Abstract
Phosphorylation of PTEN (phosphatase and tensin homologue) affects PTEN protein stability and function. In this study, phosphorylated PTEN (pPTEN) was observed in 45 (73.8%) of 61 cases with acute myeloid leukaemia (AML). Phosphorylation of Akt and its downstream molecules [FKHR; Forkhead (Drosophila) homologue 1; and GSK-3beta; glycogen synthase kinase 3 beta] was significantly associated with pPTEN (P < 0.001). The complete remission rates were not different with respect to pPTEN, but overall survival was significantly shorter in patients with pPTEN (P < 0.05). Constitutive PTEN phosphorylation may add insight into the molecular pathogenesis of AML, and may be a new parameter for an unfavourable outcome.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acute Disease
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Adolescent
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Adult
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Aged
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Blotting, Western
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DNA-Binding Proteins / metabolism
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Female
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Forkhead Box Protein O1
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Forkhead Transcription Factors
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Glycogen Synthase Kinase 3 / metabolism
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Glycogen Synthase Kinase 3 beta
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Humans
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Leukemia, Myeloid / metabolism*
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Leukemia, Myeloid / mortality
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Male
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Middle Aged
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Multivariate Analysis
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PTEN Phosphohydrolase
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Phosphoric Monoester Hydrolases / analysis*
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Phosphorylation
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Prognosis
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Protein Serine-Threonine Kinases*
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Proto-Oncogene Proteins / metabolism
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Proto-Oncogene Proteins c-akt
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Statistics, Nonparametric
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Transcription Factors / metabolism
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Tumor Suppressor Proteins / analysis*
Substances
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DNA-Binding Proteins
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FOXO1 protein, human
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Forkhead Box Protein O1
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Forkhead Transcription Factors
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Proto-Oncogene Proteins
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Transcription Factors
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Tumor Suppressor Proteins
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AKT1 protein, human
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GSK3B protein, human
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Glycogen Synthase Kinase 3 beta
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Protein Serine-Threonine Kinases
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Proto-Oncogene Proteins c-akt
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Glycogen Synthase Kinase 3
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Phosphoric Monoester Hydrolases
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PTEN Phosphohydrolase
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PTEN protein, human