Abstract
Acute myeloid leukaemia (AML) is a type of cancer affecting all ages but it is more common in adults, as compared to children. Recent advancements in proteomics and mass spectrometry tools, offer a comprehensive solution to study the molecular complexity of diseases, such as cancers. This study is focused on the proteomic profiling of AML in comparison to healthy control for which, a systematic 5D proteomic approach for the fractionation of pooled plasma samples was used. Methodology includes depletion of Top-7 abundant proteins, ZOOM-isoelectric focusing (ZOOM-IEF), two-dimensional gel electrophoresis (2-DGE), and matrix-assisted laser desorption/ionization mass spectrometry (MALDI-MS) analysis followed by the validation of identified biomarker proteins using enzyme linked immunosorbent assay (ELISA). Up-/down-fold changes in concentration of proteins were observed in 2-DGE of AML in comparison with the healthy control and a total of 34 proteins were identified in fractioned plasma. Among them, fifteen proteins were significantly differentiated and five proteins; SAA1, complement factor C7, ApoE, plasminogen, and ApoA1 were later verified by ELISA in individual samples, which showed that SAA1 and plasminogen could be used as potential biomarker for AML.