The Expression of HMGB1 on Microparticles from Jurkat and HL-60 Cells Undergoing Apoptosis in vitro

Scandinavian Journal of Immunology

Volumn 80, Issue 2, 2014, Pages 101-110

  Spencer, D M ^a   Mobarrez, F ^b   Wallen H ^b   Pisetsky, D S ^a,c  

^a DUKE UNIVERSITY MEDICAL CENTER   (United States)

^b DANDERYD HOSPITAL   (Sweden)

^c DURHAM VA MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ETOPOSIDE; HIGH MOBILITY GROUP B1 PROTEIN; STAUROSPORINE;

APOPTOSIS; ARTICLE; CONTROLLED STUDY; FLOW CYTOMETRY; FREEZE THAWING; HL 60 CELL LINE; HUMAN; HUMAN CELL; IN VITRO STUDY; JURKAT CELL LINE; MEMBRANE MICROPARTICLE; NECROSIS; PRIORITY JOURNAL; PROTEIN EXPRESSION; WESTERN BLOTTING;

ANTIBODIES, MONOCLONAL; ANTINEOPLASTIC AGENTS, PHYTOGENIC; APOPTOSIS; CELL LINE, TUMOR; CELL-DERIVED MICROPARTICLES; ENZYME INHIBITORS; ETOPOSIDE; HL-60 CELLS; HMGB1 PROTEIN; HUMANS; JURKAT CELLS; PROTEIN TRANSPORT; STAUROSPORINE;

EID: 84903895909     PISSN: 03009475     EISSN: 13653083     Source Type: Journal    
DOI: 10.1111/sji.12191     Document Type: Article

References (42)

1. Andersson U, Tracey KJ. HMGB1 is a therapeutic target for sterile inflammation and infection. Annu Rev Immunol 2011;29:139-62.
2. Harris HE, Andersson U, Pisetsky DS. HMGB1: a multifunctional alarmin driving autoimmune and inflammatory disease. Nat Rev Rheumatol 2012;8:195-202.
3. Štros M. HMGB proteins: interactions with DNA and chromatin. Biochim Biophys Acta 2010;1799:101-13.
4. Thomas JO, Stott K. H1 and HMGB1: modulators of chromatin structure. Biochem Soc Trans 2012;40:341-6.
5. Scaffidi P, Misteli T, Bianchi ME. Release of chromatin protein HMGB1 by necrotic cells triggers inflammation. Nature 2002;418:191-5.
6. Bonaldi T, Talamo F, Scaffidi P et al. Monocytic cells hyperacetylate chromatin protein HMGB1 to redirect it towards secretion. EMBO J 2003;22:5551-60.
7. 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.
8. Venereau E, Casalgrandi M, Schiraldi M et al. Mutually exclusive redox forms of HMGB1 promote cell recruitment or proinflammatory cytokine release. J Exp Med 2012;209:1519-28.
9. 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;93:1-9.
10. Park JS, Svetkauskaite D, He Q et al. Involvement of toll-like receptors 2 and 4 in cellular activation by high mobility group box 1 protein. J Biol Chem 2004;279:7370-7.
11. Yang H, Hreggvidsdottir HS, Palmblad K et al. 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;107:11942-7.
12. Wähämaa H, Schierbeck H, Hreggvidsdottir HS et al. High mobility group box protein 1 in complex with lipopolysaccharide or IL-1 promotes an increased inflammatory phenotype in synovial fibroblasts. Arthritis Res Ther 2011;13:R136.
13. Hreggvidsdottir HS, Lundbert AM, Aveberger AC, Klevenvall L, Andersoon U, Harris HE. High mobility group box protein 1 (HMGB1)-partner molecule complexes enhance cytokine production by signaling through the partner molecule receptor. Mol Med 2012;18:224-30.
14. 2 biosynthesis pathway in synovial fibroblasts. Scand J Immunol 2013;77:350-60.
15. Tran TT, Groben P, Pisetsky DS. The release of DNA into the plasma of mice following hepatic cell death by apoptosis and necrosis. Biomarkers 2008;13:184-200.
16. Kutcher ME, Xu J, Vilardi RF, Ho C, Esmon CT, Cohen MJ. Extracellular histone release in response to traumatic injury: implications for a compensatory role of activated protein C. J Trauma Acute Care Surg 2012;73:1389-94.
17. Antoine DJ, Jenkins RE, Dear JW 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;56:1070-9.
18. Bell CW, Jiang W, Reich CF III, Pisetsky DS. The extracellular release of HMGB1 during apoptotic cell death. Am J Physiol Cell Physiol 2006;29:C1318-25.
19. Lamkanfi M, Sarkar A, Walle LV et al. Inflammasome-dependent release of the alarmin HMGB1 in endotoxemia. J Immunol 2010;185:4385-92.
20. Garcia-Romo GS, Caielli S, Vega B et al. Netting neutrophils are major inducers of type I IFN production in pediatric systemic lupus erythematosus. Sci Transl Med 2011;3:73ra20.
21. Beyer C, Stearns NA, Giessl A, Distler JH, Schett G, Pisetsky DS. The extracellular release of DNA and HMGB1 from Jurkat T cells during in vitro necrotic cell death. Innate Immun 2012;18:727-37.
22. György B, Szabó TG, Pásztói M et al. Membrane vesicles, current state-of-the art: emerging role of extracellular vesicles. Cell Mol Life Sci 2011;68:2667-88.
23. Pisetsky DS, Ullal AL, Gauley J, Ning TC. Microparticles as mediators and biomarkers of rheumatic disease. Rheumatology (Oxford) 2012;51:1737-46.
24. Reich CF III, Pisetsky DS. The content of DNA and RNA in microparticles released by Jurkat and HL-60 cells undergoing in vitro apoptosis. Exp Cell Res 2009;315:760-8.
25. Ullal AJ, Reich CF III, Clowse M et al. Microparticles as antigenic targets of antibodies to DNA and nucleosomes in systemic lupus erythematosus. J Immunol 2011;36:173-80.
26. Schiller M, Bekeredijian-Ding I, Heyder P, Blank N, Ho AD, Lorenz HM. Autoantigens are translocated into small apoptotic bodies during early stages of apoptosis. Cell Death Differ 2008;15:183-91.
27. Suber T, Rosen A. Apoptotic cell blebs: repositories of autoantigens and contributors to immune context. Arthritis Rheum 2009;60:2216-9.
28. Lane JD, Allan VJ, Woodman PG. Active relocation of chromatin and endoplasmic reticulum into blebs in late apoptotic cells. J Cell Sci 2005;118:4059-71.
29. Charras GT. A short history of blebbing. J Microsc 2008;231:466-78.
30. Charras GT, Coughlin M, Mitchison TJ, Mahadevan L. Life and times of a cellular bleb. Biophys J 2008;94:1836-53.
31. Schiller M, Heyder P, Ziegler S et al. During apoptosis HMGB1 is translocated into apoptotic cell-derived membraneous vesicles. Autoimmunity 2013;46:342-6.
32. Seifert JK, France MP, Zhao J et al. Large volume hepatic freezing: association with significant release of the cytokines interleukin-6 and tumor necrosis factor a in a rat model. World J Surg 2002;26:1333-41.
33. Casiano CA, Ochs RL, Tan EM. Distinct cleavage products of nuclear proteins in apoptosis and necrosis revealed by autoantibody probes. Cell Death Differ 1998;5:183-90.
34. Sparatore B, Patrone M, Passalacqua M et al. Extracellular processing of amphoterin generates a peptide active on erythroleukaemia cell differentiation. Biochem J 2001;357:569-74.
35. Ito T, Kawahara K, Okamoto K et al. Proteolytic cleavage of high mobility group box 1protein by thrombin-thrombomodulin complexes. Arterioscler Thromb Vasc Biol 2008;28:1825-30.
36. Leblanc PM, Doggett TA, Choi J et al. An immunogenic peptide in the A-box of HMGB1 protein reverses apoptosis-induced tolerance through RAGE receptor. J Biol Chem 2014;289:7777-86.
37. Soop A, Hällström L, Frostell C, Wällén H, Mobarrez F, Pisetsky DS. Effect of lipopolysaccharide administration on the number, phenotype and content of nuclear molecules in blood microparticles of normal human subjects. Scand J Immunol 2013;78:205-13.
38. Dragovic RA, Gardiner C, Brooks AS et al. Sizing and phenotyping of cellular vesicles using nanoparticle tracing analysis. Nanomedicine 2011;7:780-8.
39. Ullal AJ, Pisetsky DS, Reich CF III. Use of SYTO 13, a fluorescent dye binding nucleic acids, for the detection of microparticles in in vitro systems. Cytometry A 2010;77:294-301.
40. MacKenzie A, Wilson HL, Kiss-Toth E, Dower S, North RA, Surprenant A. Rapid secretion of interleukin-1beta by microvesicle shedding. Immunity 2001;15:825-35.
41. Berda-Haddad Y, Robert S, Salers P et al. Sterile inflammation of endothelial cell-derived apoptotic bodies is mediated by interleukin 1a{script}. Proc Natl Acad Sci U S A 2011;108:20684-9.
42. Wang JG, Williams JC, Davis BK et al. Monocytic microparticles activate endothelial cells in an IL-1β-dependent manner. Blood 2011;118:2366-74.