Phosphatase and tensin homologue phosphorylation in the C‐terminal regulatory domain is frequently observed in acute myeloid leukaemia and associated with poor …

JW Cheong, JI Eom, HY Maeng, ST Lee… - British journal of …, 2003 - Wiley Online Library
JW Cheong, JI Eom, HY Maeng, ST Lee, JS Hahn, YW Ko, YH Min
British journal of haematology, 2003Wiley Online Library
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‐3β; 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 …
Summary
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‐3β; 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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