Abstract
Mutations in the cytosolic 5' nucleotidase II (NT5C2) gene drive resistance to thiopurine chemotherapy in relapsed acute lymphoblastic leukemia (ALL). Mechanistically, NT5C2 mutant proteins have increased nucleotidase activity as a result of altered activating and autoregulatory switch-off mechanisms. Leukemias with NT5C2 mutations are chemoresistant to 6-mercaptopurine yet show impaired proliferation and self-renewal. Direct targeting of NT5C2 or inhibition of compensatory pathways active in NT5C2 mutant cells may antagonize the emergence of NT5C2 mutant clones driving resistance and relapse in ALL.
© 2019 by The American Society of Hematology.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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5'-Nucleotidase*
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Cell Proliferation* / drug effects
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Cell Proliferation* / genetics
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Drug Resistance, Neoplasm / drug effects
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Drug Resistance, Neoplasm / genetics
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Humans
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Mercaptopurine / therapeutic use*
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Mutation*
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Neoplasm Proteins* / genetics
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Neoplasm Proteins* / metabolism
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Precursor Cell Lymphoblastic Leukemia-Lymphoma* / drug therapy
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Precursor Cell Lymphoblastic Leukemia-Lymphoma* / enzymology
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Precursor Cell Lymphoblastic Leukemia-Lymphoma* / genetics
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Precursor Cell Lymphoblastic Leukemia-Lymphoma* / pathology
Substances
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Neoplasm Proteins
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Mercaptopurine
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5'-Nucleotidase
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NT5C2 protein, human