BCR-ABL: An Anti-Apoptosis Gene in Chronic Myelogenous Leukemia

References

• Champlin K.E., Golde D. Chronic myelogenous leukemia: recent advances. Blood 1981; 65: 1039–1047
   Google Scholar
• Nowell P.C., Hungerford D.A. A minute chromosome in human granulocyte leukemia. Science 1960; 132: 1497–1500
   Web of Science ®Google Scholar
• Groffen J., Morris C.M., Heisterkamp N. Philadelphia chromosome translocation. Chronic meleogenous Leukemia, Molecular Approach to Research and Therapy, A. Deissroth, R.B. Arlingus. Dekker, New York, NY 1991; 181
   Google Scholar
• Koeffler P.H., Golde D. Chronic Myelogenous Leukemia–hew Concepts. New Eng. J. Med. 1981; 319: 1201–1208
   Web of Science ®Google Scholar
• Bernards A, Rubin C.M., Westbrook C.A., Paskind M., Baltinore D. The first intron in the human c-abl gene is at least 200 kilobase long and is a target for translocation in chronic myelogenous leukemia. Mol. Cell Biol. 1984; 7: 3231–3236
   Google Scholar
• Oppi C., Shore S.K., Reddy E.P. Nucleotide sequence of testis-derived cDNAs: Implications for testis specific transcription and abl oncogene activation. Proc. Natl. Acad. Sci. 1987; 84: 8200–8204
   PubMed Web of Science ®Google Scholar
• Henkemeyer M.J., Bennett R.L., Gertler F.B., Hoffmann F.M. DNA sequence, structure and tyrosine kinase activity of the Drosophila melanogaster abelson proto-oncogene homolog. mol, Cell Biol. 1988; 8: 843–853
   PubMed Web of Science ®Google Scholar
• Tybulewicz V.L., Crawford C.E., Jackson P.K., Mulligan R.C. Neonatal Iethality and lymphopenia in mice with a homozygous disruption of the c-abl protooncogene. Cell 1991; 65: 1153–1164
   PubMed Web of Science ®Google Scholar
• van Etten K.A., Jackson P., Baltimore D. The mouse type IV c-abl gene product is a nuclear protein, and activation of transforming ability is associated with cytoplasmic localization. Cell l989; 58: 669–478
   PubMed Web of Science ®Google Scholar
• Witte O.N., Rosenberg N.E., Baltimore D. A normal cell protein cross-reactive to the major abelson murine leukemia virus product. Nature 1979; 396–398
   PubMed Web of Science ®Google Scholar
• McGahon A., Bissonnette R., Schmitt M., Cotter K.M., Green D.R., Cotter T.G. BCR-abl maintains resistance of chronic myelogenous leukemia cells to apoptosis. Blood 1994; 83: 1179–1187
   PubMed Web of Science ®Google Scholar
• Pendergast A.M., Traugh J.A., Witte O.N. Normal cellular and transformation associated abl proteins share common sites for protein kinase C phosphorylation. Mol. Cell Biol. 1987; 7: 4280–4289
   PubMed Web of Science ®Google Scholar
• Rosenberg N., Chen Y.Y. Lymphoid cells transformed by abelson virus require the v-abl protein tyrosine kinase only during early GI. Proc. Natl. Acad. Sci. USA 1992; 89: 6683–4687
   PubMed Web of Science ®Google Scholar
• Jackson P., Baltimore D. N-terminal mutations activates the leukemogenic potential of the myristoylated form of c-abl. EMBO J. 1989; 8: 449–456
   PubMed Web of Science ®Google Scholar
• Muller A.J., Young J.C., Pendergast A.M., Pondel M., Littman D.R., Witte O.N. BCR first exon sequences specifically activates the BCWABL tyrosine kinase oncogene of Philadelphia chromosome positive human leukemias. Molecular and Cellular Biology 1991; 11: 1785–1792
   PubMed Web of Science ®Google Scholar
• Pendergast A.M., Muller A.J., Havlik M.H., Maru Y., Witte O.N. BCR sequences essential for transformation by the BCWABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell 1991; 66: 161–171
   PubMed Web of Science ®Google Scholar
• Kerr J.F.R., Wyllie A.H., Currie A.R. Apoptosis: a basic biological phenomenon with wide ranging implications in tissue kinetics. Br. J. Cancer 1972; 26: 239–257
   PubMed Web of Science ®Google Scholar
• Wyllie A.H., Moms R.G., Smith A.L., Dunlop D. Chromatin cleavage in apoptosis: association with condensed chromatin morphology and dependence on macromolecular synthesis. J. Pathol. 1984; 142: 67–77
   PubMed Web of Science ®Google Scholar
• Savill J., Fadok V., Henson P., Haslett C. Phagocyte recognition of cells undergoing apoptosis. Immunology Today 1993; 14: 131–136
   PubMedGoogle Scholar
• Cohen J.J., Duke R. Glucocorticoid activation of a calcium-dependent endonuclease in thymocyte nuclei leads to cell death. J. Immunol. 1984; 132: 38–42
   PubMed Web of Science ®Google Scholar
• Martin S.J., Lennon S.V., Bonham A.M., Cotter T.G. Induction of apoptosis (programmed cell death) in human leukemic HL-60 cells by inhibition of RNA and protein synthesis. J. Immunol. 1990; 145: 1859–1867
   PubMed Web of Science ®Google Scholar
• Evan G.I., Wyllie A.H., Gilbert C.S., Littlewood T.D., Land H., Brooks M., Waters C.M., Penn L.Z., Hancock D.C. Induction of apoptosis in fibroblasts by c-mye protein. Cell. 1992; 69: 119–128
   PubMed Web of Science ®Google Scholar
• Shi Y., Glynn J., Guilbert L., Cotter T., Bissonnette R., Green D. Role of c-mye in activation-induced apoptotic cell death in T cell hybridomas. Science 1992; 257: 212–214
   PubMed Web of Science ®Google Scholar
• Lowe S.W., Ruley H.E., Jacks T., Housman D.E. p53-dependent apoptosis modulates the cytotoxicity of anticancer agents. Cell 1993; 74: 957–967
   PubMed Web of Science ®Google Scholar
• Hockenberry D., Nunez G., Milliman C., Schreiber R., Korsmeyer S.J. Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death. Nature 1990; 348: 334–336
   PubMed Web of Science ®Google Scholar
• McDonnell T.J., Deane N., Flatt F.M., Nunez G., Jaeger U., McKearn J.P., Korsmeyer S.J. Bcl-2 immunoglobulin transgenic mice demonstrate extended B cell survival and follicular lymphoproliferation. Cell 1989; 57: 79–88
   PubMed Web of Science ®Google Scholar
• Daley G.Q., McLaughlin J., Witte O.N., Baltimore D. The CML-specific p210 ber/abl protein, unlike v-abl does not transform NIH-3T3 fibroblasts. Science 1987; 237: 532–537
   PubMed Web of Science ®Google Scholar
• Kipreos E.T., Wang G. Differential phosphorylation of c-Abl in the cell cycle determined by cdc2 kinase and phosphatase activity. Science 1990; 248: 217–220
   PubMed Web of Science ®Google Scholar
• Evans C.A., Owen-Lynch P., Whetton A.D., Dive C. Activation of the abelson tyrosine kinase activity is associated with suppression of apoptosis in haematopoietic cells. Cancer Rex 1993; 53: 1735–1741
   PubMed Web of Science ®Google Scholar
• Watkins D.C., Moxham C.M., Morris A.J., Malbon C.C. Suppression of Gi alpha enhances phospholipase C signalling. Biochem. L 1994; 299: 593–596
   PubMed Web of Science ®Google Scholar
• Bedi A., Zehnbauer B.A., Barber J.P., Sharkis S.J., Jones R.J. Inhibition of apoptosis by BCR-ABL in chronic myeloid leukemia. Blood 1994; 83: 2038–2044
   PubMed Web of Science ®Google Scholar
• Skorski T., Nieborowska-Skorska M., Nicolaides N.C., Szeylik C., Iversen P., Iozzo G., Zon G., Calabretta B. Suppression of Philadelphia leukemia cell growth in mice by BCR-ABL antisense oligodeoxynucleatides. Proc. Natl. Acad. Sci. 1994; 91: 4504–4508
   PubMed Web of Science ®Google Scholar