Role of apoptosis failure in etiopathogenesis of systemic lupus erythematosus and murine lupus

References

• van Zandbergen G, Bollinger A, Wenzel A et al. Leishmania disease development depends on the presence of apoptotic promastigotes in the virulent inoculum. Proc. Natl Acad. Sci. USA103(37), 13837–13842 (2006).
   PubMed Web of Science ®Google Scholar
• Kerr JF, Wyllie AH, Currie AR. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer26(4), 239–257 (1972).
   PubMed Web of Science ®Google Scholar
• Bratton SB, MacFarlane M, Cain K, Cohen GM. Protein complexes activate distinct caspase cascades in death receptor and stress-induced apoptosis. Exp. Cell Res.256(1), 27–33 (2000).
   PubMed Web of Science ®Google Scholar
• Widmann C, Gibson S, Johnson GL. Caspase-dependent cleavage of signaling proteins during apoptosis. A turn-off mechanism for anti-apoptotic signals. J. Biol. Chem.273(12), 7141–7147 (1998).
   PubMed Web of Science ®Google Scholar
• Lazebnik YA, Kaufmann SH, Desnoyers S, Poirier GG, Earnshaw WC. Cleavage of poly(ADP-ribose) polymerase by a proteinase with properties like ICE. Nature371(6495), 346–347 (1994).
   PubMed Web of Science ®Google Scholar
• Kothakota S, Azuma T, Reinhard C et al. Caspase-3-generated fragment of gelsolin: effector of morphological change in apoptosis. Science278(5336), 294–298 (1997).
   PubMed Web of Science ®Google Scholar
• Stegh AH, Herrmann H, Lampel S et al. Identification of the cytolinker plectin as a major early in vivo substrate for caspase 8 during CD95- and tumor necrosis factor receptor-mediated apoptosis. Mol. Cell. Biol.20(15), 5665–5679 (2000).
   PubMed Web of Science ®Google Scholar
• Villa PG, Henzel WJ, Sensenbrenner M, Henderson CE, Pettmann B. Calpain inhibitors, but not caspase inhibitors, prevent actin proteolysis and DNA fragmentation during apoptosis. J. Cell. Sci.111, 713–722 (1998).
   PubMed Web of Science ®Google Scholar
• Rao L, Perez D, White E. Lamin proteolysis facilitates nuclear events during apoptosis. J. Cell Biol.135, 1441–1455 (1996).
   PubMed Web of Science ®Google Scholar
• Heyder P, Gaipl US, Beyer TD et al. Early detection of apoptosis by staining of acid-treated apoptotic cells with FITC-labeled lectin from Narcissus pseudonarcissus. Cytometry55A(2), 86–93 (2003).
   Google Scholar
• Appelt U, Sheriff A, Gaipl US et al. Viable, apoptotic and necrotic monocytes expose phosphatidylserine: cooperative binding of the ligand Annexin V to dying but not viable cells and implications for PS-dependent clearance. Cell Death Differ.12(2), 194–196 (2005).
   PubMedGoogle Scholar
• Fadok VA, Voelker DR, Campbell PA et al. Exposure of phosphatidylserine on the surface of apoptotic lymphocytes triggers specific recognition and removal by macrophages. J. Immunol.148(7), 2207–2216 (1992).
   PubMed Web of Science ®Google Scholar
• Verhoven B, Schlegel RA, Williamson P. Mechanisms of phosphatidylserine exposure, a phagocyte recognition signal, on apoptotic T lymphocytes. J. Exp. Med.182(5), 1597–1601 (1995).
   PubMed Web of Science ®Google Scholar
• Bratton DL, Fadok VA, Richter DA et al. Appearance of phosphatidylserine on apoptotic cells requires calcium-mediated nonspecific flip-flop and is enhanced by loss of the aminophospholipid translocase. J. Biol. Chem.272(42), 26159–26165 (1997).
   PubMed Web of Science ®Google Scholar
• Cohen GM, Sun XM, Snowden RT, Dinsdale D, Skilleter DN. Key morphological features of apoptosis may occur in the absence of internucleosomal DNA fragmentation. Biochem. J.286, 331–334 (1992).
   PubMed Web of Science ®Google Scholar
• Hsu H, Xiong J, Goeddel DV. The TNF receptor 1-associated protein TRADD signals cell death and NF-κ B activation. Cell81(4), 495–504 (1995).
   PubMed Web of Science ®Google Scholar
• Scaffidi C, Fulda S, Srinivasan A et al. Two CD95 (APO-1/Fas) signaling pathways. EMBO J.17(6), 1675–1687 (1998).
   PubMed Web of Science ®Google Scholar
• Li P, Nijhawan D, Budihardjo I et al. Cytochrome c and dATP-dependent formation of Apaf-1/caspase-9 complex initiates an apoptotic protease cascade. Cell91(4), 479–489 (1997).
   PubMed Web of Science ®Google Scholar
• Hengartner MO. The biochemistry of apoptosis. Nature407(6805), 770–776 (2000).
   PubMed Web of Science ®Google Scholar
• Nakagawa T, Zhu H, Morishima N et al. Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-β. Nature403(6765), 98–103 (2000).
   PubMed Web of Science ®Google Scholar
• Coleman ML, Sahai EA, Yeo M et al. Membrane blebbing during apoptosis results from caspase-mediated activation of ROCK I. Nat. Cell Biol.3(4), 339–345 (2001).
   PubMed Web of Science ®Google Scholar
• Savill J, Dransfield I, Gregory C, Haslett C. A blast from the past: clearance of apoptotic cells regulates immune responses. Nat. Rev. Immunol.2(12), 965–975 (2002).
   PubMed Web of Science ®Google Scholar
• Hart SP, Smith JR, Dransfield I. Phagocytosis of opsonized apoptotic cells: roles for ‘old-fashioned’ receptors for antibody and complement. Clin. Exp. Immunol.135(2), 181–185 (2004).
   PubMed Web of Science ®Google Scholar
• Lauber K, Bohn E, Krober SM et al. Apoptotic cells induce migration of phagocytes via caspase-3-mediated release of a lipid attraction signal. Cell113(6), 717–730 (2003).
   PubMed Web of Science ®Google Scholar
• Nagaosa K, Shiratsuchi A, Nakanishi Y. Concomitant induction of apoptosis and expression of monocyte chemoattractant protein-1 in cultured rat luteal cells by nuclear factor-κB and oxidative stress. Dev. Growth Differ.45(4), 351–359 (2003).
   PubMedGoogle Scholar
• Franz S, Frey B, Sheriff A et al. Lectins detect changes of the glycosylation status of plasma membrane constituents during late apoptosis. Cytometry A69(4), 230–239 (2006).
   PubMedGoogle Scholar
• Arur S, Uche UE, Rezaul K et al. Annexin I is an endogenous ligand that mediates apoptotic cell engulfment. Dev. Cell4(4), 587–598 (20003).
   Google Scholar
• Ogden CA, deCathelineau A, Hoffmann PR et al. C1q and mannose binding lectin engagement of cell surface calreticulin and CD91 initiates macropinocytosis and uptake of apoptotic cells. J. Exp. Med.194(6), 781–795 (2001).
   PubMed Web of Science ®Google Scholar
• Vandivier RW, Ogden CA, Fadok VA et al. Role of surfactant proteins A, D, and C1q in the clearance of apoptotic cells in vivo and in vitro: calreticulin and CD91 as a common collectin receptor complex. J. Immunol.169(7), 3978–3986 (2002).
   PubMed Web of Science ®Google Scholar
• Okazaki Y, Ohno H, Takase K, Ochiai T, Saito T. Cell surface expression of calnexin, a molecular chaperone in the endoplasmic reticulum. J. Biol. Chem.275(46), 35751–35758 (2000).
   PubMedGoogle Scholar
• Hanayama R, Tanaka M, Miyasaka K et al. Autoimmune disease and impaired uptake of apoptotic cells in MFG-E8-deficient mice. Science304(5674), 1147–1150 (2004).
   PubMed Web of Science ®Google Scholar
• Duvall E, Wyllie AH, Morris RG. Macrophage recognition of cells undergoing programmed cell death (apoptosis). Immunology56(2), 351–358 (1985).
   PubMed Web of Science ®Google Scholar
• Kim S, Elkon KB, Ma X. Transcriptional suppression of interleukin-12 gene expression following phagocytosis of apoptotic cells. Immunity21(5), 643–653 (2004).
   PubMedGoogle Scholar
• Gao Y, Herndon JM, Zhang H, Griffith TS, Ferguson TA. Antiinflammatory effects of CD95 ligand (FasL)-induced apoptosis. J. Exp. Med.188(5), 887–896 (1998).
   PubMed Web of Science ®Google Scholar
• Cohen PL, Caricchio R, Abraham V et al. Delayed apoptotic cell clearance and lupus-like autoimmunity in mice lacking the c-mer membrane tyrosine kinase. J. Exp. Med.196(1), 135–140 (2002).
   PubMed Web of Science ®Google Scholar
• Marshak-Rothstein A, Rifkin IR. Immunologically active autoantigens: the role of Toll-like receptors in the development of chronic inflammatory disease. Annu. Rev. Immunol.25(1), 419–441 (2007).
   PubMed Web of Science ®Google Scholar
• Marshak-Rothstein A. Toll-like receptors in systemic autoimmune disease. Nat. Rev. Immunol.6(11), 823 (2006).
   PubMed Web of Science ®Google Scholar
• Ren Y, Stuart L, Lindberg FP et al. Nonphlogistic clearance of late apoptotic neutrophils by macrophages: efficient phagocytosis independent of β(2) integrins. J. Immunol.166(7) 4743–4750 (2001).
   PubMedGoogle Scholar
• Herrmann M, Voll RE, Kalden JR. Etiopathogenesis of systemic lupus erythematosus. Immunol. Today21(9), 424–426 (2000).
   PubMedGoogle Scholar
• Herrmann M, Winkler T, Gaipl U et al. Etiopathogenesis of systemic lupus erythematosus. Int. Arch. Allergy Immunol.123(1), 28–35 (2000).
   PubMed Web of Science ®Google Scholar
• Chu JL, Drappa J, Parnassa A, Elkon KB. The defect in Fas mRNA expression in MRL/lpr mice is associated with insertion of the retrotransposon. ETn. J. Exp. Med.178(2), 723–730 (1993).
   PubMed Web of Science ®Google Scholar
• Watanabe-Fukunaga R, Brannan CI, Copeland NG, Jenkins NA, Nagata S. Lymphoproliferation disorder in mice explained by defects in Fas antigen that mediates apoptosis. Nature356(6367) 314–317 (1992).
   PubMed Web of Science ®Google Scholar
• Lynch DH, Watson ML, Alderson MR et al. The mouse Fas-ligand gene is mutated in gld mice and is part of a TNF family gene cluster. Immunity1(2), 131–136 (1994).
   PubMed Web of Science ®Google Scholar
• Canale VC, Smith CH. Chronic lymphadenopathy simulating malignant lymphoma. J. Pediatr.70(6), 891–899 (1967).
   PubMed Web of Science ®Google Scholar
• Del-Rey M, Ruiz-Contreras J, Bosque A et al. A homozygous Fas ligand gene mutation in a patient causes a new type of autoimmune lymphoproliferative syndrome. Blood108(4), 1306–1312 (2006).
   PubMed Web of Science ®Google Scholar
• Rieux-Laucat F, Le Deist F, Fischer A. Autoimmune lymphoproliferative syndromes: genetic defects of apoptosis pathways. Cell Death Differ.10(1), 124–133 (2003).
   PubMed Web of Science ®Google Scholar
• Sneller MC, Straus SE, Jaffe ES et al. A novel lymphoproliferative/autoimmune syndrome resembling murine lpr/gld disease. J. Clin. Invest.90(2), 334–341 (1992).
   PubMed Web of Science ®Google Scholar
• Mok CC, Lau CS. Pathogenesis of systemic lupus erythematosus. J. Clin. Pathol.56(7), 481–490 (2003).
   PubMed Web of Science ®Google Scholar
• Nisengard RJ, Jablonska S, Chorzelski TP et al. Diagnosis of systemic lupus erythematosus. Importance of antinuclear antibody titers and peripheral staining patterns. Arch. Dermatol.111(10), 1298–1300 (1975).
   PubMedGoogle Scholar
• Salmon JE, Kimberly RP, Gibofsky A, Fotino M. Defective mononuclear phagocyte function in systemic lupus erythematosus: dissociation of Fc receptor-ligand binding and internalization. J. Immunol.133(5), 2525–2531 (1984).
   PubMedGoogle Scholar
• Svensson B. Monocyte in vitro function in systemic lupus erythematosus (SLE). I. A clinical and immunological study. Scand. J. Rheumatol. Suppl.31, 29–41 (1980).
   PubMedGoogle Scholar
• Herrmann M, Voll RE, Zoller OM et al. Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus. Arthritis Rheum.41(7), 1241–1250 (1998).
   PubMed Web of Science ®Google Scholar
• Munoz LE, Gaipl US, Franz S et al. SLE – a disease of clearance deficiency? .Rheumatology (Oxford)44(9), 1101–1107 (2005).
   PubMed Web of Science ®Google Scholar
• Baumann I, Kolowos W, Voll RE et al. Impaired uptake of apoptotic cells into tingible body macrophages in germinal centers of patients with systemic lupus erythematosus. Arthritis Rheum.46(1), 191–201 (2002).
   PubMed Web of Science ®Google Scholar
• Janeway C. Immunobiology. The Immune System in Health and Disease. Current Biology Publications, NY, USA 339–358, 433–434 (1999).
   Google Scholar
• Meyer O, Hauptmann G, Tappeiner G, Ochs HD, Mascart-Lemone F. Genetic deficiency of C4, C2 or C1q and lupus syndromes. Association with anti-Ro (SS-A) antibodies. Clin. Exp. Immunol.62(3), 678–684 (1985).
   PubMed Web of Science ®Google Scholar
• Carroll MC. A protective role for innate immunity in systemic lupus erythematosus. Nat. Rev. Immunol.4(10), 825–831 (2004).
   PubMed Web of Science ®Google Scholar
• Gaipl US, Kuenkele S, Voll RE et al. Complement binding is an early feature of necrotic and a rather late event during apoptotic cell death. Cell Death Differ.8(4), 327–334 (2001).
   PubMed Web of Science ®Google Scholar
• Botto M, Dell’Agnola C, Bygrave AE et al. Homozygous C1q deficiency causes glomerulonephritis associated with multiple apoptotic bodies. Nat. Genet.19(1), 56–59 (1998).
   PubMed Web of Science ®Google Scholar
• Taylor P, Botto M, Walport M. The complement system. Curr. Biol.8(8), R259–R261 (1998).
   Google Scholar
• Walport MJ, Davies KA, Botto M. C1q and systemic lupus erythematosus. Immunobiology199(2), 265–285 (1998).
   PubMed Web of Science ®Google Scholar
• Taylor PR, Carugati A, Fadok VA et al. A hierarchical role for classical pathway complement proteins in the clearance of apoptotic cells in vivo. J. Exp. Med.192(3), 359–366 (2000).
   PubMed Web of Science ®Google Scholar
• Chitrabamrung S, Rubin RL, Tan EM. Serum deoxyribonuclease I and clinical activity in systemic lupus erythematosus. Rheumatol. Int.1(2), 55–60 (1981).
   PubMed Web of Science ®Google Scholar
• Gaipl US, Beyer TD, Heyder P et al. Cooperation between C1q and DNase I in the clearance of necrotic cell-derived chromatin. Arthritis Rheum.50(2), 640–649 (2004).
   PubMedGoogle Scholar
• Gewurz H, Zhang XH, Lint TF. Structure and function of the pentraxins. Curr. Opin. Immunol.7(1), 54–64 (1995).
   PubMed Web of Science ®Google Scholar
• Volanakis JE. Human C-reactive protein: expression, structure, and function. Mol. Immunol.38(2–3), 189–197 (2001).
   PubMed Web of Science ®Google Scholar
• Pereira Da Silva JA, Elkon KB, Hughes GR, Dyck RF, Pepys MB. C-reactive protein levels in systemic lupus erythematosus: a classification criterion? Arthritis Rheum.23(6), 770–771 (1980).
   PubMedGoogle Scholar
• Pepys MB, Lanham JG, De Beer FC. C-reactive protein in SLE. Clin. Rheum. Dis.8(1), 91–103 (1982).
   PubMedGoogle Scholar
• Russell AI, Cunninghame Graham DS, Shepherd C et al. Polymorphism at the C-reactive protein locus influences gene expression and predisposes to systemic lupus erythematosus. Hum. Mol. Genet.13(1), 137–147 (2004).
   PubMed Web of Science ®Google Scholar
• Bell SA, Faust H, Schmid A, Meurer M. Autoantibodies to C-reactive protein (CRP) and other acute-phase proteins in systemic autoimmune diseases. Clin. Exp. Immunol.113(3), 327–332 (1998).
   PubMed Web of Science ®Google Scholar
• Rovere P, Peri G, Fazzini F et al. The long pentraxin PTX3 binds to apoptotic cells and regulates their clearance by antigen-presenting dendritic cells. Blood96(13), 4300–4306 (2000).
   PubMed Web of Science ®Google Scholar
• Gaipl US, Voll RE, Sheriff A et al. Impaired clearance of dying cells in systemic lupus erythematosus. Autoimmun. Rev.4(4) 189–194 (2005).
   PubMed Web of Science ®Google Scholar
• Ballestar E, Esteller M, Richardson BC. The epigenetic face of systemic lupus erythematosus. J. Immunol.176(12), 7143–7147 (2006).
   PubMed Web of Science ®Google Scholar
• Wallace DJ. Antimalarial therapies. In: Dubois’ Lupus Erythematosus. Wallace DJ, Hahn BH (Eds). Lippincott Williams & Wilkins, PA, USA (2007).
   Google Scholar
• McCune WJ, Marder W, Riskalla M. Immunosuppressive drug therapy. In: Dubois’ Lupus Erythematosus. Wallace DJ, Hahn BH (Eds). Lippincott Williams & Wilkins, PA, USA (2007).
   Google Scholar
• Ginzler EM, Dvorkina O. Newer therapeutic approaches for systemic lupus erythematosus. Rheum. Dis. Clin. North Am.31(2), 315–328 (2005).
   PubMedGoogle Scholar
• Heasman SJ, Giles KM, Rossi AG et al. Interferon γ suppresses glucocorticoid augmentation of macrophage clearance of apoptotic cells. Eur. J. Immunol.34(6), 1752–1761 (2004).
   PubMedGoogle Scholar