Abstract
Massive evidence suggests that genetic abnormalities contribute to the development of lung cancer. These molecular abnormalities may serve as diagnostic, prognostic and predictive biomarkers for this deadly disease. It is imperative to search these biomarkers in different tumorigenesis pathways so as to provide the most appropriate therapy for each individual patient with lung malignancy. Phosphoproteomics is a promising technology for the identification of biomarkers and novel therapeutic targets for cancer. Thousands of proteins interact via physical and chemical association. Moreover, some proteins can covalently modify other proteins post-translationally. These post-translational modifications ultimately give rise to the emergent functions of cells in sequence, space and time. Phosphoproteomics clinical researches imply the comprehensive analysis of the proteins that are expressed in cells or tissues and can be employed at different stages. In addition, understanding the functions of phosphorylated proteins requires the study of proteomes as linked systems rather than collections of individual protein molecules. In fact, proteomics approaches coupled with affinity chromatography strategies followed by mass spectrometry have been used to elucidate relevant biological questions. This article will discuss the relevant clues of post-translational modifications, phosphorylated proteins, and useful proteomics approaches to identify molecular cancer signatures. The recent progress in phosphoproteomics research in lung cancer will be also discussed.
Highlights
Lung cancer is the most commonly diagnosed cancer and the leading cause of cancer-related death worldwide [1]
As it is difficult to discuss the advantages and limitations of each type of instrument within the broad field of qualitative and quantitative phosphoprotein analysis, and since the development of mass spectrometers is occurring at a rapid pace, we suggest that experienced biological mass spectrometry (MS) labs be consulted during the planning stages of phosphoprotein experiments to determine the most appropriate instrumentation and methodologies likely to provide the desired results
liquid chromatography (LC)-field asymmetric waveform ion mobility spectrometry (FAIMS)-MS experiments performed on TiO2-enriched tryptic digests from Drosophila melanogaster provided a 50% increase in phosphopeptide identification compared to conventional LC-MS analysis
Summary
Lung cancer is the most commonly diagnosed cancer and the leading cause of cancer-related death worldwide [1]. Massive evidence suggests that genetic abnormalities contribute to the development of lung cancer These molecular abnormalities may serve as diagnostic, prognostic and predictive biomarkers for this deadly disease. Recent advances in phosphoproteomics technology enable the identification of biomarkers by proteome phosphorylation analysis in a variety of scenarios that can be implemented in biomedical research and translational setting [6]. Biomarkers prove to be vital for the identification of early cancer and those subjects at risk of developing cancer as a normal cell progresses through the complex process of transformation to a cancerous state [7,8,9,10,11,12,13,14]. This article will discuss the ongoing researches in post-translational modifications (PTMs), phosphorylated proteins, and useful proteomics approaches to identify molecular cancer signatures.
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