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Cell Growth and Development

Growth Suppression of Pre-T Acute Lymphoblastic Leukemia Cells by Inhibition of Notch Signaling

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Pages 655-664 | Received 26 Jul 2002, Accepted 21 Oct 2002, Published online: 27 Mar 2023

REFERENCES

  • Artavanis-Tsakonas, S., M. D. Rand, and R. J. Lake. 1999. Notch signaling: cell fate control and signal integration in development. Science 284: 770–776.
  • Aster, J., W. Pear, R. Hasserjian, H. Erba, F. Davi, B. Luo, M. Scott, D. Baltimore, and J. Sklar. 1994. Functional analysis of the TAN-1 gene, a human homolog of Drosophila notch. Cold Spring Harbor Symp. Quant. Biol. 59: 125–136.
  • Aster, J. C., E. S. Robertson, R. P. Hasserjian, J. R. Turner, E. Kieff, and J. Sklar. 1997. Oncogenic forms of NOTCH1 lacking either the primary binding site for RBP-Jκ or nuclear localization sequences retain the ability to associate with RBP-Jκ and activate transcription. J. Biol. Chem. 272: 11336–11343.
  • Aster, J. C., L. Xu, F. G. Karnell, V. Patriub, J. C. Pui, and W. S. Pear. 2000. Essential roles for ankyrin repeat and transactivation domains in induction of T-cell leukemia by Notch1. Mol. Cell. Biol. 20: 7505–7515.
  • Berezovska, O., C. Jack, P. McLean, J. C. Aster, C. Hicks, W. Xia, M. S. Wolfe, W. T. Kimberly, G. Weinmaster, D. J. Selkoe, and B. T. Hyman. 2000. Aspartate mutations in presenilin and gamma-secretase inhibitors both impair notch1 proteolysis and nuclear translocation with relative preservation of notch1 signaling. J. Neurochem. 75: 583–593.
  • Berry, L. W., B. Westlund, and T. Schedl. 1997. Germ-line tumor formation caused by activation of glp-1, a Caenorhabditis elegans member of the Notch family of receptors. Development 124: 925–936.
  • Brou, C., F. Logeat, N. Gupta, C. Bessia, O. LeBail, J. R. Doedens, A. Cumano, P. Roux, R. A. Black, and A. Israel. 2000. A novel proteolytic cleavage involved in Notch signaling: the role of the disintegrin-metalloprotease TACE. Mol. Cell 5: 207–216.
  • Bush, G., G. diSibio, A. Miyamoto, J. B. Denault, R. Leduc, and G. Weinmaster. 2001. Ligand-induced signaling in the absence of furin processing of Notch1. Dev. Biol. 229: 494–502.
  • Capobianco, A. J., P. Zagouras, C. M. Blaumueller, S. Artavanis-Tsakonas, and J. M. Bishop. 1997. Neoplastic transformation by truncated alleles of human NOTCH1/TAN1 and NOTCH2. Mol. Cell. Biol. 17: 6265–6273.
  • Carlesso, N., J. C. Aster, J. Sklar, and D. T. Scadden. 1999. Notch1-induced delay of human hematopoietic progenitor cell differentiation is associated with altered cell cycle kinetics. Blood 93: 838–848.
  • De Celis, J. F., and S. J. Bray. 2000. The Abruptex domain of Notch regulates negative interactions between Notch, its ligands and Fringe. Development 127: 1291–1302.
  • Deftos, M. L., Y. W. He, E. W. Ojala, and M. J. Bevan. 1998. Correlating notch signaling with thymocyte maturation. Immunity 9: 777–786.
  • De Strooper, B., W. Annaert, P. Cupers, P. Saftig, K. Craessaerts, J. S. Mumm, E. H. Schroeter, V. Schruvers, M. S. Wolfe, W. J. Ray, A. Goate, and R. Kopan. 1999. A presenilin-1-dependent-secretase-like protease mediates release of Notch intracellular domain. Nature 398: 518–522.
  • Dovey, H. F., V. John, J. P. Anderson, L. Z. Chen, P. de Saint Andrieu, L. Y. Fang, S. B. Freedman, B. Folmer, E. Goldbach, E. J. Holsztynska, K. L. Hu, K. L. Johnson-Wood, S. L. Kennedy, D. Kholodenko, J. E. Knops, L. H. Latimer, M. Lee, Z. Liao, I. M. Lieberburg, R. N. Motter, L. C. Mutter, J. Nietz, K. P. Quinn, K. L. Sacchi, P. A. Seubert, G. M. Shopp, E. D. Thorsett, J. S. Tung, J. Wu, S. Yang, C. T. Yin, D. B. Schenk, P. C. May, L. D. Altstiel, M. H. Bender, L. N. Boggs, T. C. Britton, J. C. Clemens, D. L. Czilli, D. K. Dieckman-McGinty, J. J. Droste, K. S. Fuson, B. D. Gitter, P. A. Hyslop, E. M. Johnstone, W. Y. Li, S. P. Little, T. E. Mabry, F. D. Miller, and J. E. Audia. 2001. Functional gamma-secretase inhibitors reduce beta-amyloid peptide levels in brain. J. Neurochem. 76: 173–181.
  • Doyle, T. G., C. Wen, and I. Greenwald. 2000. SEL-8, a nuclear protein required for LIN-12 and GLP-1 signaling in Caenorhabditis elegans. Proc. Natl. Acad. Sci. USA 97: 7877–7881.
  • Ellisen, L. W., J. Bird, D. C. West, A. L. Soreng, T. C. Reynolds, S. D. Smith, and J. Sklar. 1991. TAN-1, the human homolog of the Drosophila notch gene, is broken by chromosomal translocations in T lymphoblastic neoplasms. Cell 66: 649–661.
  • Esler, W. P., W. T. Kimberly, B. L. Ostaszewski, W. Ye, T. S. Diehl, D. J. Selkoe, and M. S. Wolfe. 2002. Activity-dependent isolation of the presenilin-gamma-secretase complex reveals nicastrin and a gamma substrate. Proc. Natl. Acad. Sci. USA 99: 2720–2725.
  • Fares, H., and I. Greenwald. 1999. SEL-5, a serine/threonine kinase that facilitates lin-12 activity in Caenorhabditis elegans. Genetics 153: 1641–1654.
  • Fortini, M. E., I. Rebay, L. A. Caron, and S. Artavanis-Tsakonas. 1993. An activated Notch receptor blocks cell-fate commitment in the developing Drosophila eye. Nature 365: 555–557.
  • Fryer, C. J., E. Lamar, I. Turbachova, C. Kintner, and K. A. Jones. 2002. Mastermind mediates chromatin-specific transcription and turnover of the Notch enhancer complex. Genes Dev. 16: 1397–1411.
  • Go, M. J., D. S. Eastman, and S. Artavanis-Tsakonas. 1998. Cell proliferation control by Notch signaling in Drosophila development. Development 125: 2031–2040.
  • Greenwald, I., and G. Seydoux. 1990. Analysis of gain-of-function mutations of the lin-12 gene of Caenorhabditis elegans. Nature 346: 197–199.
  • Henkel, T., P. D. Ling, S. D. Hayward, and M. G. Peterson. 1994. Mediation of Epstein-Barr virus EBNA2 transactivation by recombination signal-binding protein Jκ. Science 265: 92–95.
  • Hsieh, J. J., T. Henkel, P. Salmon, E. Robey, M. G. Peterson, and S. D. Hayward. 1996. Truncated mammalian Notch1 activates CBF1/RBPJκ-repressed genes by a mechanism resembling that of Epstein-Barr virus EBNA2. Mol. Cell. Biol. 16: 952–959.
  • Huppert, S. S., A. Le, E. H. Schroeter, J. S. Mumm, M. T. Saxena, L. A. Milner, and R. Kopan. 2000. Embryonic lethality in mice homozygous for a processing-deficient allele of Notch1. Nature 405: 966–970.
  • Izon, D. J., J. A. Punt, L. Xu, F. G. Karnell, D. Allman, P. S. Myung, N. J. Boerth, J. C. Pui, G. A. Koretzky, and W. S. Pear. 2001. Notch1 regulates maturation of CD4+ and CD8+ thymocytes by modulating TCR signal strength. Immunity 14: 253–264.
  • Jeffries, S., and A. J. Capobianco. 2000. Neoplastic transformation by Notch requires nuclear localization. Mol. Cell. Biol. 20: 3928–3941.
  • Jeffries, S., D. J. Robbins, and A. J. Capobianco. 2002. Characterization of a high-molecular-weight Notch complex in the nucleus of Notch(ic)-transformed RKE cells and in a human T-cell leukemia cell line. Mol. Cell. Biol. 22: 3927–3941.
  • Jehn, B. M., W. Bielke, W. S. Pear, and B. A. Osborne. 1999. Protective effects of notch-1 on TCR-induced apoptosis. J. Immunol. 162: 635–638.
  • Jundt, F., I. Anagnostopoulos, R. Forster, S. Mathas, H. Stein, and B. Dorken. 2002. Activated Notch1 signaling promotes tumor cell proliferation and survival in Hodgkin and anaplastic large cell lymphoma. Blood 99: 3398–3403.
  • Kato, H., Y. Taniguchi, H. Kurooka, S. Minoguchi, T. Sakai, S. Nomura-Okazaki, K. Tamura, and T. Honjo. 1997. Involvement of RBP-J in biological functions of mouse Notch1 and its derivatives. Development 124: 4133–4141.
  • Kurooka, H., and T. Honjo. 2000. Functional interaction between the mouse notch1 intracellular region and histone acetyltransferases PCAF and GCN5. J. Biol. Chem. 275: 17211–17220.
  • Kurooka, H., K. Kuroda, and T. Honjo. 1998. Roles of the ankyrin repeats and C-terminal region of the mouse notch1 intracellular region. Nucleic Acids Res. 26: 5448–5455.
  • Lieber, T., S. Kidd, E. Alcamo, V. Corbin, and M. W. Young. 1993. Antineurogenic phenotypes induced by truncated Notch proteins indicate a role in signal transduction and may point to a novel function for Notch in nuclei. Genes Dev. 7: 1949–1965.
  • Logeat, F., C. Bessia, C. Brou, O. LeBail, S. Jarriault, N. G. Seidah, and A. Israel. 1998. The Notch1 receptor is cleaved constitutively by a furin-like convertase. Proc. Natl. Acad. Sci. USA 95: 8108–8112.
  • Luo, B., J. C. Aster, R. P. Hasserjian, F. Kuo, and J. Sklar. 1997. Isolation and functional analysis of a cDNA for human Jagged2, a gene encoding a ligand for the Notch1 receptor. Mol. Cell. Biol. 17: 6057–6067.
  • Matsuno, K., M. J. Go, X. Sun, D. S. Eastman, and S. Artavanis-Tsakonas. 1997. Suppressor of Hairless-independent events in Notch signaling imply novel pathway elements. Development 124: 4265–4273.
  • Mumm, J. S., and R. Kopan. 2000. Notch signaling: from the outside in. Dev. Biol. 228: 151–165.
  • Nofziger, D., A. Miyamoto, K. M. Lyons, and G. Weinmaster. 1999. Notch signaling imposes two distinct blocks in the differentiation of C2C12 myoblasts. Development 126: 1689–1702.
  • Pear, W. S., J. C. Aster, M. L. Scott, R. P. Hasserjian, B. Soffer, J. Sklar, and D. Baltimore. 1996. Exclusive development of T cell neoplasms in mice transplanted with bone marrow expressing activated Notch alleles. J. Exp. Med. 183: 2283–2291.
  • Petcherski, A. G., and J. Kimble. 2000. LAG-3 is a putative transcriptional activator in the C. elegans Notch pathway. Nature 405: 364–368.
  • Pui, J. C., D. Allman, L. Xu, S. DeRocco, F. G. Karnell, S. Bakkour, J. Y. Lee, T. Kadesch, R. R. Hardy, J. C. Aster, and W. S. Pear. 1999. Notch1 expression in early lymphopoiesis influences B versus T lineage determination. Immunity 11: 299–308.
  • Radtke, F., A. Wilson, G. Stark, M. Bauer, J. van Meerwijk, H. R. MacDonald, and M. Aguet. 1999. Deficient T cell fate specification in mice with an induced inactivation of Notch1. Immunity 10: 547–558.
  • Ramain, P., K. Khechumian, L. Seugnet, N. Arbogast, C. Ackermann, and P. Heitzler. 2001. Novel Notch alleles reveal a Deltex-dependent pathway repressing neural fate. Curr. Biol. 11: 1729–1738.
  • Rebay, I., R. J. Fleming, R. G. Fehon, L. Cherbas, P. Cherbas, and S. Artavanis-Tsakonas. 1991. Specific EGF repeats of Notch mediate interactions with Delta and Serrate: implications for Notch as a multifunctional receptor. Cell 67: 687–699.
  • Robbins, J., B. J. Blondel, D. Gallahan, and R. Callahan. 1992. Mouse mammary tumor gene int-3: a member of the notch gene family transforms mammary epithelial cells. J. Virol. 66: 2594–2599.
  • Ronchini, C., and A. J. Capobianco. 2001. Induction of cyclin D1 transcription and CDK2 activity by Notch(ic): implication for cell cycle disruption in transformation by Notch(ic). Mol. Cell. Biol. 21: 5925–5934.
  • Schagger, H., and G. von Jagow. 1987. Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem. 166: 368–379.
  • Schroeter, E. H., J. A. Kisslinger, and R. Kopan. 1998. Notch-1 signalling requires ligand-induced proteolytic release of intracellular domain. Nature 393: 382–386.
  • Seiffert, D., J. D. Bradley, C. M. Rominger, D. H. Rominger, F. Yang, J. E. Meredith, Jr., Q. Wang, A. H. Roach, L. A. Thompson, S. M. Spitz, J. N. Higaki, S. R. Prakash, A. P. Combs, R. A. Copeland, S. P. Arneric, P. R. Hartig, D. W. Robertson, B. Cordell, A. M. Stern, R. E. Olson, and R. Zaczek. 2000. Presenilin-1 and -2 are molecular targets for gamma-secretase inhibitors. J. Biol. Chem. 275: 34086–34091.
  • Shawber, C., D. Nofziger, J. J. Hsieh, C. Lindsell, O. Bogler, D. Hayward, and G. Weinmaster. 1996. Notch signaling inhibits muscle cell differentiation through a CBF1-independent pathway. Development 122: 3765–3773.
  • Struhl, G., and A. Adachi. 1998. Nuclear access and action of notch in vivo. Cell 93: 649–660.
  • Struhl, G., and I. Greenwald. 2001. Presenilin-mediated transmembrane cleavage is required for Notch signal transduction in Drosophila. Proc. Natl. Acad. Sci. USA 98: 229–234.
  • Tani, S., H. Kurooka, T. Aoki, N. Hashimoto, and T. Honjo. 2001. The N- and C-terminal regions of RBP-J interact with the ankyrin repeats of Notch1 RAMIC to activate transcription. Nucleic Acids Res. 29: 1373–1380.
  • Taniguchi, Y., H. Karlstrom, J. Lundkvist, T. Mizutani, A. Otaka, M. Vestling, A. Bernstein, D. Donoviel, U. Lendahl, and T. Honjo. 2002. Notch receptor cleavage depends on but is not directly executed by presenilins. Proc. Natl. Acad. Sci. USA 99: 4014–4019.
  • Wang, S., S. Younger-Shepherd, L. Y. Jan, and Y. N. Jan. 1997. Only a subset of the binary cell fate decisions mediated by Numb/Notch signaling in Drosophila sensory organ lineage requires Suppressor of Hairless. Development 124: 4435–4446.
  • Weihofen, A., K. Binns, M. K. Lemberg, K. Ashman, and B. Martoglio. 2002. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296: 2215–2218.
  • Wolfe, M. S. 2001. gamma-Secretase inhibitors as molecular probes of presenilin function. J. Mol. Neurosci. 17: 199–204.
  • Wolfe, M. S., W. Xia, B. L. Ostaszewski, T. S. Diehl, W. T. Kimberly, and D. J. Selkoe. 1999. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and gamma-secretase activity. Nature 398: 513–517.
  • Wu, L., J. C. Aster, S. C. Blacklow, R. Lake, S. Artavanis-Tsakonas, and J. D. Griffin. 2000. MAML1, a human homologue of drosophila mastermind, is a transcriptional coactivator for NOTCH receptors. Nat. Genet. 26: 484–489.
  • Yan, X. Q., U. Sarmiento, Y. Sun, G. Huang, J. Guo, T. Juan, G. Van, M. Y. Qi, S. Scully, G. Senaldi, and F. A. Fletcher. 2001. A novel Notch ligand, Dll4, induces T-cell leukemia/lymphoma when overexpressed in mice by retroviral-mediated gene transfer. Blood 98: 3793–3799.

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