Kerr, J.F., Wyllie, A.H. & Currie, A.R. Apoptosis: a basic biological phenomenon with wide-ranging implications in tissue kinetics. Br. J. Cancer 26, 239–257 (1972).
Jacobson, M.D., Weil, M. & Raff, M.C. Programmed cell death in animal development. Cell 88, 347–354 (1997).
Vaux, D.L. & Korsmeyer, S.J. Cell death in development. Cell 96, 245–254 (1999).
Raff, M. Cell suicide for beginners. Nature 396, 119–122 (1998).
Nagata, S. Apoptosis by death factor. Cell 88, 355–365 (1997).
Ashkenazi, A. & Dixit, V.M. Death receptors: signaling and modulation. Science 281, 1305–1308 (1998).
Green, D.R. & Reed, J.C. Mitochondria and apoptosis. Science 281, 1309–1312 (1998).
Thornberry, N.A. & Lazebnik, Y. Caspases: enemies within. Science 281, 1312–1316 (1998).
Earnshaw, W.C., Martins, L.M. & Kaufmann, S.H. Mammalian caspases: structure, activation, substrates, and functions during apoptosis. Annu. Rev. Biochem. 68, 383–424 (1999).
Los, M., Wesselborg, S. & Schulze-Osthoff, K. The role of caspases in development, immunity, and apoptotic signal transduction: lessons from knockout mice. Immunity 10, 629–639 (1999).
Savill, J. & Fadok, V. Corpse clearance defines the meaning of cell death. Nature 407, 784–788 (2000).
Wyllie, A.H. Glucocorticoid-induced thymocyte apoptosis is associated with endogenous endonuclease activation. Nature 284, 555–556 (1980).
Nagata, S., Nagase, H., Kawane, K., Mukae, N. & Fukuyama, H. Degradation of chromosomal DNA during apoptosis. Cell Death Differ. (in the press).
Enari, M. et al. A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD. Nature 391, 43–50 (1998).
Liu, X., Zou, H., Slaughter, C. & Wang, X. DFF, a heterodimeric protein that functions downstream of caspase-3 to trigger DNA fragmentation during apoptosis. Cell 89, 175–184 (1997).
Sakahira, H., Enari, M. & Nagata, S. Cleavage of CAD inhibitor in CAD activation and DNA degradation during apoptosis. Nature 391, 96–99 (1998).
McCarty, J.S., Toh, S.Y. & Li, P. Multiple domains of DFF45 bind synergistically to DFF40: roles of caspase cleavage and sequestration of activator domain of DFF40. Biochem. Biophys. Res. Commun. 264, 181–185 (1999).
Sakahira, H. & Nagata, S. Co-translational folding of caspase-activated DNase with Hsp70, Hsp40 and inhibitor of caspase-activated DNase. J. Biol. Chem. 277, 3364–3370 (2002).
Zhang, J. et al. Resistance to DNA fragmentation and chromatin condensation in mice lacking the DNA fragmentation factor 45. Proc. Natl. Acad. Sci. USA 95, 12480–12485 (1998).
McIlroy, D. et al. An auxiliary mode of apoptotic DNA fragmentation provided by phagocytes. Genes Dev. 14, 549–558 (2000).
Li, L.Y., Luo, X. & Wang, X. Endonuclease G is an apoptotic DNase when released from mitochondria. Nature 412, 95–99 (2001).
Parrish, J. et al. Mitochondrial endonuclease G is important for apoptosis in C. elegans. Nature 412, 90–94 (2001).
van Loo, G. et al. Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation. Cell Death Differ. 8, 1136–1142 (2001).
Hanayama, R. et al. Identification of a factor that links apoptotic cells to phagocytes. Nature 417, 182–187 (2002).
Bernardi, G. in The Enzymes (ed. Boyer, P.D.) 271–287 (Academic Press, New York and London, 1971).
Kawane, K. et al. Requirement of DNase II for definitive erythropoiesis in the mouse fetal liver. Science 292, 1546–1549 (2001).
Krieser, R.J. et al. Deoxyribonuclease IIa is required during the phagocytic phase of apoptosis and its loss causes lethality. Cell Death Differ. 9, 956–962 (2002).
Kawane, K. et al. Structure and promoter analysis of murine CAD and ICAD genes. Cell Death Differ. 6, 745–752 (1999).
Oberhammer, F. et al. Apoptotic death in epithelial cells: cleavage of DNA to 300 and/or 50 kb fragments prior to or in the absence of internucleosomal fragmentation. EMBO J. 12, 3679–3684 (1993).
Godfrey, D.I., Kennedy, J., Suda, T. & Zlotnik, A. A developmental pathway involving four phenotypically and functionally distinct subsets of CD3−CD4−CD8− triple-negative adult mouse thymocytes defined by CD44 and CD25 expression. J. Immunol. 150, 4244–4252 (1993).
Yaegashi, Y., Nielsen, P., Sing, A., Galanos, C. & Freudenberg, M.A. Interferon β, a cofactor in the interferon γ production induced by gram-negative bacteria in mice. J. Exp. Med. 181, 953–960 (1995).
Su, D.M., Wang, J., Lin, Q., Cooper, M.D. & Watanabe, T. Interferons α/β inhibit IL-7-induced proliferation of CD4− CD8− CD3− CD44+ CD25+ thymocytes, but do not inhibit that of CD4− CD8− CD3− CD44− CD25− thymocytes. Immunology 90, 543–549 (1997).
Lin, Q., Dong, C. & Cooper, M.D. Impairment of T and B cell development by treatment with a type I interferon. J. Exp. Med. 187, 79–87 (1998).
Montgomery, R.A. & Dallman, M.J. Semi-quantitative polymerase chain reaction analysis of cytokine and cytokine receptor gene expression during thymic ontogeny. Cytokine 9, 717–726 (1997).
Arends, M.J., Morris, R.G. & Wyllie, A.H. The role of the endonuclease. Am. J. Pathol. 136, 593–608 (1993).
Gavrieli, Y., Sherman, Y. & Ben-Sasson, S.A. Identification of programmed cell death in situ via specific labeling of nuclear DNA fragmentation. J. Cell Biol. 119, 493–501 (1992).
Staley, K., Blaschke, A. & Chun, J. Apoptotic DNA fragmentation is detected by a semi-quantitative ligation-mediated PCR of blunt DNA ends. Cell Death Differ. 4, 66–75 (1997).
Peitsch, M.C. et al. Characterization of the endogenous deoxyribonuclease involved in nuclear DNA degradation during apoptosis (programmed cell death). EMBO J. 12, 371–377 (1993).
Susin, S.A. et al. Molecular characterization of mitochondrial apoptosis-inducing factor. Nature 397, 441–446 (1999).
Wu, Y.C., Stanfield, G.M. & Horvitz, H.R. NUC-1, a Caenorhabditis elegans DNase II homolog, functions in an intermediate step of DNA degradation during apoptosis. Genes Dev. 14, 536–548 (2000).
Mukae, N., Yokoyama, H., Yokokura, T., Sakoyama, Y. & Nagata, S. Activation of the innate immunity in Drosophila by endogenous chromosomal DNA that escaped apoptotic degradation. Genes Dev. 16, 2662–2671 (2002).
Durrieu, F. et al. Caspase activation is an early event in anthracycline-induced apoptosis and allows detection of apoptotic cells before they are ingested by phagocytes. Exp. Cell Res. 240, 165–175 (1998).
Binder, D., Fehr, J., Hengartner, H. & Zinkernagel, R.M. Virus-induced transient bone marrow aplasia: major role of interferon-α/β during acute infection with the noncytopathic lymphocytic choriomeningitis virus. J. Exp. Med. 185, 517–530 (1997).
Doly, J., Civas, A., Navarro, S. & Uze, G. Type I interferons: expression and signalization. Cell Mol. Life Sci. 54, 1109–1121 (1998).
Krieg, A.M. CpG motifs in bacterial DNA and their immune effects. Annu. Rev. Immunol. 20, 709–760 (2002).
Hemmi, H. et al. A Toll-like receptor recognizes bacterial DNA. Nature 408, 740–745 (2000).
Bird, A.P. CpG-rich islands and the function of DNA methylation. Nature 321, 209–213 (1986).
Leadbetter, E.A. et al. Chromatin-IgG complexes activate B cells by dual engagement of IgM and Toll-like receptors. Nature 416, 603–607 (2002).
Kondoh, G. et al. Easy assessment of ES cell clone potency for chimeric development and germ-line competency by an optimized aggregation method. J. Biochem. Biophys. Methods 39, 137–142 (1999).
Platt, N., Suzuki, H., Kurihara, Y., Kodama, T. & Gordon, S. Role for the class A macrophage scavenger receptor in the phagocytosis of apoptotic thymocytes in vitro. Proc. Natl. Acad. Sci. USA 93, 12456–12460 (1996).
Takeshita, S., Kaji, K. & Kudo, A. Identification and characterization of the new osteoclast progenitor with macrophage phenotypes being able to differentiate into mature osteoclasts. J. Bone Miner. Res. 15, 1477–1488 (2000).
Laird, P.W. et al. Simplified mammalian DNA isolation procedure. Nucleic Acids Res. 19, 4293 (1991).
Sambrook, J. & Russell, D.W. Molecular Cloning: A Laboratory Manual (Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 2001).