. Xiao X. Heat shock response inhibits release of high mobility group box 1 protein induced by endotoxin in murine macrophages. Shock. 2005;23:434–440.[PubMed]
  • 222. Tang D. Shi Y. Kang R. Li T. Xiao W. Wang H. Xiao X. Hydrogen peroxide stimulates macrophages and monocytes to actively release HMGB1. J Leukoc Biol. 2007;81:741–747.
  • 223. Taniguchi N. Kawahara K. Yone K. Hashiguchi T. Yamakuchi M. Goto M. Inoue K. Yamada S. Ijiri K. Matsunaga S. Nakajima T. Komiya S. Maruyama I. High mobility group box chromosomal protein 1 plays a role in the pathogenesis of rheumatoid arthritis as a novel cytokine. Arthritis Rheum. 2003;48:971–981.[PubMed]
  • 224. Tatsuta T. Langer T. Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 2008;27:306–314.
  • 225. Tesniere A. Panaretakis T. Kepp O. Apetoh L. Ghiringhelli F. Zitvogel L. Kroemer G. Molecular characteristics of immunogenic cancer cell death. Cell Death Differ. 2008;15:3–12.[PubMed]
  • 226. Thomas JO. HMG1 and 2: architectural DNA-binding proteins. Biochem Soc Trans. 2001;29:395–401.[PubMed]
  • 227. Tian J. Avalos AM. Mao SY. Chen B. Senthil K. Wu H. Parroche P. Drabic S. Golenbock D. Sirois C. Hua J. An LL. Audoly L. La Rosa G. Bierhaus A. Naworth P. Marshak-Rothstein A. Crow MK. Fitzgerald KA. Latz E. Kiener PA. Coyle AJ. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol. 2007;8:487–496.[PubMed]
  • 228. Tirouvanziam R. Conrad CK. Bottiglieri T. Herzenberg LA. Moss RB. High-dose oral N-acetylcysteine, a glutathione prodrug, modulates inflammation in cystic fibrosis. Proc Natl Acad Sci U S A. 2006;103:4628–4633.
  • 229. Topalova D. Ugrinova I. Pashev IG. Pasheva EA. HMGB1 protein inhibits DNA replication in vitro: a role of the acetylation and the acidic tail. Int J Biochem Cell Biol. 2008;40:1536–1542.[PubMed]
  • 230. Treutiger CJ. Mullins GE. Johansson AS. Rouhiainen A. Rauvala HM. Erlandsson-Harris H. Andersson U. Yang H. Tracey KJ. Andersson J. Palmblad JE. High mobility group 1 B-box mediates activation of human endothelium. J Intern Med. 2003;254:375–385.[PubMed]
  • 231. Tsung A. Klune JR. Zhang X. Jeyabalan G. Cao Z. Peng X. Stolz DB. Geller DA. Rosengart MR. Billiar TR. HMGB1 release induced by liver ischemia involves Toll-like receptor 4 dependent reactive oxygen species production and calcium-mediated signaling. J Exp Med. 2007;204:2913–2923.
  • 232. Tsung A. Sahai R. Tanaka H. Nakao A. Fink MP. Lotze MT. Yang H. Li J. Tracey KJ. Geller DA. Billiar TR. The nuclear factor HMGB1 mediates hepatic injury after murine liver ischemia-reperfusion. J Exp Med. 2005;201:1135–1143.
  • 233. Ulloa L. Messmer D. High-mobility group box 1 (HMGB1) protein: friend and foe. Cytokine Growth Factor Rev. 2006;17:189–201.[PubMed]
  • 234. Ulloa L. Ochani M. Yang H. Tanovic M. Halperin D. Yang R. Czura CJ. Fink MP. Tracey KJ. Ethyl pyruvate prevents lethality in mice with established lethal sepsis and systemic inflammation. Proc Natl Acad Sci U S A. 2002;99:12351–12356.
  • 235. Uramoto H. Izumi H. Nagatani G. Ohmori H. Nagasue N. Ise T. Yoshida T. Yasumoto K. Kohno K. Physical interaction of tumour suppressor p53/p73 with CCAAT-binding transcription factor 2 (CTF2) and differential regulation of human high-mobility group 1 (HMG1) gene expression. Biochem J. 2003;371:301–310.
  • 236. Urbonaviciute V. Meister S. Furnrohr BG. Frey B. Guckel E. Schett G. Herrmann M. Voll RE. Oxidation of the alarmin high-mobility group box 1 protein (HMGB1) during apoptosis. Autoimmunity. 2009;42:305–307.[PubMed]
  • 237. Varma SD. Devamanoharan PS. Ali AH. Prevention of intracellular oxidative stress to lens by pyruvate and its ester. Free Radic Res. 1998;28:131–135.[PubMed]
  • 238. Velazquez JM. Lindquist S. hsp70: nuclear concentration during environmental stress and cytoplasmic storage during recovery. Cell. 1984;36:655–662.[PubMed]
  • 239. Verrier CS. Roodi N. Yee CJ. Bailey LR. Jensen RA. Bustin M. Parl FF. High-mobility group (HMG) protein HMG-1 and TATA-binding protein-associated factor TAF(II)30 affect estrogen receptor-mediated transcriptional activation. Mol Endocrinol. 1997;11:1009–1019.[PubMed]
  • 240. Victor VM. Rocha M. Sola E. Banuls C. Garcia-Malpartida K. Hernandez-Mijares A. Oxidative stress, endothelial dysfunction and atherosclerosis. Curr Pharm Des. 2009;15:2988–3002.[PubMed]
  • 241. Wang H. Bloom O. Zhang M. Vishnubhakat JM. Ombrellino M. Che J. Frazier A. Yang H. Ivanova S. Borovikova L. Manogue KR. Faist E. Abraham E. Andersson J. Andersson U. Molina PE. Abumrad NN. Sama A. Tracey KJ. HMG-1 as a late mediator of endotoxin lethality in mice. Science. 1999;285:248–251.[PubMed]
  • 242. Wang H. Ward MF. Sama AE. Novel Hmgb1-inhibiting therapeutic agents for experimental sepsis. Shock. 2009;32:348–357.
  • 243. Wang H. Yang H. Tracey KJ. Extracellular role of HMGB1 in inflammation and sepsis. J Intern Med. 2004;255:320–331.[PubMed]
  • 244. Wang Q. Ding Q. Zhou Y. Gou X. Hou L. Chen S. Zhu Z. Xiong L. Ethyl pyruvate attenuates spinal cord ischemic injury with a wide therapeutic window through inhibiting high-mobility group box 1 release in rabbits. Anesthesiology. 2009;110:1279–1286.[PubMed]
  • 245. Watanabe T. Kubota S. Nagaya M. Ozaki S. Nagafuchi H. Akashi K. Taira Y. Tsukikawa S. Oowada S. Nakano S. The role of HMGB-1 on the development of necrosis during hepatic ischemia and hepatic ischemia/reperfusion injury in mice. J Surg Res. 2005;124:59–66.[PubMed]
  • 246. Webb C. Twedt D. Oxidative stress and liver disease. Vet Clin North Am Small Anim Pract. 2008;38:125–135. v, [[PubMed]
  • 247. Wegerich F. Turano P. Allegrozzi M. Mohwald H. Lisdat F. Cytochrome C mutants for superoxide biosensors. Anal Chem. 2009;81:2976–2984.[PubMed]
  • 248. Welch WJ. Feramisco JR. Nuclear and nucleolar localization of the 72,000-dalton heat shock protein in heat-shocked mammalian cells. J Biol Chem. 1984;259:4501–4513.[PubMed]
  • 249. Wells PG. McCallum GP. Chen CS. Henderson JT. Lee CJ. Perstin J. Preston TJ. Wiley MJ. Wong AW. Oxidative stress in developmental origins of disease: teratogenesis, neurodevelopmental deficits, and cancer. Toxicol Sci. 2009;108:4–18.[PubMed]
  • 250. Wilmanski J. Siddiqi M. Deitch EA. Spolarics Z. Augmented IL-10 production and redox-dependent signaling pathways in glucose-6-phosphate dehydrogenase-deficient mouse peritoneal macrophages. J Leukoc Biol. 2005;78:85–94.[PubMed]
  • 251. Winterbourn CC. Hampton MB. Thiol chemistry and specificity in redox signaling. Free Radic Biol Med. 2008;45:549–561.[PubMed]
  • 252. Wu H. Chen G. Wyburn KR. Yin J. Bertolino P. Eris JM. Alexander SI. Sharland AF. Chadban SJ. TLR4 activation mediates kidney ischemia/reperfusion injury. J Clin Invest. 2007;117:2847–2859.
  • 253. Yan SD. Chen X. Fu J. Chen M. Zhu H. Roher A. Slattery T. Zhao L. Nagashima M. Morser J. Migheli A. Nawroth P. Stern D. Schmidt AM. RAGE and amyloid-beta peptide neurotoxicity in Alzheimer's disease. Nature. 1996;382:685–691.[PubMed]
  • 254. Yanai H. Ban T. Wang Z. Choi MK. Kawamura T. Negishi H. Nakasato M. Lu Y. Hangai S. Koshiba R. Savitsky D. Ronfani L. Akira S. Bianchi ME. Honda K. Tamura T. Kodama T. Taniguchi T. HMGB proteins function as universal sentinels for nucleic-acid-mediated innate immune responses. Nature. 2009;462:99–103.[PubMed]
  • 255. Yang D. Chen Q. Yang H. Tracey KJ. Bustin M. Oppenheim JJ. 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]
  • 256. Yang H. Hreggvidsdottir HS. Palmblad K. Wang H. Ochani M. Li J. Lu B. Chavan S. Rosas-Ballina M. Al-Abed Y. Akira S. Bierhaus A. Erlandsson-Harris H. Andersson U. Tracey KJ. A critical cysteine is required for HMGB1 binding to Toll-like receptor 4 and activation of macrophage cytokine release. Proc Natl Acad Sci U S A. 2010;107:11942–11947.
  • 257. Yang J. Huang C. Jiang H. Ding J. Statins attenuate high mobility group box-1 protein induced vascular endothelial activation: a key role for TLR4/NF-kappaB signaling pathway. Mol Cell Biochem. 2010;345:189–195.[PubMed]
  • 258. Yang QW. Lu FL. Zhou Y. Wang L. Zhong Q. Lin S. Xiang J. Li JC. Fang CQ. Wang JZ. HMBG1 mediates ischemia-reperfusion injury by TRIF-adaptor independent Toll-like receptor 4 signaling. J Cereb Blood Flow Metab. 2010 Aug 11; doi: 10.1038/jcbfm.2010.129. [Epub ahead of print] ] [
  • 259. Yao D. Brownlee M. Hyperglycemia-induced reactive oxygen species increase expression of RAGE and RAGE ligands. Diabetes. 2010;59:249–255.
  • 260. Yee KS. Wilkinson S. James J. Ryan KM. Vousden KH. PUMA- and Bax-induced autophagy contributes to apoptosis. Cell Death Differ. 2009;16:1135–1145.
  • 261. Yen WL. Klionsky DJ. How to live long and prosper: autophagy, mitochondria, and aging. Physiology (Bethesda) 2008;23:248–262.[PubMed]
  • 262. Yin YX. Yao YM. Liu RM. Zhai HX. Li L. Zhang JJ. Chen HW. Wang L. Li N. Xia YF. [The effect of simvastatin on the expression of high mobility group box-1 protein in atherosclerotic rats] Zhongguo Wei Zhong Bing Ji Jiu Yi Xue. 2010;22:306–308.[PubMed]
  • 263. Youn JH. Shin JS. Nucleocytoplasmic shuttling of HMGB1 is regulated by phosphorylation that redirects it toward secretion. J Immunol. 2006;177:7889–7897.[PubMed]
  • 264. Yu M. Wang H. Ding A. Golenbock DT. Latz E. Czura CJ. Fenton MJ. Tracey KJ. Yang H. HMGB1 signals through toll-like receptor (TLR) 4 and TLR2. Shock. 2006;26:174–179.[PubMed]
  • 265. Yu YM. Kim JB. Lee KW. Kim SY. Han PL. Lee JK. Inhibition of the cerebral ischemic injury by ethyl pyruvate with a wide therapeutic window. Stroke. 2005;36:2238–2243.[PubMed]
  • 266. Yuk JM. Yang CS. Shin DM. Kim KK. Lee SK. Song YJ. Lee HM. Cho CH. Jeon BH. Jo EK. A dual regulatory role of apurinic/apyrimidinic endonuclease 1/redox factor-1 in HMGB1-induced inflammatory responses. Antioxid Redox Signal. 2009;11:575–588.[PubMed]
  • 267. Yun N. Eum HA. Lee SM. Protective role of heme oxygenase-1 against liver damage caused by hepatic ischemia and reperfusion in rats. Antioxid Redox Signal. 2010;13:1503–1512.[PubMed]
  • 268. Zafarullah M. Li WQ. Sylvester J. Ahmad M. Molecular mechanisms of N-acetylcysteine actions. Cell Mol Life Sci. 2003;60:6–20.[PubMed]
  • 269. Zeh HJ., 3rd Lotze MT. Addicted to death: invasive cancer and the immune response to unscheduled cell death. J Immunother. 2005;28:1–9.[PubMed]
  • 270. Zeng S. Dun H. Ippagunta N. Rosario R. Zhang QY. Lefkowitch J. Yan SF. Schmidt AM. Emond JC. Receptor for advanced glycation end product (RAGE)-dependent modulation of early growth response-1 in hepatic ischemia/reperfusion injury. J Hepatol. 2009;50:929–936.[PubMed]
  • 271. Zhang CC. Krieg S. Shapiro DJ. HMG-1 stimulates estrogen response element binding by estrogen receptor from stably transfected HeLa cells. Mol Endocrinol. 1999;13:632–643.[PubMed]
  • 272. Zhang X. Wheeler D. Tang Y. Guo L. Shapiro RA. Ribar TJ. Means AR. Billiar TR. Angus DC. Rosengart MR. Calcium/calmodulin-dependent protein kinase (CaMK) IV mediates nucleocytoplasmic shuttling and release of HMGB1 during lipopolysaccharide stimulation of macrophages. J Immunol. 2008;181:5015–5023.
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