Abstract
Gastrointestinal (GI) cancer remains one of the common causes of morbidity and mortality. A high number of cases are diagnosed at an advanced stage, leading to a poor survival rate. This is primarily attributed to the lack of reliable diagnostic biomarkers and limited treatment options. Therefore, more sensitive, specific biomarkers and curative treatments are desirable. Functional proteomics as a research area in the proteomic field aims to elucidate the biological function of unknown proteins and unravel the cellular mechanisms at the molecular level. Phosphoproteomic and glycoproteomic studies have emerged as two efficient functional proteomics approaches used to identify diagnostic biomarkers, therapeutic targets, the molecular basis of disease and mechanisms underlying drug resistance in GI cancers. In this review, we present an overview on how functional proteomics may contribute to the understanding of GI cancers, namely colorectal, gastric, hepatocellular carcinoma and pancreatic cancers. Moreover, we have summarized recent methodological developments in phosphoproteomics and glycoproteomics for GI cancer studies.
Highlights
Cancer is the third most leading cause of death worldwide after ischemic heart disease and stroke
Lin and colleagues combined stable isotope dimethylation labeling coupled with online 3D SCX-TiO2/RP using an LTQ-Orbitrap and super-SILAC mix coupled with selected ion monitoring/ accurate inclusion mass screening (SIM/AIMS), in order to develop a strategy for both the discovery and targeted verification of differentially phosphorylated proteins in three hepatocellular carcinoma (HCC) and their nearby tissue specimens
Phosphoproteomics and glycoproteomics have proved to be strongly efficient in GI cancer research, yielding important biological surprises even when other omics strategies were not informative
Summary
Cancer is the third most leading cause of death worldwide after ischemic heart disease and stroke. Protein phosphorylation primarily occurs on serine, threonine and tyrosine residues and the aberrant phosphorylation of critical regulatory proteins drives numerous molecular mechanisms during tumorigenesis [16], suggesting kinases as the therapeutic targets and phosphorylation-related events as reliable biomarkers. Glycosylation is another crucial form of protein post-translational modification that exists in about 50% of mammalian proteins [17]. Protein glycosylation plays a pivotal role in many biological pathways and molecular functions including cell–cell recognition, communication and adhesion, and has been shown to be altered during the process of tumor development and progression [4], providing an interesting field for cancer biomarker discovery. A comprehensive overview of developed strategies in these fields is provided
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