Cited by 103Acute Lymphoblastic Leukemia researchAmino Acid Enzymes and MetabolismBiochemical and Molecular Research

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A Genome-Wide View of the In vitro Response to l-Asparaginase in Acute Lymphoblastic Leukemia

Fine, Bernard M., Kaspers, Gertjan J.L., Ho, Minh, Loonen, Anne H., Boxer, Linda M.·2005·Cancer Research

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Abstract

To investigate the effect of l-asparaginase on acute lymphoblastic leukemia (ALL), we used cDNA microarrays to obtain a genome-wide view of gene expression both at baseline and after in vitro exposure to l-asparaginase in cell lines and pediatric ALL samples. In 16 cell lines, a baseline gene expression pattern distinguished l-asparaginase sensitivity from resistance. However, for 28 pediatric ALL samples, no consistent baseline expression pattern was associated with sensitivity to l-asparaginase. In particular, baseline expression of asparagine synthetase (ASNS) was not predictive of response to l-asparaginase. After exposure to l-asparaginase, 5 cell lines and 10 clinical samples exhibited very similar changes in the expression of a large number of genes. However, the gene expression changes occurred more slowly in the clinical samples. These changes included a consistent increase in expression of tRNA synthetases and solute transporters and activating transcription factor and CCAAT/enhancer binding protein family members, a response similar to that observed with amino acid starvation. There was also a consistent decrease in many genes associated with proliferation. Taken together, the changes seem to reflect a consistent coordinated response to asparagine starvation in both cell lines and clinical samples. Importantly, in the clinical samples, increased expression of ASNS after l-asparaginase exposure was not associated with in vitro resistance to l-asparaginase, indicating that ASNS-independent mechanisms of in vitro l-asparaginase resistance are common in ALL. These results suggest that targeting particular genes involved in the response to amino acid starvation in ALL cells may provide a novel way to overcome l-asparaginase resistance.

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Cluster analysis and display of genome-wide expression patterns
Eisen, M. B., Spellman, P. T., Brown, P. O., & Botstein, D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.25.14863 · Cited by 16,184
In silico prediction of protein-protein interactions in human macrophages
Souiai, O., Guerfali, F. Z., Miled, S. B., Brun, C., & Benkahla, A. (2014) · BMC Research Notes · doi:10.1186/1756-0500-7-157 · Cited by 10,785
Significance analysis of microarrays applied to the ionizing radiation response
Tusher, V. G., Tibshirani, R., & Chu, G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091062498 · Cited by 10,568
Quantitative Monitoring of Gene Expression Patterns with a Complementary DNA Microarray
Schena, M., Shalon, D., Davis, R. W., & Brown, P. O. (1995) · Science · doi:10.1126/science.270.5235.467 · Cited by 9,609
Cancer: Principles and Practice of Oncology.
(1991) · Annals of Internal Medicine · doi:10.7326/0003-4819-114-9-819_4 · Cited by 8,524
Genomic Expression Programs in the Response of Yeast Cells to Environmental Changes
Gasch, A. P., Spellman, P. T., Kao, C. M., Carmel-Harel, O., Eisen, M. B., Storz, G., Botstein, D., & Brown, P. O. (2000) · Molecular Biology of the Cell · doi:10.1091/mbc.11.12.4241 · Cited by 4,815
Diagnosis of multiple cancer types by shrunken centroids of gene expression
Tibshirani, R. J., Hastie, T. J., Narasimhan, B., & Chu, G. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.082099299 · Cited by 2,931
Involvement of a homolog of Drosophila trithorax by 11q23 chromosomal translocations in acute leukemias
Tkachuk, D., Köhler, S., & Cleary, M. L. (1992) · Cell · doi:10.1016/0092-8674(92)90602-9 · Cited by 913
Acute Lymphoblastic Leukemia
Pui, C., & Evans, W. E. (1998) · New England Journal of Medicine · doi:10.1056/nejm199808273390907 · Cited by 841
The t(4;11) chromosome translocation of human acute leukemias fuses the ALL-1 gene, related to Drosophila trithorax, to the AF-4 gene
Gu, Y., Nakamura, T., Alder, H., Prasad, R., Canaani, O. D., Cimino, G. G., Croce, C. M., & Canaani, E. (1992) · Cell · doi:10.1016/0092-8674(92)90603-a · Cited by 822

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Suto, H., Yasuda, H., Isobe, Y., Sasaki, M., Imai, H., Tsutsui, M., Oshimi, K., Komatsu, N., & Sugimoto, K. (2010) · Acta Haematologica · doi:10.1159/000313362 · Cited by 5
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Chen, J., Luo, J., Liu, Y., Zhou, J., Cui, H., & Deng, L. (2025) · Carcinogenesis · doi:10.1093/carcin/bgaf035 · Cited by 4
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He, Y., Li, B., Luo, C., Shen, S., Chen, J., Xue, H.-L., Tang, J., & Gu, L.-J. (2011) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-011-0243-4 · Cited by 4
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Pottier, N., Cheok, M. H.-C., & Kager, L. (2008) · Expert Review of Clinical Pharmacology · doi:10.1586/17512433.1.3.401 · Cited by 1
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Bullinger, L., & Fröhling, S. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-382227-7.00058-6 · Cited by 1
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Nardini, C., Masotti, D., Yoon, S., Macii, E., Kuo, M. D., Micheli, G. D., & Luca Benini, C. (2006) · IEEE Symposium on Computers and Communications (ISCC) · doi:10.1109/iscc.2006.101 · Cited by 1
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Bullinger, L., Döhner, H., & Pollack, J. R. (2009) · Elsevier eBooks · doi:10.1016/b978-0-12-369420-1.00070-6 · Cited by 1
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Bullinger, L., Döhner, H., & Pollack, J. R. (2008) · Humana Press eBooks · doi:10.1007/978-1-59745-576-3_8
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Kaspers, G. J. L. (2009) · Blood · doi:10.1182/blood-2009-01-198846
Self-citation
Molecular mechanisms of glucocorticoid resistance in childhood acute lymphoblastic leukemia
Tissing, W. J. E. (2006) · RePub (Erasmus University Rotterdam)
Genetic and BiologicalDiversity in TEL-AML1 Positive ALL
Stams, W. A. G. (2005) · RePub (Erasmus University Rotterdam)

Authors: Fine, B. M., Kaspers, G. J. L., Ho, M., Loonen, A. H., & Boxer, L. M.
Affiliations: Howard Hughes Medical Institute (US)
Amsterdam UMC Location Vrije Universiteit Amsterdam (NL)
VA Palo Alto Health Care System (US)
ORCID: Fine, Bernard M.
Kaspers, Gertjan J.L.
Venue: Cancer Research
Publisher: American Association for Cancer Research (AACR)
Published: 2005-01-01
Volume: 65
Issue: 1
Pages: 291-299
ISSN: 0008-5472 (ISSN-L)
1538-7445
DOI: 10.1158/0008-5472.291.65.1
OpenAlex: W1867192423
Cited by: 103
References: 52
Citations by year: 2025: 3 · 2024: 2 · 2023: 4 · 2022: 5 · 2021: 3 · 2020: 3 · 2019: 4 · 2018: 4 · 2017: 3 · 2016: 2 · 2015: 8 · 2014: 11 · 2012: 5
FWCI: 10.44
Type: journal article
Language: en
Open access: closed
Locations: Cancer Research (publishedVersion)
PubMed (publishedVersion)
Pure Amsterdam UMC (submittedVersion)
Data Archiving and Networked Services (DANS) (submittedVersion)
Funders: National Institutes of Health (1r01ca092326-01)
National Cancer Institute (CA85129, CA92326, K08CA095563, U01CA085129)
Topics: Health Sciences › Medicine › Hematology › Acute Lymphoblastic Leukemia research
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Amino Acid Enzymes and Metabolism
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
Keywords: L-asparaginase, acute lymphoblastic leukemia, pediatric leukemia, gene expression profiling, asparagine synthetase, drug resistance, tRNA synthetase, amino acid transporters, C/EBP transcription factors, cell proliferation, leukemia cell lines
MeSH terms: Adolescent, Antineoplastic Agents, Asparaginase, Child, Female, Humans, Male, Recurrence, Translocation, Genetic, Genome, Human, Artificial Gene Fusion, Cell Line, Tumor, Precursor Cell Lymphoblastic Leukemia-Lymphoma

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A Genome-Wide View of the In vitro Response to l-Asparaginase in Acute Lymphoblastic Leukemia

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