Phosphatase and tensin homologue phosphorylation in the C-terminal regulatory domain is frequently observed in acute myeloid leukaemia and associated with poor clinical outcome
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Cheong, JW
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Cheong, JW
Eom, JI
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Eom, JI
Maeng, HY
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Maeng, HY
Lee, ST
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Lee, ST
Hahn, JS
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Hahn, JS
Ko, YW
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Ko, YW
Min, YH
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机构:Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
Min, YH
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[1] Yonsei Univ, Coll Med, Dept Internal Med, Seoul 120752, South Korea
[2] Yonsei Univ, Coll Med, Clin Res Ctr, Seoul 120752, South Korea
[3] Yonsei Univ, Coll Med, Brain Korean 21 Project Med Sci, Seoul 120752, South Korea
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.