Normal and cancer cell line proteomes were profiled using high throughput mass spectrometry
techniques. Application of protein-level and peptide-level sample fractionation combined with LC−MS/MS analysis enabled identification of 2235 unmodified proteins representing a broad range of
functional and compartmental classes. An iterative multistep search strategy was used to identify post-translational modifications, revealing several proteins that are preferentially modified in cancer cells.
Information regarding both unmodified and modified protein forms was combined with publicly
available gene expression and protein−protein interaction data. The resulting integrated dataset revealed
several functionally related proteins that are differentially regulated between normal and cancer cell
lines.
Keywords: post-translational modifications • breast cancer • proteome • mass spectrometry • membrane proteins
• high throughput • subcellular • multidimensional liquid chromatography • functional genomics • pathway