The identification of protein biomarkers for acute myeloid leukemia (AML)
that could find applications in AML diagnosis and prognosis, treatment and the selection
for bone marrow transplant requires substantial comparative analyses of the proteomes
from AML patients. In the past years, several studies have suggested some
biomarkers for AML diagnosis or AML classification using methods for sample preparation
with low proteome coverage and low resolution mass spectrometers. However, most of the studies did not follow
up, confirm or validate their candidates with more patient samples. Current proteomics methods, new high resolution and
fast mass spectrometers allow the identification and quantification of several thousands of proteins obtained from few tens
of μg of AML cell lysate. Enrichment methods for posttranslational modifications (PTM), such as phosphorylation, can
isolate several thousands of site-specific phosphorylated peptides from AML patient samples, which subsequently can be
quantified with high confidence in new mass spectrometers. While recent reports aiming to propose proteomic or phosphoproteomic
biomarkers on the studied AML patient samples have taken advantage of the technological progress, the access
to large cohorts of AML patients to sample from and the availability of appropriate control samples still remain challenging.
Keywords: Acute myeloid leukemia, biomarker, mass spectrometry, proteomics, phosphoproteomics, diagnosis, prognosis.
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