Erratum: The HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis (Journal of Clinical Investigation (2015)125:2 (539–550) DOI: 10.1172/JCI76887);The HMGB1/RAGE axis triggers neutrophil-mediated injury amplification following necrosis

Journal of Clinical Investigation

Volumn 125, Issue 2, 2015, Pages 539-550

  Huebener, Peter ^a   Pradere, Jean Philippe ^a   Hernandez, Celine ^a   Gwak, Geum Youn ^a   Caviglia, Jorge Matias ^a   Mu, Xueru ^a   Loike, John D ^a   Jenkins, Rosalind E ^b   Antoine, Daniel J ^b   Schwabe, Robert F ^a  

^a Och Spine at New York Presbyterian Hospitals   (United States)

^b UNIVERSITY OF LIVERPOOL   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FAS ANTIGEN; HIGH MOBILITY GROUP B1 PROTEIN; LEUKOCYTE ELASTASE; PARACETAMOL; TUMOR NECROSIS FACTOR; ADVANCED GLYCATION END PRODUCT RECEPTOR; ANALGESIC AGENT; FAS PROTEIN, MOUSE; HMGB1 PROTEIN, MOUSE; IMMUNOGLOBULIN RECEPTOR; LIPOPOLYSACCHARIDE; TUMOR NECROSIS FACTOR ALPHA;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL TISSUE; APOPTOSIS; ARTICLE; BONE MARROW; CELL DAMAGE; CELL DEATH; CELL SPECIFICITY; CELL SURVIVAL; CONTROLLED STUDY; EPITHELIUM CELL; INFLAMMATION; LETHALITY; LIVER CELL; MACROPHAGE; MORTALITY; MOUSE; NEUTROPHIL; NONHUMAN; PRIORITY JOURNAL; TISSUE NECROSIS; ANIMAL; CHEMICALLY INDUCED; GENETICS; KNOCKOUT MOUSE; METABOLISM; NECROSIS; NEUTROPHIL CHEMOTAXIS; PATHOLOGY; SEPTIC SHOCK; TOXIC HEPATITIS;

ACETAMINOPHEN; ADVANCED GLYCOSYLATION END PRODUCT-SPECIFIC RECEPTOR; ANALGESICS, NON-NARCOTIC; ANIMALS; ANTIGENS, CD95; DRUG-INDUCED LIVER INJURY; HEPATOCYTES; HMGB1 PROTEIN; INFLAMMATION; LEUKOCYTE ELASTASE; LIPOPOLYSACCHARIDES; MACROPHAGES; MICE; MICE, KNOCKOUT; NECROSIS; NEUTROPHIL INFILTRATION; NEUTROPHILS; RECEPTORS, IMMUNOLOGIC; SHOCK, SEPTIC; TUMOR NECROSIS FACTOR-ALPHA;

EID: 84948614431     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI126976     Document Type: Erratum

References (63)

1. Kono H, Rock KL. How dying cells alert the immune system to danger. Nat Rev Immunol. 2008;8(4):279-289.
2. Matzinger P. The danger model: a renewed sense of self. Science. 2002;296(5566):301-305.
3. Scaffidi P, Misteli T, Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature. 2002;418(6894):191-195.
4. Lotze MT, Tracey KJ. High-mobility group box 1 protein (HMGB1): nuclear weapon in the immune arsenal. Nat Rev Immunol. 2005;5(4):331-342.
5. Zitvogel L, Kepp O, Kroemer G. Decoding cell death signals in inflammation and immunity. Cell. 2010;140(6):798-804.
6. Chen GY, Nunez G. Sterile inflammation: sensing and reacting to damage. Nat Rev Immunol. 2010;10(12):826-837.
7. Kaczmarek A, Vandenabeele P, Krysko DV. Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity. 2013;38(2):209-223.
8. Broere F, van der Zee R, van Eden W. Heat shock proteins are no DAMPs, rather 'DAMPERs'. Nat Rev Immunol. 2011;11(8):565.
9. Bianchi ME. HMGB1 loves company. J Leukoc Biol. 2009;86(3):573-576.
10. Hreggvidsdottir HS, et al. The alarmin HMGB1 acts in synergy with endogenous and exogenous danger signals to promote inflammation. J Leukoc Biol. 2009;86(3):655-662.
11. Tsan MF. Heat shock proteins and high mobility group box 1 protein lack cytokine function. J Leukoc Biol. 2011;89(6):847-853.
12. Bald T, et al. Ultraviolet-radiation-induced inflammation promotes angiotropism and metastasis in melanoma. Nature. 2014;507(7490):109-113.
13. Wang H, et al. HMG-1 as a late mediator of endotoxin lethality in mice. Science. 1999;285(5425):248-251.
14. Bianchi ME, Agresti A. HMG proteins: dynamic players in gene regulation and differentiation. Curr Opin Genet Dev. 2005;15(5):496-506.
15. Calogero 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(3):276-280.
16. Huebener P, et al. High-mobility group box is dispensable for autophagy, mitochondrial quality control and organ function in vivo. Cell Metab. 2014;19(1):1-9.
17. Huang H, et al. Hepatocyte specific HMGB1 deletion worsens the injury in liver ischemia/reperfusion: A role for intracellular HMGB1 in cellular protection. Hepatology. 2014;59(5):1984-1997.
18. Yanai H, et al. Conditional ablation of HMGB1 in mice reveals its protective function against endotoxemia and bacterial infection. Proc Natl Acad Sci U S A. 2013;110(51):20699-20704.
19. Yang H, Antoine DJ, Andersson U, Tracey KJ. The many faces of HMGB1: molecular structure-functional activity in inflammation, apoptosis, and chemotaxis. J Leukoc Biol. 2013;93(6):865-873.
20. Venereau E, et al. Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J Exp Med. 2012;209(9):1519-1528.
21. Beutler B, Milsark IW, Cerami AC. Passive immunization against cachectin/tumor necrosis factor protects mice from lethal effect of endotoxin. Science. 1985;229(4716):869-871.
22. Tracey KJ, et al. Anti-cachectin/TNF monoclonal antibodies prevent septic shock during lethal bacteraemia. Nature. 1987;330(6149):662-664.
23. Ohlsson K, Bjork P, Bergenfeldt M, Hageman R, Thompson RC. Interleukin-1 receptor antagonist reduces mortality from endotoxin shock. Nature. 1990;348(6301):550-552.
24. Silva AT, Bayston KF, Cohen J. Prophylactic and therapeutic effects of a monoclonal antibody to tumor necrosis factor-alpha in experimental gram-negative shock. J Infect Dis. 1990;162(2):421-427.
25. Pasparakis M, Alexopoulou L, Episkopou V, Kollias G. Immune and inflammatory responses in TNFα-deficient mice: a critical requirement for TNFα in the formation of primary B cell follicles, follicular dendritic cell networks and germinal centers, and in the maturation of the humoral immune response. J Exp Med. 1996;184(4):1397-1411.
26. Rothe J, Mackay F, Bluethmann H, Zinkernagel R, Lesslauer W. Phenotypic analysis of TNFR1-deficient mice and characterization of TNFR1-deficient fibroblasts in vitro. Circ Shock. 1994;44(2):51-56.
27. Peschon JJ, et al. TNF receptor-deficient mice reveal divergent roles for p55 and p75 in several models of inflammation. J Immunol. 1998;160(2):943-952.
28. Fisher CJ, et al. Treatment of septic shock with the tumor necrosis factor receptor: Fc fusion protein. The Soluble TNF Receptor Sepsis Study Group. N Engl J Med. 1996;334(26):1697-1702.
29. Angus DC, van der Poll T. Severe sepsis and septic shock. N Engl J Med. 2013;369(9):840-851.
30. Kuhn R, Schwenk F, Aguet M, Rajewsky K. Inducible gene targeting in mice. Science. 1995;269(5229):1427-1429.
31. Yang H, et al. Reversing established sepsis with antagonists of endogenous high-mobility group box 1. Proc Natl Acad Sci U S A. 2004;101(1):296-301.
32. de Boer J, et al. Transgenic mice with hematopoietic and lymphoid specific expression of Cre. Eur J Immunol. 2003;33(2):314-325.
33. Georgiades P, et al. VavCre transgenic mice: a tool for mutagenesis in hematopoietic and endothelial lineages. Genesis. 2002;34(4):251-256.
34. Eltzschig HK, Eckle T. Ischemia and reperfusion - from mechanism to translation. Nat Med. 2011;17(11):1391-1401.
35. Antoine DJ, et al. Mechanistic biomarkers provide early and sensitive detection of acetaminopheninduced acute liver injury at first presentation to hospital. Hepatology. 2013;58(2):777-787.
36. Bernal W, Wendon J. Acute liver failure. N Engl J Med. 2013;369(26):2525-2534.
37. Heard KJ. Acetylcysteine for acetaminophen poisoning. N Engl J Med. 2008;359(3):285-292.
38. Bonaldi T, et al. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J. 2003;22(20):5551-5560.
39. Ge X, et al. High mobility group box-1 (HMGB1) participates in the pathogenesis of alcoholic liver disease (ALD). J Biol Chem. 2014;289(33):22672-22691.
40. Antoine DJ, Harris HE, Andersson U, Tracey KJ, Bianchi ME. A systematic nomenclature for the redox states of high mobility group box (HMGB) proteins. Mol Med. 2014;20:135-137.
41. Andersson U, Tracey KJ. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu Rev Immunol. 2011;29:139-162.
42. Belaaouaj A, et al. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat Med. 1998;4(5):615-618.
43. Mollica L, et al. Glycyrrhizin binds to high-mobility group box 1 protein and inhibits its cytokine activities. Chem Biol. 2007;14(4):431-441.
44. Manns MP, et al. Glycyrrhizin in patients who failed previous interferon alpha-based therapies: biochemical and histological effects after 52 weeks. J Viral Hepat. 2012;19(8):537-546.
45. Zigmond E, et al. Infiltrating monocyte-derived macrophages and resident kupffer cells display different ontogeny and functions in acute liver injury. J Immunol. 2014;193(1):344-353.
46. Kessenbrock K, et al. Proteinase 3 and neutrophil elastase enhance inflammation in mice by inactivating antiinflammatory progranulin. J Clin Invest. 2008;118(7):2438-2447.
47. Neumann K, et al. Clec12a is an inhibitory receptor for uric acid crystals that regulates inflammation in response to cell death. Immunity. 2014;40(3):389-399.
48. Yipp BG, et al. Infection-induced NETosis is a dynamic process involving neutrophil multitasking in vivo. Nat Med. 2012;18(9):1386-1393.
49. Kang R, et al. Intracellular Hmgb1 inhibits inflammatory nucleosome release and limits acute pancreatitis in mice. Gastroenterology. 2014;146(4):1097-1107.
50. McDonald B, et al. Intravascular danger signals guide neutrophils to sites of sterile inflammation. Science. 2010;330(6002):362-366.
51. Yamasaki S, Ishikawa E, Sakuma M, Hara H, Ogata K, Saito T. Mincle is an ITAM-coupled activating receptor that senses damaged cells. Nat Immunol. 2008;9(10):1179-1188.
52. Nystrom S, et al. TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. EMBO J. 2013;32(1):86-99.
53. Tsung A, et al. The nuclear factor HMGB1 mediates hepatic injury after murine liver ischemia-reperfusion. J Exp Med. 2005;201(7):1135-1143.
54. Seki E, et al. TLR4 enhances TGF-β signaling and hepatic fibrosis. Nat Med. 2007;13(11):1324-1332.
55. Pusterla T, et al. Receptor for advanced glycation endproducts (RAGE) is a key regulator of oval cell activation and inflammation-associated liver carcinogenesis in mice. Hepatology. 2013;58(1):363-373.
56. Li Y, Karlin A, Loike JD, Silverstein SC. A critical concentration of neutrophils is required for effective bacterial killing in suspension. Proc Natl Acad Sci U S A. 2002;99(12):8289-8294.
57. Swamydas M, Lionakis MS. Isolation, purification and labeling of mouse bone marrow neutrophils for functional studies and adoptive transfer experiments. J Vis. 2013; Exp (77): e50586.
58. Davis BK. Isolation, culture, and functional evaluation of bone marrow-derived macrophages. Methods Mol Biol. 2013;1031:27-35.
59. Dapito DH, et al. Promotion of hepatocellular carcinoma by the intestinal microbiota and TLR4. Cancer Cell. 2012;21(4):504-516.
60. Mederacke I, et al. Fate tracing reveals hepatic stellate cells as dominant contributors to liver fibrosis independent of its aetiology. Nat Commun. 2013;4:2823.
61. Antoine DJ, et al. High-mobility group box-1 protein and keratin-18, circulating serum proteins informative of acetaminophen-induced necrosis and apoptosis in vivo. Toxicol Sci. 2009;112(2):521-531.
62. Yang H, et al. Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Mol Med. 2012;18:250-259.
63. Antoine DJ, et al. Molecular forms of HMGB1 and keratin-18 as mechanistic biomarkers for mode of cell death and prognosis during clinical acetaminophen hepatotoxicity. J Hepatol. 2012;56(5):1070-1079.