The expression of HMGB1 on microparticles released during cell activation and cell death in vitro and in vivo

Molecular Medicine

Volumn 20, Issue 1, 2014, Pages 158-163

  Pisetsky, David S ^a,b  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b DURHAM VA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGICAL MARKER; CYSTEINE; HIGH MOBILITY GROUP B1 PROTEIN; INTERLEUKIN 1; LIPOPOLYSACCHARIDE; POLYINOSINIC POLYCYTIDYLIC ACID;

ACETYLATION; APOPTOSIS; ARTICLE; AUTOIMMUNE DISEASE; CELL ACTIVATION; CELL DEATH; CELL MEMBRANE PERMEABILITY; CYTOKINE PRODUCTION; EXTRACELLULAR SPACE; HUMAN; IMMUNITY; IMMUNOGENICITY; IMMUNOPATHOGENESIS; IN VITRO STUDY; IN VIVO STUDY; INFLAMMATION; MEMBRANE MICROPARTICLE; NONHUMAN; NUCLEAR LOCALIZATION SIGNAL; PARTICLE SIZE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; PROTEIN PROTEIN INTERACTION; PROTEIN SECRETION; PROTEIN STRUCTURE; PROTEIN TRANSPORT; PYROPTOSIS; SIGNAL TRANSDUCTION;

ANIMALS; ANTINEOPLASTIC AGENTS; CELL DEATH; CELL LINE, TUMOR; CELL-DERIVED MICROPARTICLES; HMGB PROTEINS; HUMANS; IMMUNITY, INNATE; MACROPHAGES; MICE;

EID: 84898725886     PISSN: 10761551     EISSN: None     Source Type: Journal    
DOI: 10.2119/molmed.2014.00014     Document Type: Article

References (55)

1. Harris HE, Andersson U, Pisetsky DS. (2012) HMGB1: a multifunctional alarmin driving autoimmune and inflammatory disease. Nat. Rev. Rheumatol. 8:195-202.
2. Yang H, Antoine DJ, Andersson U, Tracey KJ. (2013) The many faces of HMGB1: a molecular structure-functional activity in inflammation, apoptosis, and chemotaxis. J. Leukoc. Biol. 93:865-73.
3. Štros M. (2010) HMGB proteins: interactions with DNA and chromatin. Biochim. Biophys. Acta. 1799:101-13.
4. Thomas JO, Stott K. (2012) H1 and HMGB1: modulators of chromatin structure. Biochem. Soc. Trans. 40:341-6.
5. Wang H, et al. (1999) HMG-1 as a late mediator of endotoxin lethality in mice. Science. 285:248-51.
6. Andersson U, Tracey KJ. (2011) HMGB1 is a therapeutic target for sterile inflammation and infection. Annu. Rev. Immunol. 29:139-62.
7. Venereau E, et al. (2012) Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J. Exp. Med. 209:1519-28.
8. Yang H, et al. (2012) Redox modification of cysteine residues regulates the cytokine activity of high mobility group box-1 (HMGB1). Mol. Med. 18:250-9.
9. Venereau E, Schiraldi M, Uguccioni M, Bianchi ME. (2013) HMGB1 and leukocyte migration during trauma and sterile inflammation. Mol. Immunol. 55:76-82.
10. Gardella S, et al. (2002) The nuclear protein HMGB1 is secreted by monocytes via a nonclassical, vesicle-mediated secretory pathway. EMBO Rep. 3:995-1001.
11. Scaffidi P, Misteli T, Bianchi ME. (2002) Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature. 418:191-5.
12. Bonaldi T, et al. (2003) Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J. 22:5551-60.
13. Rovere-Querini P, et al. (2004) HMGB1 is an endogenous immune adjuvant released by necrotic cells. EMBO Rep. 5:825-30.
14. Lu B, et al. (2014) JAK/STAT1 signaling promotes HMGB1 hyperacetylation and nuclear translocation. Proc. Natl. Acad. Sci. U. S. A. 111:3068-73.
15. Miao EA, Rajan JV, Aderem A. (2011) Caspase-1-induced pyroptotic cell death. Immunol. Rev. 243:206-14.
16. Lamkanfi M, et al. (2010) Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia. J. Immunol. 185:4385-92.
17. Nyström S, et al. (2013) TLR activation regulates damage-associated molecular pattern isoforms released during pyroptosis. EMBO J. 32:86-99.
18. Duprez L, et al. (2011) RIP kinase-dependent necrosis drives lethal systemic inflammatory response syndrome. Immunity. 35:908-18.
19. Galluzzi L, et al. (2012) Molecular definitions of cell death subroutines: recommendations of the Nomenclature Committee on Cell Death 2012. Cell Death Differ. 19:107-20.
20. Kaczmarek A, Vandenabeele P, Krysko DV. (2013) Necroptosis: the release of damage-associated molecular patterns and its physiological relevance. Immunity. 38:209-23.
21. Linkermann A, Green DR. (2014) Necroptosis. N. Engl. J. Med. 370:455-65.
22. Beyer C, et al. (2012) The extracellular release of DNA and HMGB1 from Jurkat T cells during in vitro necrotic cell death. Innate Immun. 18:727-37.
23. Bell CW, Jiang W, Reich CF 3rd, Pisetsky DS. (2006) The extracellular release of HMGB1 during apoptotic cell death. Am. J. Physiol. Cell Physiol. 291:C1318-25.
24. Kazama H, Ricci J-E, Herndon HM, Hoppe G, Green DR. (2008) Induction of immunological tolerance by apoptotic cells requires caspase-dependent oxidation of high-mobility group box-1 protein. Immunity. 29:21-32.
25. Urbonaviciute V, et al. (2009) Oxidation of the alarmin high-mobility group box 1 protein (HMGB1) during apoptosis. Autoimmunity. 42:305-7.
26. Ditsworth D, Zong WX, Thompson CB. (2007) Activation of poly(ADP)-ribose polymerase (PARP-1) induces release of the pro-inflammatory mediator HMGB1 from the nucleus. J. Biol. Chem. 282:17845-54.
27. Kennedy CL, Smith DJ, Lyras D, Chakravorty A, Rood JI. (2009) Programmed cellular necrosis mediated by the pore-forming b-Toxin from Clostridium septicum. PLoS Pathog. 5:e1000516.
28. Morinaga Y, et al. (2010) Legionella pneumophilia induces cathepsin B-dependent necrotic cell death with releasing high mobility group box 1 in macrophages. Respir. Res. 11:158-66.
29. Lau A, et al. (2013) RIPK3-mediated necroptosis promotes donor kidney inflammatory injury and reduces allograft survival. Am. J. Transplant. 13:2805-18.
30. Inoue H, Tani K. (2014) Multimodal immunogenic cancer cell death as a consequence of anticancer cytotoxic treatments. Cell Death Differ. 21:39-49.
31. Jiang N, Reich CF 3rd, Pisetsky DS. (2003) Role of macrophages in the generation of circulating blood nucleosomes from dead and dying cells. Blood. 102:2243-50.
32. György B, et al. (2011) Membrane vesicles, current state-of-the art: emerging role of extracellular vesicles. Cell. Mol. Life Sci. 68:2667-88.
33. Van der Pol E, Böing AN, Harrison P, Sturk A, Nieuwland R. (2012) Classification, functions, and clinical relevance of extracellular vesicles. Pharmacol. Rev. 64:676-705.
34. Shifrin DA Jr., Becckler MD, Coffey RJ, Tyska MJ. (2013) Extracellular vesicles: communication, coercion, and conditioning. Mol. Biol. Cell. 24:1253-9.
35. Charras GT. (2008) A short history of blebbing. J. Microsc. 231:466-78.
36. Charras GT, Coughlin M, Mitchison TJ, Mahadevan L. (2008) Life and times of a cellular bleb. Biophys. J. 94:1836-53.
37. Berda-Haddad Y, et al. (2011) Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin-1i. Proc. Natl. Acad. Sci. U. S. A. 108:20684-9.
38. Casciola-Rosen LA, Anhalt G, Rosen A. (1994) Autoantigens targeted in systemic lupus erythematosus are clustered in two populations of surface structures on apoptotic keratinocytes. J. Exp. Med. 179:1317-30.
39. Schiller M, et al. (2008) Autoantigens are translocated into small apoptotic bodies during early stages of apoptosis. Cell Death Differ. 15:183-91.
40. Orozco AF, Lewis DE. (2010) Flow cytometric analysis of circulating microparticles in plasma. Cytometry A. 77:502-14.
41. Pisetsky DS, Ullal AJ, Gauley J, Ning TC. (2012) Microparticles as mediators and biomarkers of rheumatic disease. Rheumatology (Oxford). 51:1737-46.
42. Reich CF 3rd, Pisetsky DS. (2009) The content of DNA and RNA in microparticles released by Jurkat and HL-60 cells undergoing in vitro apoptosis. Exp. Cell Res. 315:760-8.
43. Ullal AJ, Pisetsky DS, Reich CF 3rd. (2010) Use of SYTO 13, a fluorescent dye binding nucleic acids, for the detection of microparticles in in vitro systems. Cytometry A. 77:294-301.
44. Pisetsky DS. (2013) The translocation of nuclear molecules during inflammation and cell death. Antioxid. Redox Signal. 20:1117-25.
45. Jiang W, Li J, Gallowitsch-Puerta M, Tracey KJ, Pisetsky DS. (2005) The effects of CpG DNA on HMGB1 release by murine macrophage cell lines. J. Leukoc. Biol. 78:930-6.
46. Jiang W, Pisetsky DS. (2006) The role of IFNalpha and nitric oxide in the release of HMGB1 by RAW 264.7 cells stimulated with polyinosinicpolycytidylic acid or lipopolysaccharide. J. Immunol. 177:3337-43.
47. Jiang W, Bell CW, Pisetsky DS. (2007) The relationship between apoptosis and high-mobility group protein 1 release from murine macrophages stimulated with lipopolysaccharide or polyinosinicpolycytidylic acid. J. Immunol. 178:6495-503.
48. Gauley J, Pisetsky DS. (2010) The release of micro-particles by RAW 264.7 macrophage cells stimulated with TLR ligands. J. Leukoc. Biol. 87:1115-23.
49. Spencer DM, Gauley J, Pisetsky DS. (2014) The properties of microparticles from RAW 264.7 macrophage cells undergoing in vitro activation or apoptosis. Innate Immun. 20:239-48.
50. Soop A, et al. (2013) Effect of lipopolysaccharide administration on the number, phenotype and content of nuclear molecules in blood microparticles of normal human subjects. Scand. J. Immunol. 78:205-13.
51. Hallström L, Berghäll E, Frostell C, Sollevi A, Soop AL. (2011) Immunomodulation by a combination of nitric oxide and glucocorticoids in a human endotoxin model. Acta. Anaesthesiol. Scand. 55:20-7.
52. Rouhiainen A, Imai S, Rauvala H, Parkkinen J. (2000) Occurrence of amphoterin (HMG1) as an endogenous protein of human platelets that is exported to the cell surface upon platelet activation. Thromb. Haemost. 84:1087-94.
53. Maugeri N, et al. (2012) Circulating platelets as a source of the damage-associated molecular pattern HMGB1 in patients with systemic sclerosis. Autoimmunity. 45:584-7.
54. Hreggvidsdottir HS, et al. (2009) The alarmin HMGB1 acts in synergy with endogenous and exogenous danger signals to promote inflammation. J. Leukoc. Biol. 86:655-62.
55. Leclerc P, et al. (2013) IL-1./HMGB1 complexes promote the PGE2 biosynthesis pathway in synovial fibroblasts. Scand J. Immunol. 77:350-60.