HMGB1 release by inflammasomes

References

• Goodwin GH, Sanders C, Johns EW. A new group of chromatin-associated proteins with a high content of acidic and basic amino acids. Eur J Biochem 1973; 38:14 - 19
   PubMedGoogle Scholar
• Hardman CH, Broadhurst RW, Raine AR, Grasser KD, Thomas JO, Laue ED. Structure of the A-domain of HMG1 and its interaction with DNA as studied by heteronuclear three- and four-dimensional NMR spectroscopy. Biochemistry 1995; 34:16596 - 16607
   PubMed Web of Science ®Google Scholar
• Weir HM, Kraulis PJ, Hill CS, Raine AR, Laue ED, Thomas JO. Structure of the HMG box motif in the B-domain of HMG1. EMBO J 1993; 12:1311 - 1319
   PubMed Web of Science ®Google Scholar
• Lotze MT, Tracey KJ. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nature Rev Immunol 2005; 5:331 - 342
   PubMed Web of Science ®Google Scholar
• Prendergast P, Onate SA, Christensen K, Edwards DP. Nuclear accessory factors enhance the binding of progesterone receptor to specific target DNA. J Steroid Biochem Mol Biol 1994; 48:1 - 13
   PubMed Web of Science ®Google Scholar
• 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 Web of Science ®Google Scholar
• Bustin M. Regulation of DNA-dependent activities by the functional motifs of the high-mobility-group chromosomal proteins. Mol Cell Biol 1999; 19:5237 - 5246
   PubMed Web of Science ®Google Scholar
• Calogero S, Grassi F, Aguzzi A, Voigtlander T, Ferrier P, Ferrari S, et al. 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 Web of Science ®Google Scholar
• Wang H, Bloom O, Zhang M, Vishnubhakat JM, Ombrellino M, Che J, et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science 1999; 285:248 - 251
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Sarkar A, Vande Walle L, Vitari AC, Amer AO, Wewers MD, et al. Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia. J Immunol 2010; 185:4385 - 4392
   PubMed Web of Science ®Google Scholar
• Yang H, Ochani M, Li J, Qiang X, Tanovic M, Harris HE, 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
• Suda K, Kitagawa Y, Ozawa S, Saikawa Y, Ueda M, Ebina M, et al. Anti-high-mobility group box chromosomal protein 1 antibodies improve survival of rats with sepsis. World J Surg 2006; 30:1755 - 1762
   PubMed Web of Science ®Google Scholar
• Sunden-Cullberg J, Norrby-Teglund A, Rouhiainen A, Rauvala H, Herman G, Tracey KJ, et al. Persistent elevation of high mobility group box-1 protein (HMGB1) in patients with severe sepsis and septic shock. Crit Care Med 2005; 33:564 - 573
   PubMed Web of Science ®Google Scholar
• Levy RM, Mollen KP, Prince JM, Kaczorowski DJ, Vallabhaneni R, Liu S, et al. Systemic inflammation and remote organ injury following trauma require HMGB1. Am J Physiol Regul Integr Comp Physiol 2007; 293:R1538 - R1544
   PubMed Web of Science ®Google Scholar
• Tsung A, Sahai R, Tanaka H, Nakao A, Fink MP, Lotze MT, et al. The nuclear factor HMGB1 mediates hepatic injury after murine liver ischemia-reperfusion. J Exp Med 2005; 201:1135 - 1143
   PubMed Web of Science ®Google Scholar
• Goldstein RS, Gallowitsch-Puerta M, Yang L, Rosas-Ballina M, Huston JM, Czura CJ, et al. Elevated high-mobility group box 1 levels in patients with cerebral and myocardial ischemia. Shock 2006; 25:571 - 574
   PubMed Web of Science ®Google Scholar
• Faraco G, Fossati S, Bianchi ME, Patrone M, Pedrazzi M, Sparatore B, et al. High mobility group box 1 protein is released by neural cells upon different stresses and worsens ischemic neurodegeneration in vitro and in vivo. J Neurochem 2007; 103:590 - 603
   PubMed Web of Science ®Google Scholar
• 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 Web of Science ®Google Scholar
• Kohno T, Anzai T, Naito K, Miyasho T, Okamoto M, Yokota H, et al. Role of high-mobility group box 1 protein in post-infarction healing process and left ventricular remodelling. Cardiovasc Res 2009; 81:565 - 573
   PubMed Web of Science ®Google Scholar
• Kokkola R, Sundberg E, Ulfgren AK, Palmblad K, Li J, Wang H, et al. High mobility group box chromosomal protein 1: a novel proinflammatory mediator in synovitis. Arthritis Rheum 2002; 46:2598 - 2603
   PubMed Web of Science ®Google Scholar
• Taniguchi N, Kawahara K, Yone K, Hashiguchi T, Yamakuchi M, Goto M, et al. 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 Web of Science ®Google Scholar
• 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 Web of Science ®Google Scholar
• Blanco P, Palucka AK, Pascual V, Banchereau J. Dendritic cells and cytokines in human inflammatory and autoimmune diseases. Cytokine Growth Factor Rev 2008; 19:41 - 52
   PubMed Web of Science ®Google Scholar
• Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol 1994; 12:991 - 1045
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Dixit VM. IL-33 raises alarm. Immunity 2009; 31:5 - 7
   PubMed Web of Science ®Google Scholar
• Kokkola R, Andersson A, Mullins G, Ostberg T, Treutiger CJ, Arnold B, et al. RAGE is the major receptor for the proinflammatory activity of HMGB1 in rodent macrophages. Scand J Immunol 2005; 61:1 - 9
   PubMed Web of Science ®Google Scholar
• Dumitriu IE, Baruah P, Valentinis B, Voll RE, Herrmann M, Nawroth PP, et al. Release of high mobility group box 1 by dendritic cells controls T cell activation via the receptor for advanced glycation end products. J Immunol 2005; 174:7506 - 7515
   PubMed Web of Science ®Google Scholar
• Wang H, Yang H, Tracey KJ. Extracellular role of HMGB1 in inflammation and sepsis. J Intern Med 2004; 255:320 - 331
   PubMed Web of Science ®Google Scholar
• Li J, Wang H, Mason JM, Levine J, Yu M, Ulloa L, et al. Recombinant HMGB1 with cytokine-stimulating activity. J Immunol Methods 2004; 289:211 - 223
   PubMed Web of Science ®Google Scholar
• Rouhiainen A, Tumova S, Valmu L, Kalkkinen N, Rauvala H. Pivotal advance: analysis of proinflammatory activity of highly purified eukaryotic recombinant HMGB1 (amphoterin). J Leukoc Biol 2007; 81:49 - 58
   PubMed Web of Science ®Google Scholar
• Tian J, Avalos AM, Mao SY, Chen B, Senthil K, Wu H, et al. Toll-like receptor 9-dependent activation by DNA-containing immune complexes is mediated by HMGB1 and RAGE. Nat Immunol 2007; 8:487 - 496
   PubMed Web of Science ®Google Scholar
• van Zoelen MA, Yang H, Florquin S, Meijers JC, Akira S, Arnold B, Nawroth PP, et al. Role of toll-like receptors 2 and 4, and the receptor for advanced glycation end products in high-mobility group box 1-induced inflammation in vivo. Shock 2009; 31:280 - 284
   PubMed Web of Science ®Google Scholar
• Park JS, Gamboni-Robertson F, He Q, Svetkauskaite D, Kim JY, Strassheim D, Sohn JW, et al. High mobility group box 1 protein interacts with multiple Toll-like receptors. Am J Physiol Cell Physiol 2006; 290:C917 - C924
   PubMed Web of Science ®Google Scholar
• Park JS, Svetkauskaite D, He Q, Kim JY, Strassheim D, Ishizaka A, et al. Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein. J Biol Chem 2004; 279:7370 - 7377
   PubMed Web of Science ®Google Scholar
• Lee MC, Miller EA, Goldberg J, Orci L, Schekman R. Bi-directional protein transport between the ER and Golgi. Annu Rev Cell Dev Biol 2004; 20:87 - 123
   PubMed Web of Science ®Google Scholar
• Trombetta ES, Parodi AJ. Quality control and protein folding in the secretory pathway. Annu Rev Cell Dev Biol 2003; 19:649 - 676
   PubMed Web of Science ®Google Scholar
• Nickel W, Rabouille C. Mechanisms of regulated unconventional protein secretion. Nature Rev Mol Cell Biol 2009; 10:148 - 155
   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 - 195
   PubMed Web of Science ®Google Scholar
• Rubartelli A, Cozzolino F, Talio M, Sitia R. A novel secretory pathway for interleukin-1 beta, a protein lacking a signal sequence. EMBO J 1990; 9:1503 - 1510
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Dixit VM. Inflammasomes: guardians of cytosolic sanctity. Immunol Rev 2009; 227:95 - 105
   PubMed Web of Science ®Google Scholar
• Kanneganti TD, Lamkanfi M, Nunez G. Intracellular NOD-like receptors in host defense and disease. Immunity 2007; 27:549 - 559
   PubMed Web of Science ®Google Scholar
• O'Neill LA, Bowie AG. Sensing and signaling in antiviral innate immunity. Curr Biol 2010; 20:R328 - R333
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Dixit VM. The inflammasomes. PLoS Pathog 2009; 5:e1000510
   PubMed Web of Science ®Google Scholar
• Mariathasan S, Weiss DS, Newton K, McBride J, O'Rourke K, Roose-Girma M, et al. Cryopyrin activates the inflammasome in response to toxins and ATP. Nature 2006; 440:228 - 232
   PubMed Web of Science ®Google Scholar
• Munoz-Planillo R, Franchi L, Miller LS, Nunez G. A critical role for hemolysins and bacterial lipoproteins in Staphylococcus aureus-induced activation of the Nlrp3 inflammasome. J Immunol 2009; 183:3942 - 3948
   Google Scholar
• Willingham SB, Allen IC, Bergstralh DT, Brickey WJ, Huang MT, Taxman DJ, et al. NLRP3 (NALP3, Cryopyrin) facilitates in vivo caspase-1 activation, necrosis, and HMGB1 release via inflammasome-dependent and -independent pathways. J Immunol 2009; 183:2008 - 2015
   PubMed Web of Science ®Google Scholar
• Keller M, Ruegg A, Werner S, Beer HD. Active caspase-1 is a regulator of unconventional protein secretion. Cell 2008; 132:818 - 831
   PubMed Web of Science ®Google Scholar
• Becker CE, Creagh EM, O'Neill LA. Rab39a binds caspase-1 and is required for caspase-1-dependent interleukin-1beta secretion. J Biol Chem 2009; 284:34531 - 34537
   PubMed Web of Science ®Google Scholar
• Lamkanfi M, Dixit VM. Manipulation of host cell death pathways during microbial infections. Cell Host Microbe 2010; 8:44 - 54
   PubMed Web of Science ®Google Scholar
• Lamkanfi M. Emerging inf lammasome effector mechanisms. Nat Rev Immunol 2011; 11:213 - 220
   PubMed Web of Science ®Google Scholar
• Rovere-Querini P, Capobianco A, Scaffidi P, Valentinis B, Catalanotti F, Giazzon M, et al. HMGB1 is an endogenous immune adjuvant released by necrotic cells. EMBO Rep 2004; 5:825 - 830
   PubMed Web of Science ®Google Scholar