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Phosphatase and Tensin Homologue Phosphorylation in the C-terminal Regulatory Domain is Frequently Observed in Acute Myeloid Leukaemia and Associated with Poor Clinical Outcome

Overview
Journal Br J Haematol
Specialty Hematology
Date 2003 Jul 25
PMID 12877673
Citations 29
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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.

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