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Introduction
Acute promyelocytic leukemia (APL) is identified as the M3 subtype of acute myeloid leukemia (AML) and it appears to be the most malignant form of AML, characterized by a severe bleeding tendency and a fatal course of only weeks. Cytogenetically, a specific chromosome translocation, t(15;17)(q22;q21), occurs in more than 95% of APL patients which results in the rearrangement of the promyelocytic leukemia (PML) and retinoic acid receptor α (RARα) genes and the expression of PML-RARα chimeric protein (1,2). The frontline treatment for APL is chemotherapy, including the use of anthracycline and cytosine arabinoside, with a complete remission (CR) rate of 75 to 80% in newly diagnosed patients. The use of arsenic trioxide (ATO) from the early 1990s has further improved the clinical outcome of refractory or relapsed APL, as well as newly diagnosed APL (3,4). NB4, a maturation inducible cell line with a t(15;17) marker, is the cell model most commonly used in APL research (5).
Following genomics and transcriptomics, proteomics is considered to be the next step in the study of biological systems (6). Proteomics is the large-scale study of proteins, particularly their structures and functions (7). One of the most promising developments to come from the study of human proteins has been the identification of potential new drugs for the treatment of disease (8). This relies on proteomic information to identify proteins associated with a disease, which computer software may then use as targets in the design of new drugs (8). A proteome is the entire set of proteins expressed by a genome, cell, tissue or organism. More specifically, it is the set of expressed proteins in a given type of cell or organism at a given time under defined conditions (9–11). Proteomics, the study of the proteome, has largely been practiced through the separation of proteins by two-dimensional gel electrophoresis (2-DE) (12,13). In the first dimension, the proteins are separated by isoelectric focusing (IEF), which resolves proteins on the basis of charge. In the second dimension, proteins are separated by molecular weight using SDS-PAGE. The gel is dyed with Coomassie Brilliant Blue or silver to visualize the proteins. Spots on the gel are proteins that have migrated to specific locations. The mass spectrometer has augmented proteomics (14,15). Peptide mass fingerprinting (PMF)...