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Journal articles on the topic 'Proteine bcr-abl'

Author: Grafiati

Published: 4 June 2021

Last updated: 12 February 2022

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1

Tsukahara, Fujiko, and Yoshiro Maru. "Bag1 directly routes immature BCR-ABL for proteasomal degradation." Blood 116, no. 18 (2010): 3582–92. http://dx.doi.org/10.1182/blood-2009-10-249623.

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Abstract Degradation of BCR-ABL oncoproteins by heat shock protein 90 (Hsp90) inhibitors in chronic myelogenous leukemia is expected to overcome resistance to ABL tyrosine kinase inhibitors. However, the precise mechanisms still remain to be uncovered. We found that while c-Cbl E3 ligase induced ubiquitin-dependent degradation of mature and phosphorylated BCR-ABL proteins, another E3 ligase CHIP (carboxyl terminus of the Hsc70-interacting protein) degraded immature BCR-ABL proteins and efficiently suppressed BCR-ABL–dependent leukemic growth. Interestingly, Bag1 (Bcl-2-associated athanogene-1)

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2

Gorre, Mercedes E., Katharine Ellwood-Yen, Gabriela Chiosis, Neal Rosen, and Charles L. Sawyers. "BCR-ABL point mutants isolated from patients with imatinib mesylate–resistant chronic myeloid leukemia remain sensitive to inhibitors of the BCR-ABL chaperone heat shock protein 90." Blood 100, no. 8 (2002): 3041–44. http://dx.doi.org/10.1182/blood-2002-05-1361.

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Clinical resistance to imatinib mesylate is commonly observed in patients with advanced Philadelphia chromosome– positive (Ph+) leukemias. Acquired resistance is typically associated with reactivation of BCR-ABL due to kinase domain mutations or gene amplification, indicating that BCR-ABL remains a viable target for inhibition in these patients. Strategies for overcoming resistance can be envisioned through exploitation of other molecular features of the BCR-ABL protein, such as its dependence on the molecular chaperone heat shock protein 90 (Hsp90). To determine whether inhibition of Hsp90 co

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3

Chen, Ying, Nicole Froehlich, and Stefan K. Bohlander. "Towards the In Vivo Identificaton of Leukemogenic Fusion Proteins." Blood 104, no. 11 (2004): 2970. http://dx.doi.org/10.1182/blood.v104.11.2970.2970.

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Abstract Currently there are no methods available to identifiy leukemogenic fusion proteins in vivo. All available methods, like Southern blotting, PCR, FISH or Western blotting, require the destruction of the cells that are assayed. A method for the in vivo detection of leukemogenic fusion proteins would be highly desirable because it would open up new approaches to study leukemia and might lead to novel treatment strategies. We have developed a strategy for the in vivo detection of the BCR/ABL fusion protein. BCR/ABL is found in virtually all cases chronic myeloid leukemia (CML) and a large

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4

Perazzona, Bastianella, Yan Wang, and Ralph B. Arlinghaus. "Role of BCR in Down-Modulation of BCR-ABL Oncogenicity in CML." Blood 112, no. 11 (2008): 3210. http://dx.doi.org/10.1182/blood.v112.11.3210.3210.

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Abstract Bcr-Abl acquires its transforming ability through its up-regulated Abl tyrosine kinase activity. Bcr is a phosphoprotein with a novel serine/threonine kinase activity encoded by its first exon. Over-expression of BCR in K562 cells produces a phosphoserine form of Bcr and interferes with the oncogenic effects of BCR-ABL in mice (Lin et al., Oncogene 2001). We have recently shown the inhibitory effects of Bcr on Bcr-Abl, in a nude mouse solid tumor model. Expression of BCR/GFP in TonB210 cells used for injection delayed tumor formation and tumors were 50% smaller compared to the TonB210

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5

Zheng, Xiaomin, Saskia Güller, Gesine Bug, et al. "The Reciprocal t(9;22)-Translocation Products ABL/BCR Have Leukemogenic Potential Independently from BCR/ABL." Blood 104, no. 11 (2004): 214. http://dx.doi.org/10.1182/blood.v104.11.214.214.

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Abstract In 95% of chronic myeloid leukemia (CML) and in 25% of acute lymphatic leukemia (ALL) the t(9;22) translocation fuses the bcr gene on chromosome 22 to the abl gene on chromosome 9 and vice versa. On 22+ the different breakpoints leads to the formation of two different major fusion genes: the major breakpoint (M-bcr) related to CML and the minor (m-bcr) related to ALL. The chimaeric fusion gene on 22+ (Philadelphia-chromosome) encodes for the BCR/ABL protein, the p210(BCR/ABL) in CML and the p185(BCR/ABL) in Ph+ALL. The fusion gene on 9+ encodes for the reciprocal ABL/BCR proteins, the

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6

Weerkamp, Floor, E. Dekking, Vincent H. J. Van der Velden, et al. "Flow Cytometric Detection of BCR-ABL Fusion Proteins in Leukemia Patients Via An Immunobead Assay." Blood 112, no. 11 (2008): 2533. http://dx.doi.org/10.1182/blood.v112.11.2533.2533.

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Abstract The BCR-ABL fusion gene results from the translocation t(9;22). It is the hallmark of chronic myeloid leukemia (CML) and is present in a poor-risk subgroup of precursor B cell acute lymphoblastic leukemia (ALL), which represents 25–30% of adult ALL and 3–5% of childhood ALL. Consequently the detection of the BCR-ABL aberration is of utmost importance for diagnosis and classification of leukemia patients and can also be used as marker for monitoring of BCR-ABL+ leukemias to evaluate treatment effectiveness. So far, the BCR-ABL aberration has been detected by cytogenetics, FISH or PCR,

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7

Wohlbold, Lara, Heiko van der Kuip, Alexandra Moehring, et al. "Repeated Application of Sequence-Specific SiRNA Molecules Leads to an Effective Downmodulation of All Clinically Relevant bcr-abl Gene Variants." Blood 104, no. 11 (2004): 4319. http://dx.doi.org/10.1182/blood.v104.11.4319.4319.

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Abstract Fusion transcripts such as bcr-abl encoding pathological oncogenic proteins represent ideal targets for a tumor-specific RNA interference (RNAi) approach. The aim of the present study was to optimize the efficacy of bcr-abl RNAi. We evaluated several synthetic siRNAs targeting the fusion sites of all common bcr-abl transcript variants (e14a2, e13a2, or e1a2). Significant knock-down of p210Bcr-abl and p190Bcr-abl fusion proteins was successfully achieved in bcr-abl expressing 32D cells and human leukemic K562 and MEG-01 cells. Repeated application of siRNA proved to be significantly mo

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8

Million, Ryan P., and Richard A. Van Etten. "The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase." Blood 96, no. 2 (2000): 664–70. http://dx.doi.org/10.1182/blood.v96.2.664.014k52_664_670.

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The BCR/ABL oncogene results from a balanced translocation between chromosomes 9 and 22 and is found in patients with chronic myeloid leukemia (CML) and in some patients with acute B-lymphoid leukemia. The Bcr/Abl fusion protein is a constitutively active tyrosine kinase that stimulates several intracellular signaling pathways, including activation of Ras through direct binding of the SH2-containing adapter protein Grb2 to Bcr tyrosine 177. A tyrosine-to-phenylalanine mutation (Y177F) at this site blocks the co-association of Bcr/Abl and Grb2 in vivo and impairs focus formation by Bcr/Abl in f

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9

Castro, Fabiola A., Gabriela Brumatti, and Gustavo P. Amarante-Mendes. "Expression of BCR-ABL Does Not Inhibit Apoptosis In Vitro, on a B Lymphoblastoid Cell Line." Blood 104, no. 11 (2004): 4242. http://dx.doi.org/10.1182/blood.v104.11.4242.4242.

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Abstract The bcr-abl oncogene is generated by the Philadelphia chromosome (Ph) translocation, fusing the BCR gene to the ABL gene and occurs mainly in two different forms. In chronic myelogenous leukemia (CML) a 210kDa Bcr-Abl protein is associated with proliferation and accumulation of myeloid cells and their precursors, whereas a 185kDa form is responsible for the pathogenesis of acute lymphocytic leukemia (ALL). Bcr-Abl not only induces cellular transformation but also regulates cell proliferation and confers resistance to a variety of apoptosis-inducing agents. Much attention has been focu

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10

Wohlbold, Lara, Heiko van der Kuip, Cornelius Miething, et al. "Inhibition of bcr-abl gene expression by small interfering RNA sensitizes for imatinib mesylate (STI571)." Blood 102, no. 6 (2003): 2236–39. http://dx.doi.org/10.1182/blood-2002-12-3899.

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Abstract Bcr-Abl proteins are effective inducers of the leukemic phenotype in chronic myeloid leukemia (CML) and distinct variants of acute lymphoblastic leukemia (ALL). Targeting bcr-abl by treatment with the selective tyrosine kinase inhibitor imatinib has proved to be highly efficient for controlling leukemic growth. However, it is unclear whether imatinib is sufficient to eradicate the disease because of primary or secondary resistance of leukemic cells. Therefore, targeting Bcr-Abl with an alternative approach is of great interest. We demonstrate that RNA interference (RNAi) with a breakp

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11

Cortez, D., L. Kadlec, and A. M. Pendergast. "Structural and signaling requirements for BCR-ABL-mediated transformation and inhibition of apoptosis." Molecular and Cellular Biology 15, no. 10 (1995): 5531–41. http://dx.doi.org/10.1128/mcb.15.10.5531.

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BCR-ABL is a deregulated tyrosine kinase expressed in Philadelphia chromosome-positive human leukemias. Prolongation of hematopoietic cell survival by inhibition of apoptosis has been proposed to be an integral component of BCR-ABL-induced chronic myelogenous leukemia. BCR-ABL elicits transformation of both fibroblast and hematopoietic cells and blocks apoptosis following cytokine deprivation in various factor-dependent cells. To elucidate the mechanisms whereby BCR-ABL induces transformation and blocks apoptosis in hematopoietic cells, we examined the biological effects of expression of a ser

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12

Bartholomeusz, Geoffrey A., Nichalos Donato, Zeev Estrov, Waldemar Priebe, and Moshe Talpaz. "Activation of a Novel Proteasomal Independent Bcr/Abl Degradation Pathway by WP1130 Induces Apoptosis in CML Cells." Blood 106, no. 11 (2005): 2862. http://dx.doi.org/10.1182/blood.v106.11.2862.2862.

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Abstract Chronic myelogenous leukemia (CML) is a clonal myeloproliferative disorder of hematopoietic stem cells caused by 9:22 reciprocal chromosomal translocation resulting in expression of a highly stable, constitutively active tyrosine kinase, Bcr/Abl. Inhibition of Bcr/Abl with imatinib mesylate, a potent Abl-specific tyrosine kinase inhibitor, is a highly effective therapy for this disease. However, clinical resistance occurs particularly in the later stages of the disease due mainly to the occurrence of point mutations in the Abl kinase domain and continual Bcr/Abl signaling. Alternative

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13

Weisberg, Ellen, and James D. Griffin. "Mechanism of resistance to the ABL tyrosine kinase inhibitor STI571 in BCR/ABL–transformed hematopoietic cell lines." Blood 95, no. 11 (2000): 3498–505. http://dx.doi.org/10.1182/blood.v95.11.3498.011k27_3498_3505.

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The tyrosine kinase activity of the Bcr/Abl oncogene is required for transformation of hematopoietic cells. The tyrosine kinase inhibitor STI571 (formerly called CGP57148B, Novartis Pharmaceuticals) inhibits BCR/ABL, TEL/ABL, and v-ABL kinase activity and inhibits growth and viability of cells transformed by any of these ABL oncogenes. Here we report the generation of 2 BCR/ABL–positive cell lines that have developed partial resistance to STI571. BCR/ABL–transformed Ba/F3 hematopoietic cells and Philadelphia-positive human K562 cells were cultured in gradually increasing concentrations of STI5

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14

Demirel, Özlem, Olivier Balló, Hubert Serve, and Christian H. Brandts. "The Role Of SOCS1 In BCR-ABL Mediated Transformation and Leukemogenesis." Blood 122, no. 21 (2013): 2507. http://dx.doi.org/10.1182/blood.v122.21.2507.2507.

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Abstract The BCR-ABL oncogene activates several signaling pathways, most notably by constitutive phosphorylation of the signal transducer and activator of transcription protein 5 (STAT5). After phosphorylation and nuclear translocation, STAT5 transcriptionally activates numerous genes responsible for proliferation, survival and differentiation of hematopoietic stem and progenitor cells. Among the STAT5 target genes are suppressor of cytokine signaling (SOCS) proteins. SOCS proteins inhibit JAK kinases by multiple mechanisms, thereby terminating cytokine signaling in a classical negative feedba

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15

Liu, J., Y. Wu, G. Z. Ma, et al. "Inhibition of Bcr serine kinase by tyrosine phosphorylation." Molecular and Cellular Biology 16, no. 3 (1996): 998–1005. http://dx.doi.org/10.1128/mcb.16.3.998.

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The first exon of the BCR gene encodes a new serine/threonine protein kinase. Abnormal fusion of the BCR and ABL genes, resulting from the formation of the Philadelphia chromosome (Ph), is the hallmark of Ph-positive leukemia. We have previously demonstrated that the Bcr protein is tyrosine phosphorylated within first-exon sequences by the Bcr-Abl oncoprotein. Here we report that in addition to tyrose 177 (Y-177), Y-360 and Y283 are phosphorylated in Bcr-Abl proteins in vitro. Moreover, Bcr tyrosine 360 is phosphorylated in vivo within both Bcr-Abl and Bcr. Bcr mutant Y177F had a greatly reduc

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16

Moore, James C., Chi Ly, Halbur Luke, and S. Tiong Ong. "Enhanced Killing of Chronic Myelogenous Leukemia Cells by Rapamycin and Imatinib Is Associated with Differential Inhibition of 4E-BP1 and eIF4E Phosphorylation and Decreased Protein Expression by Non-Overlapping Mechanisms." Blood 104, no. 11 (2004): 1993. http://dx.doi.org/10.1182/blood.v104.11.1993.1993.

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Abstract The Bcr-abl tyrosine kinase is known to promote transformation by dysregulating gene transcription, but its role in dysregulating translation is less well documented. Our recent work has implicated the mammalian target of rapamycin (mTOR) signaling as a downstream target of Bcr-Abl, since we find that the mTOR effectors, 4E-BP1 and S6, are phosphorylated in a Bcr-Abl kinase-dependent manner (Ly et al., Cancer Research, 2003). Because mTOR is a central regulator of eukaryotic translation, and inhibitors of mTOR act synergistically with imatinib mesylate (imatinib) to kill CML cells, th

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17

Million, Ryan P., and Richard A. Van Etten. "The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase." Blood 96, no. 2 (2000): 664–70. http://dx.doi.org/10.1182/blood.v96.2.664.

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Abstract The BCR/ABL oncogene results from a balanced translocation between chromosomes 9 and 22 and is found in patients with chronic myeloid leukemia (CML) and in some patients with acute B-lymphoid leukemia. The Bcr/Abl fusion protein is a constitutively active tyrosine kinase that stimulates several intracellular signaling pathways, including activation of Ras through direct binding of the SH2-containing adapter protein Grb2 to Bcr tyrosine 177. A tyrosine-to-phenylalanine mutation (Y177F) at this site blocks the co-association of Bcr/Abl and Grb2 in vivo and impairs focus formation by Bcr

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18

Yan, Zhengwei, Karthigayan Shanmugasundaram, Dongwen Ma, Jiayu Luo, Shiwen Luo, and Hai Rao. "The N-terminal domain of the non-receptor tyrosine kinase ABL confers protein instability and suppresses tumorigenesis." Journal of Biological Chemistry 295, no. 27 (2020): 9069–75. http://dx.doi.org/10.1074/jbc.ra120.012821.

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Chromosome translocation can lead to chimeric proteins that may become oncogenic drivers. A classic example is the fusion of the BCR activator of RhoGEF and GTPase and the ABL proto-oncogene nonreceptor tyrosine kinase, a result of a chromosome abnormality (Philadelphia chromosome) that causes leukemia. To unravel the mechanism underlying BCR-ABL–mediated tumorigenesis, here we compared the stability of ABL and the BCR-ABL fusion. Using protein degradation, cell proliferation, 5-ethynyl-2-deoxyuridine, and apoptosis assays, along with xenograft tumor analysis, we found that the N-terminal segm

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19

Weisberg, Ellen, and James D. Griffin. "Mechanism of resistance to the ABL tyrosine kinase inhibitor STI571 in BCR/ABL–transformed hematopoietic cell lines." Blood 95, no. 11 (2000): 3498–505. http://dx.doi.org/10.1182/blood.v95.11.3498.

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Abstract The tyrosine kinase activity of the Bcr/Abl oncogene is required for transformation of hematopoietic cells. The tyrosine kinase inhibitor STI571 (formerly called CGP57148B, Novartis Pharmaceuticals) inhibits BCR/ABL, TEL/ABL, and v-ABL kinase activity and inhibits growth and viability of cells transformed by any of these ABL oncogenes. Here we report the generation of 2 BCR/ABL–positive cell lines that have developed partial resistance to STI571. BCR/ABL–transformed Ba/F3 hematopoietic cells and Philadelphia-positive human K562 cells were cultured in gradually increasing concentration

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20

Scheich, Florian, Christian Peschel, and Helga Bernhard. "The Immunogenicity of BCR/ABL+ Cells Is Dominated by BCR/ABL-Regulated Antigens and Is Impaired by the Inhibition of BCR/ABL Kinase Activity." Blood 108, no. 11 (2006): 2200. http://dx.doi.org/10.1182/blood.v108.11.2200.2200.

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Abstract The inhibition of BCR/ABL kinase activity by imatinib mesylate (IM, STI571, Gleevec®) is the standard therapy for patients with Philadelphia chromosome+ (Ph+) chronic myeloid leukemia (CML). However, the long term treatment with IM or other BCR/ABL kinase inhibitors may be limited due to the development of resistant disease and accumulating side effects. Immunotherapeutical approaches directed against Ph+ CML may overcome these problems. So far, the research to develop an immunotherapy against Ph+ leukemia focused on the BCR-ABL fusion protein, giving the promising opportunity to stim

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21

Wu, Ji, Feng Meng, Moshe Talpaz, and Nicholas J. Donato. "Lyn Kinase Alters Gab2 Phosphorylation and c-Cbl Protein Levels To Regulate Imatinib Sensitivity and Survival of Chronic Myelogenous Leukemia Cells." Blood 108, no. 11 (2006): 2132. http://dx.doi.org/10.1182/blood.v108.11.2132.2132.

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Abstract The tyrosine kinase inhibitor imatinib mesylate (Gleevec) is effective in controlling BCR-ABL expressing leukemias but resistance occurs in some early phase patients while it is more common in advanced disease. Resistance has been generally associated with mutations in the BCR-ABL kinase that effect drug affinity. However patients are also increasingly reported to fail imatinib therapy while retaining wild-type BCR-ABL expression. Our previous studies suggested a role for Lyn, a Src-related kinase, in imatinib resistance. K562 cells selected for imatinib resistance (K562R) overexpress

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22

Melo, JV, DE Gordon, NC Cross, and JM Goldman. "The ABL-BCR fusion gene is expressed in chronic myeloid leukemia." Blood 81, no. 1 (1993): 158–65. http://dx.doi.org/10.1182/blood.v81.1.158.158.

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Abstract Although the BCR-ABL hybrid gene on chromosome 22q-plays a pivotal role in the pathogenesis of chronic myeloid leukemia (CML), little is known of the reciprocal chimeric gene, ABL-BCR, formed on chromosome 9q+. By reverse transcription/polymerase chain reaction amplification (RT/PCR) we have detected ABL-BCR mRNA in cells from 31 of 44 BCR-ABL positive CML patients and 3 of 5 CML cell lines. Of the 34 positive samples, 31 had classical t(9;22) (q34;q11) translocations; in 3 samples there was no Philadelphia (Ph) and/or 9q+ chromosomes. ABL-BCR expression consisted of ABL(Ib)-BCR mRNA

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23

Melo, JV, DE Gordon, NC Cross, and JM Goldman. "The ABL-BCR fusion gene is expressed in chronic myeloid leukemia." Blood 81, no. 1 (1993): 158–65. http://dx.doi.org/10.1182/blood.v81.1.158.bloodjournal811158.

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Although the BCR-ABL hybrid gene on chromosome 22q-plays a pivotal role in the pathogenesis of chronic myeloid leukemia (CML), little is known of the reciprocal chimeric gene, ABL-BCR, formed on chromosome 9q+. By reverse transcription/polymerase chain reaction amplification (RT/PCR) we have detected ABL-BCR mRNA in cells from 31 of 44 BCR-ABL positive CML patients and 3 of 5 CML cell lines. Of the 34 positive samples, 31 had classical t(9;22) (q34;q11) translocations; in 3 samples there was no Philadelphia (Ph) and/or 9q+ chromosomes. ABL-BCR expression consisted of ABL(Ib)-BCR mRNA in 26 pat

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24

Saglio, G., F. Pane, E. Gottardi, et al. "Consistent amounts of acute leukemia-associated P190BCR/ABL transcripts are expressed by chronic myelogenous leukemia patients at diagnosis." Blood 87, no. 3 (1996): 1075–80. http://dx.doi.org/10.1182/blood.v87.3.1075.bloodjournal8731075.

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In chronic myelogenous leukemia (CML), the Philadelphia (Ph) chromosome translocation results in the formation of BCR/ABL genes, normally transcribed in two types of hybrid transcripts with a b2a2 or b3a2 BCR/ABL junction, which give origin to 210-kD fusion proteins (P210). A third type of BCR/ABL (with e1a2 type of junction) has been identified in approximately 50% of the Ph-positive acute lymphoblastic leukemia (Ph+ALL) cases and results in the production of a BCR/ABL protein of 190 kD (P190). The presence of this transcript has been associated almost exclusively with the presence of an acut

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25

Carlesso, N., D. A. Frank, and J. D. Griffin. "Tyrosyl phosphorylation and DNA binding activity of signal transducers and activators of transcription (STAT) proteins in hematopoietic cell lines transformed by Bcr/Abl." Journal of Experimental Medicine 183, no. 3 (1996): 811–20. http://dx.doi.org/10.1084/jem.183.3.811.

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Bcr/Abl is a chimeric oncogene that can cause both acute and chronic human leukemias. Bcr/Abl-encoded proteins exhibit elevated kinase activity compared to c-Abl, but the mechanisms of transformation are largely unknown. Some of the biological effects of Bcr/Abl overlap with those of hematopoietic cytokines, particularly interleukin 3 (IL-3). Such effects include mitogenesis, enhanced survival, and enhanced basophilic differentiation. Therefore, it has been suggested that p210Bcr/Abl and the IL-3 receptor may activate some common signal transduction pathways. An important pathway for IL-3 sign

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26

Mukhopadhyay, Soma, Ujjal Kanti Roy, Ritwik Pandey, et al. "Flow Cytometry Detection of BCR-ABL Fusion Proteins in Leukemia Patients- An Indian Experience." Blood 114, no. 22 (2009): 4710. http://dx.doi.org/10.1182/blood.v114.22.4710.4710.

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Abstract Abstract 4710 Background The BCR-ABL fusion gene results from the translocation t(9;22). It is the hallmark of chronic myeloid leukemia (CML) and is present in a poor risk subgroup of precursor B cell Acute Lymphoblastic Leukemia(ALL),which represents 25 to 30% of adult ALL and 3 to 5 % of childhood ALL. So far, the BCR-ABL aberration has been detected by cytogenetics, FISH or PCR, all techniques that are time consuming and require special facilities. We developed a simple flow cytometric bead assay for detection of the BCR-ABL fusion protein in cell lysates,using a bead bound catchin

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27

Okabe, Seiichi, Tetsuzo Tauchi, Yuko Tanaka, Seiichiro Katagiri, Toshihiko Kitahara, and Kazuma Ohyashiki. "Activity Of Omacetaxine Mepesuccinate Against Ponatinib Resistant Philadelphia Chromosome Positive Leukemia Cells." Blood 122, no. 21 (2013): 3840. http://dx.doi.org/10.1182/blood.v122.21.3840.3840.

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Abstract Chronic myeloid leukemia (CML) is characterized by cytogenetic aberration (Philadelphia chromosome: Ph) and chimeric tyrosine kinase BCR-ABL. ABL tyrosine kinase inhibitor (TKI) therapy (e.g. imatinib, nilotinib and dasatinib) has improved the survival of Ph-positive leukemia patients. However, despite the impressive efficacy of these agents, disease relapse has been observed in clinically. Mutations in the BCR-ABL kinase domain can cause of ABL TKI resistance. In particular, one of the BCR-ABL kinase domain mutations (e.g. T315I) is associated with a high level of resistance to all a

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28

Eiring, Anna M., Paolo Neviani, Ramasamy Santhanam, et al. "Requirement of the E2F3 Transcription Factor for BCR/ABL Leukemogenesis." Blood 110, no. 11 (2007): 33. http://dx.doi.org/10.1182/blood.v110.11.33.33.

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Abstract Several RNA binding proteins (RBPs) have been implicated in the progression of chronic myelogenous leukemia (CML) from the indolent chronic phase to the aggressively fatal blast crisis. In the latter phase, expression and function of specific RBPs are altered at transcriptional or post-translational levels by the increased constitutive kinase activity of the BCR/ABL oncoprotein, resulting in enhanced resistance to apoptotic stimuli, growth advantage and differentiation arrest of CD34+ CML blast crisis (CML-BC) progenitors. In the current study, we identified by RIP (RNA immunoprecipit

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29

Oyake, Tatsuo, Shigeki Ito, Shugo Kowata, Kazunori Murai, and Yoji Ishida. "Deguelin Induces Cell Growth Arrest and Cell Death Via the Suppression of BCR-ABL and Survivin Expression in BCR-ABL-T315I Mutant Cells." Blood 114, no. 22 (2009): 4255. http://dx.doi.org/10.1182/blood.v114.22.4255.4255.

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Abstract Abstract 4255 Development of kinase domain mutation is a major drug-resistance mechanism for tyrosine kinase inhibitor (TKI) in cancer therapy. A particularly challenging example is found in Philadelphia chromosome-positive chronic myelogenous leukemia (CML) where TKI STI571 is ineffective against the BCR-ABL mutant, E255K or T315I. Therefore, new agents that effectively kill these cells with kinase domain mutation are absolutely necessary. Deguelin is a rotenoid from African plant Mundulea sericea, which has been recently shown to suppress the lung tumorigenesis via inhibiting the ac

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30

Jimenez, Judy, Min Zhang, Marian L. Waterman, and Tiong Ong. "Bcr-Abl Regulates IRES-Dependent Translation of Lymphoid Enhancer Factor-1 in Chronic Myelogenous Leukemia." Blood 108, no. 11 (2006): 2124. http://dx.doi.org/10.1182/blood.v108.11.2124.2124.

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Abstract The constitutive tyrosine kinase activity of Bcr-Abl leads to aberrant expression of multiple genes by several mechanisms, including dysregulation of transcription. Recently though, increasing attention has been focused on the effect of Bcr-Abl in dysregulating translation. Our group has previously documented the effects of Bcr-Abl on key regulators of cap-dependent translation and the role that this mechanism plays in transformation (Ly et al, Cancer Research, 2003; Prabhu et al., Oncogene, in press). Here we describe a novel form of translational control by Bcr-Abl. Specifically, we

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31

Bracco, Enrico, Erika Deklic, Valentina Rosso, et al. "Nck Beta Adapter Protein Coordinates Bcr-Abl/Sam68 Intermolecular Interaction." Blood 112, no. 11 (2008): 1093. http://dx.doi.org/10.1182/blood.v112.11.1093.1093.

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Abstract Background: Philadelphia positive (Ph+) disorders, such as Chronic Myelogenous Leukemia (CML) are characterized by the presence of abnormal chromosome rising from translocation between chromosome 9 and 22 thus giving birth to a chimeric oncogenic protein named Bcr-Abl. This oncogenic kinase displays constitutive tyrosine kinase activity which leads to tyrosine residues autophosphorylation, in turn recruiting SH2 and/or PTB containing proteins. In the last decade Bcr-Abl targeted therapy has been successfully employed and, among currently available drugs inhibiting Bcr-Abl activity, Im

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32

Ziegler, Patrick, Stefan Balabanov, Ulrike Hartmann, Winfried Kammer Kammer, Alfred Nordheim, and Tim H. Brummendorf. "Identification of BCR-ABL Dependent Gene Regulation by Using a Phosphoproteomics Approach." Blood 104, no. 11 (2004): 2944. http://dx.doi.org/10.1182/blood.v104.11.2944.2944.

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Abstract Introduction: The selective tyrosine kinase inhibitor imatinib (formerly STI571, Glivecâ) has been shown to block phosphorylation of tyrosine residues by occupying the ATP binding site of the Abl tyrosine kinases Bcr-Abl, c-Abl, v-Abl and Abl-related gene (ARG), as well as platelet-derived growth factor receptor (PDGF) alpha and beta and of the receptor for human stem cell factor (SCF) c-kit. We chose a large scale phospho-proteomics approach to identify novel downstream targets of imatinib which could possibly be utilized for combined treatment strategies. Material and Methods: Phos

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Melo, Junia V., and Duncan R. Hewett. "Wrapping BCR-ABL: it's in the bag." Blood 116, no. 18 (2010): 3382–83. http://dx.doi.org/10.1182/blood-2010-08-300608.

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Abstract Leukemia, with its origin in a specific genetic abnormality, will only arise if the cell properly folds and processes the oncogenic protein encoded by the mutant gene. In this issue of Blood, Tsukahara and Maru describe a set of proteins that control the processing of the nascent BCR-ABL oncoprotein, providing new avenues for potential therapeutic intervention in chronic myelogenous leukemia (CML).

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Balabanov, Stefan, Artur Gontarewicz, Patrick Ziegler, et al. "Hypusination of eukaryotic initiation factor 5A (eIF5A): a novel therapeutic target in BCR-ABL–positive leukemias identified by a proteomics approach." Blood 109, no. 4 (2006): 1701–11. http://dx.doi.org/10.1182/blood-2005-03-037648.

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AbstractInhibition of BCR-ABL tyrosine kinase with imatinib represents a major breakthrough in the treatment of patients with chronic myeloid leukemia (CML). However, resistance to imatinib develops frequently, particularly in late-stage disease. To identify new cellular BCR-ABL downstream targets, we analyzed differences in global protein expression in BCR-ABL–positive K562 cells treated with or without imatinib in vitro. Among the 19 proteins found to be differentially expressed, we detected the down-regulation of eukaryotic initiation factor 5A (eIF5A), a protein essential for cell prolifer

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Guo, JQ, JY Lian, YM Xian, et al. "BCR-ABL protein expression in peripheral blood cells of chronic myelogenous leukemia patients undergoing therapy." Blood 83, no. 12 (1994): 3629–37. http://dx.doi.org/10.1182/blood.v83.12.3629.3629.

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Abstract Chronic myelogenous leukemia (CML) is a myeloproliferative disorder associated with the Philadelphia chromosome (Ph1) in more than 95% of these patients. The Ph1 and the resulting BCR-ABL fused genes are markers for this type of leukemia. In CML, the product of the fused BCR- ABL gene is typically a protein of approximately 2,000 amino acids termed P210 BCR-ABL. We have developed an assay for the BCR-ABL protein involving Western blotting of circulating white blood cells (WBC) with an anti-ABL monoclonal antibody that can detect P210 BCR-ABL and P145 ABL in peripheral blood cells from

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Guo, JQ, JY Lian, YM Xian, et al. "BCR-ABL protein expression in peripheral blood cells of chronic myelogenous leukemia patients undergoing therapy." Blood 83, no. 12 (1994): 3629–37. http://dx.doi.org/10.1182/blood.v83.12.3629.bloodjournal83123629.

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Chronic myelogenous leukemia (CML) is a myeloproliferative disorder associated with the Philadelphia chromosome (Ph1) in more than 95% of these patients. The Ph1 and the resulting BCR-ABL fused genes are markers for this type of leukemia. In CML, the product of the fused BCR- ABL gene is typically a protein of approximately 2,000 amino acids termed P210 BCR-ABL. We have developed an assay for the BCR-ABL protein involving Western blotting of circulating white blood cells (WBC) with an anti-ABL monoclonal antibody that can detect P210 BCR-ABL and P145 ABL in peripheral blood cells from chronic

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Coutinho, Sunita, Thomas Jahn, Marc Lewitzky, et al. "Characterization of Grb4, an adapter protein interacting with Bcr-Abl." Blood 96, no. 2 (2000): 618–24. http://dx.doi.org/10.1182/blood.v96.2.618.

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Abstract We report here the characterization of an adapter protein identified in a yeast 2-hybrid screen with the use of Bcr-Abl as the bait. Grb4 bound to Bcr-Abl in a variety of systems, both in vitro and in vivo, and is an excellent substrate of the Bcr-Abl tyrosine kinase. The association of Grb4 and Bcr-Abl in intact cells was mediated by an src homology (SH)2–mediated phosphotyrosine-dependent interaction as well as an SH3-mediated phosphotyrosine-independent interaction. Grb4 has 68% homology to the adapter protein Nck and has similar but distinct binding specificities in K562 lysates.

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Coutinho, Sunita, Thomas Jahn, Marc Lewitzky, et al. "Characterization of Grb4, an adapter protein interacting with Bcr-Abl." Blood 96, no. 2 (2000): 618–24. http://dx.doi.org/10.1182/blood.v96.2.618.014k06_618_624.

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We report here the characterization of an adapter protein identified in a yeast 2-hybrid screen with the use of Bcr-Abl as the bait. Grb4 bound to Bcr-Abl in a variety of systems, both in vitro and in vivo, and is an excellent substrate of the Bcr-Abl tyrosine kinase. The association of Grb4 and Bcr-Abl in intact cells was mediated by an src homology (SH)2–mediated phosphotyrosine-dependent interaction as well as an SH3-mediated phosphotyrosine-independent interaction. Grb4 has 68% homology to the adapter protein Nck and has similar but distinct binding specificities in K562 lysates. Subcellul

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Khajapeer, Kalubai Vari, and Rajasekaran Baskaran. "Hsp90 Inhibitors for the Treatment of Chronic Myeloid Leukemia." Leukemia Research and Treatment 2015 (December 3, 2015): 1–16. http://dx.doi.org/10.1155/2015/757694.

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Chronic myeloid leukemia (CML) is a hematological malignancy that arises due to reciprocal translocation of 3′ sequences from c-Abelson (ABL) protooncogene of chromosome 9 with 5′ sequence of truncated break point cluster region (BCR) on chromosome 22. BCR-ABL is a functional oncoprotein p210 that exhibits constitutively activated tyrosine kinase causing genomic alteration of hematopoietic stem cells. BCR-ABL specific tyrosine kinase inhibitors (TKIs) successfully block CML progression. However, drug resistance owing to BCR-ABL mutations and overexpression is still an issue. Heat-shock protein

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Jilani, I., H. Kantarjian, H. Faraji, et al. "Measurement of Free Circulating Bcr-Abl Fusion Protein and Its Phosphorylation in Patients with Chronic Myeloid Leukemia." Blood 106, no. 11 (2005): 2006. http://dx.doi.org/10.1182/blood.v106.11.2006.2006.

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Abstract Diagnosis and monitoring of therapy in chronic myeloid leukemia (CML) depend on cytogenetic, FISH, and PCR assays for detecting the fusion bcr-abl gene. However, the there is an inherent variability and difficulty in standardizing quantitative PCR-based assays. We assessed the utility of a simplified immunoassay for measuring levels of Bcr-Abl protein and phosphorylated Bcr-Abl for diagnosis of CML and detection of minimal residual disease (MRD). Bcr-Abl protein was immunoprecipitated on beads with anti-Bcr antibody, and the fusion protein was detected with anti-Abl antibody. Phosphor

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Tao, Wenjing, Hui Lin, Tong Sun, Ajoy K. Samanta, and Ralph B. Arlinghaus. "Oncogenic Transformation of NIH 3T3 Fibroblasts by BCR-ABL Oncoprotein Requires the IL-3 Receptor." Blood 110, no. 11 (2007): 3370. http://dx.doi.org/10.1182/blood.v110.11.3370.3370.

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Abstract Bcr-Abl is a leukemia-inducing protein, which causes oncogenic transformation of myeloid progenitors in Philadelphia chromosome (Ph)-positive chronic myeloid leukemia (CML) and lymphoid progenitors in Ph+ acute lymphoid leukemia (ALL). Oncogenic transformation of hematopoietic cells by the Bcr-Abl oncoprotein directly involves the activation Jak2 tyrosine kinase and the Stat5 transcription factor. Both proteins are normally linked to the IL-3/GM-CSF receptors for growth and survival. Since fibroblastic cells are not targets of BCR-ABL induced oncogenesis, we determined whether forced

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Bartholomeusz, Geoffrey A., Moshe Talpaz, Vaibhav Kapuria, et al. "Activation of a novel Bcr/Abl destruction pathway by WP1130 induces apoptosis of chronic myelogenous leukemia cells." Blood 109, no. 8 (2007): 3470–78. http://dx.doi.org/10.1182/blood-2006-02-005579.

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Abstract Imatinib mesylate (Gleevec) is effective therapy against Philadelphia chromosome–positive leukemia, but resistance develops in all phases of the disease. Bcr/Abl point mutations and other alterations reduce the kinase inhibitory activity of imatinib mesylate; thus, agents that target Bcr/Abl through unique mechanisms may be needed. Here we describe the activity of WP1130, a small molecule that specifically and rapidly down-regulates both wild-type and mutant Bcr/Abl protein without affecting bcr/abl gene expression in chronic myelogenous leukemia (CML) cells. Loss of Bcr/Abl protein c

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Mandanas, RA, DS Leibowitz, K. Gharehbaghi, et al. "Role of p21 RAS in p210 bcr-abl transformation of murine myeloid cells." Blood 82, no. 6 (1993): 1838–47. http://dx.doi.org/10.1182/blood.v82.6.1838.1838.

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Abstract The p21 RAS product has been implicated as part of the downstream signaling of certain nonreceptor tyrosine kinase oncogenes and several growth factor receptor-ligand interactions. We have reported that the chronic myelogenous leukemia oncogene p210 bcr-abl transforms a growth- factor-dependent myeloid cell line NFS/N1.H7 to interleukin-3 (IL-3) independence. In these p210 bcr-abl-transformed cells (H7 bcr-abl.A54) and in two other murine myeloid cell lines transformed to IL-3 independence by p210 bcr-abl, endogenous p21 RAS is activated as determined by an elevated ratio of associate

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Mandanas, RA, DS Leibowitz, K. Gharehbaghi, et al. "Role of p21 RAS in p210 bcr-abl transformation of murine myeloid cells." Blood 82, no. 6 (1993): 1838–47. http://dx.doi.org/10.1182/blood.v82.6.1838.bloodjournal8261838.

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The p21 RAS product has been implicated as part of the downstream signaling of certain nonreceptor tyrosine kinase oncogenes and several growth factor receptor-ligand interactions. We have reported that the chronic myelogenous leukemia oncogene p210 bcr-abl transforms a growth- factor-dependent myeloid cell line NFS/N1.H7 to interleukin-3 (IL-3) independence. In these p210 bcr-abl-transformed cells (H7 bcr-abl.A54) and in two other murine myeloid cell lines transformed to IL-3 independence by p210 bcr-abl, endogenous p21 RAS is activated as determined by an elevated ratio of associated guanosi

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Tabayashi, Takayuki, Sigal Gery, Maya Koren-Michowitz, and H. Phillip Koeffler. "Adaptor Protein Lnk Negatively Regulates Bcr-Abl-Induced Cell Proliferation through Inhibition of the Stat5 Signaling Pathway." Blood 116, no. 21 (2010): 3406. http://dx.doi.org/10.1182/blood.v116.21.3406.3406.

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Abstract Abstract 3406 Adaptor protein Lnk negatively regulates not only several hematopoietic cytokine receptors including MPL, EpoR and c-Kit, but also non-receptor tyrosine kinases such as JAK2 and Src. Our previous studies demonstrated that Lnk, when expressed in hematopoietic cell lines, binds and regulates the mutant proteins, JAK2V617F and MPLW515L. Recent in vivo studies have shown that Lnk has an important role in the development of myeloproliferative neoplasms. These data suggest that Lnk may have the ability to inhibit constitutively activated signaling pathways in hematopoietic mal

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Schemionek, Mirle, Shuchi Agrawal, Martin Stehling, et al. "Mtss1 Suppresses BCR-ABL Induced Cell Migration and Is Downregulated in CML Stem Cells." Blood 112, no. 11 (2008): 1077. http://dx.doi.org/10.1182/blood.v112.11.1077.1077.

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Abstract Migration and adhesion properties of hematopoietic stem cells (HSC) are disrupted in chronic myeloid leukemia (CML). Egression of these cells from the bone marrow is associated with cytoskeletal changes including actin remodeling. In a microarray screen of differentially regulated genes in HSC from BCR-ABL positive transgenic mice, we found downregulation of multiple genes involved in actin-associated changes of cell structure, adhesion, and migration (i.e. intersectin-1, cortactin, Mtss1, synaptopodin, and Gem GTPase). Mtss1 was further studied since it has been described to be a bin

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Balabanov, Stefan, Thoma Wilhelm, Simone Venz, et al. "Identification of Novel Biomarkers for Prediction of Response to Tyrosine Kinase Inhibitors (TKIs) by Proteomic Profiling of Imatinib as Well as 2nd and 3rd Generation TKIs in Vitro." Blood 112, no. 11 (2008): 336. http://dx.doi.org/10.1182/blood.v112.11.336.336.

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Abstract The tyrosine kinase inhibitor (TKI) Imatinib (IM) represents the gold standard firstline treatment for patients with newly diagnosed chronic myeloid leukemia (CML). For patients developing resistance or intolerance to Imatinib, the 2nd generation TKIs Dasatinib (DASA) and Nilotinib (NILO) which are approved, and Bosutinib (BOSU) which is in clinical development, possess activity against almost all mutant forms of BCR-ABL which confer Imatinib-resistance, except the gatekeeper mutation, T315I. This latter mutation occurs in approximately 15% of clinically observed mutations in chronic

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Shi, Chong-Shan, Joseph M. Tuscano, Owen N. Witte, and John H. Kehrl. "GCKR Links the Bcr-Abl Oncogene and Ras to the Stress-Activated Protein Kinase Pathway." Blood 93, no. 4 (1999): 1338–45. http://dx.doi.org/10.1182/blood.v93.4.1338.

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Abstract The Bcr-Abl oncogene, found in Philadelphia chromosome-positive myelogenous leukemia (CML), activates Ras and triggers the stress-activated protein kinase (SAPK or Jun NH2-terminal kinase [JNK]) pathway. Interruption of Ras or SAPK activation dramatically reduces Bcr-Abl–mediated transformation. Here, we report that Bcr-Abl through a Ras-dependent pathway signals the serine/threonine protein kinase GCKR (Germinal Center Kinase Related) leading to SAPK activation. Either an oncogenic form of Ras or Bcr-Abl enhances GCKR catalytic activity and its activation of SAPK, whereas inhibition

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Shi, Chong-Shan, Joseph M. Tuscano, Owen N. Witte, and John H. Kehrl. "GCKR Links the Bcr-Abl Oncogene and Ras to the Stress-Activated Protein Kinase Pathway." Blood 93, no. 4 (1999): 1338–45. http://dx.doi.org/10.1182/blood.v93.4.1338.404k27_1338_1345.

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The Bcr-Abl oncogene, found in Philadelphia chromosome-positive myelogenous leukemia (CML), activates Ras and triggers the stress-activated protein kinase (SAPK or Jun NH2-terminal kinase [JNK]) pathway. Interruption of Ras or SAPK activation dramatically reduces Bcr-Abl–mediated transformation. Here, we report that Bcr-Abl through a Ras-dependent pathway signals the serine/threonine protein kinase GCKR (Germinal Center Kinase Related) leading to SAPK activation. Either an oncogenic form of Ras or Bcr-Abl enhances GCKR catalytic activity and its activation of SAPK, whereas inhibition of GCKR i

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Donato, Nicholas, Vaibhav Kapuria, Hanshi Sun, et al. "Degrasyn-Induced Trafficking of BCR-ABL as a Novel Mechanism of Kinase Inactivation." Blood 110, no. 11 (2007): 1003. http://dx.doi.org/10.1182/blood.v110.11.1003.1003.

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Abstract Inhibitors that inactivate specific tyrosine kinases have proven to be a very effective form of therapy of many leukemias and hematopoetic disorders. Most inhibitors function by competing for the ATP-binding pocket or by preventing association with protein substrates. However, clinical and molecular studies have shown that small changes in the structure of the target kinase (point mutations, post-translational modification) affect inhibitor binding affinities, resulting in resistance to this class of inhibitor. Therefore, development of agents that reduce the activity of leukemogenic

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