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Amino Acids ; 40(3): 943-51, 2011 Mar.
Article in English | MEDLINE | ID: mdl-20711619

ABSTRACT

The aim of this study was to investigate the progression of myelodysplastic syndrome (MDS) to acute myeloid leukemia (AML) and to provide additional data regarding the proteomic analysis of AML. The protein profiles obtained were correlated to cytogenetic and molecular analyses. Bone marrow (BM) and peripheral blood (PB) samples were obtained during MDS diagnosis, at MDS transformation to AML, at de novo AML diagnosis and 3 months following treatment. As controls, non-leukemic pediatric patients were studied. Cytogenetic and molecular analyses were carried out by G banding and polymerase chain reaction followed by sequencing, respectively. Differential proteomic analysis was performed by two-dimensional gel electrophoresis and protein identification by matrix-assisted laser desorption ionization time-of-flight (MALDI-TOF) mass spectrometry. No significant correlations were noted between protein patterns and cytogenetic or molecular analyses. Certain suppressor genes, metabolic enzymes, immunoglobulins and actin-binding proteins were differentially expressed by BM or PB plasma and cell lysates compared to controls. The obtained data showed that vitamin D and gelsolin played contradicting roles in contributing and restraining leukemogenesis, while MOES, EZRI and AIFM1 could be considered as biomarkers for AML.


Subject(s)
Leukemia, Myeloid, Acute/genetics , Leukemia, Myeloid, Acute/metabolism , Myelodysplastic Syndromes/genetics , Myelodysplastic Syndromes/metabolism , Proteomics , Adolescent , Blood/metabolism , Blood Chemical Analysis , Bone Marrow/chemistry , Bone Marrow/metabolism , Child , Child, Preschool , Chromosome Aberrations , Cytogenetics , Electrophoresis, Gel, Two-Dimensional , Female , Humans , Infant , Male , Proteins/chemistry , Proteins/genetics , Proteins/metabolism , Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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