About this Research Topic
The “sweet” attachment are among the most important posttranslational modifications (PTMs) for protein and of intrigued complex character comparing to DNA and naked protein. Indeed, over 50%-70% proteins in circulation or tissues are glycosylated and glycan parts have versatile structural and functional implications. Both the configuration and composition of the attached glycans affect the activities of consensus proteins significantly. However, glycosylation is generated by complex biosynthetic pathways comprising hundreds of glycosyltransferase, glycosidases, transcriptional factors, ion channels and other proteins. In addition, absence of direct genetic templates and glyco-specific antibodies as were commonly used in DNA amplification and protein capture makes the research on glycans and glycoproteins even more difficult and thus the understanding of the pathophysiological implications of glycosylation were hampers. Fortunately, recent technological advances including MALDI-TOF/TOF-MS, capillary electrophoresis, lectin microarrays, lectin-mediated affinity capture glycopeptides have afforded new opportunities and approaches for investigating disease-, especially cancer-related glycomics. Aberrant glycosylation has been demonstrated to be closely related to carcinogenesis, fibrogenesis, infectious diseases, congenital diseases, etc. Furthermore, several studies have revealed that glycan markers might become a promising filed for cancer biomarker development.
This topic “glycomics and cancer” collection organize reviews and original research articles focusing on the pathogenesis and biomarker identification, based on glycosylation alterations and in cancers including hepatocellular carcinoma (HCC), haematological malignancies, colorectal cancer, breast cancer, and other cancers. Potential topics include, but are not limited to: aberrant glycan expression in cancer cells, glycan as biomarkers in clinical diagnosis, functional roles of glycosyltransferase and glycosidases in cancer progression, advanced strategies in glycomics and glycoproteomics.
Theoretically, glycosylation is finished mainly by liver and B-lymphocyte. Four of the well-characterized glycosylation changes in cancer development and metastasis are bisecting, branching, fucosylation and sialylation. As one of the most abundant components of circulating glycoproteins, IgG is becoming a candidate target protein for glycosylation analysis. The structural character of immunoglobulins in monoclonal gammopathy which is characterized by B cell clonal expansion, as well as that in other malignancies, might indicate disease development and progression (Gao CF, et al.). Similarly, liver diseases including HCC are also among the hot targets for glycosylation exploration. New glycan markers for liver fibrosis, cirrhosis, carcinogenesis and metastasis were increasingly recognized (Gao CF, Lu HJ, Li Z, et al); The large retrospective clinical assessment of core-fucosylated α-fetoprotein (AFP-L3) in a cohort over 10 000 cases of HCC by Gao's team would show the virtue efficacy of core-fucosylated AFP as tumor marker in clinical diagnosis and followed up monitoring. The mechanism behind the aberrant glycosylation in EMT, tumor metastasis investigated by Guan's team indicated the Akt pathways and glycosylation of CD147 involved.
Last but not least, Prof Lu's team has developed a series of novel strategies (e.g. functional nanomaterial assisted enrichment and mass spectrometric analysis), making the detection of low abundant proteins and post translational modification proteins especially glycoproteins in complex background became more sensitive and selective. The sensitivity was increased more than 2 orders of magnitudes and the selectivity was improved 2-3 orders of magnitudes. These strategies were successfully used for high-throughput analysis of the biomarkers of diseases and Lu's team were invited to write several important reviews (ChemSoc Rev, Nat Sci Rev et al.).
Conclusively, glycomics is a mystery waiting for mining. Glycomic era is believed to be on the way coming next to genomic and proteomic in following five to ten years.
The topic "glycomics and cancer" is believed to be interesting to the readers and we believe the translation of the research finding is not far away for clinical application.
This topic “glycomics and cancer” collection organize reviews and original research articles focusing on the pathogenesis and biomarker identification, based on glycosylation alterations and in cancers including hepatocellular carcinoma (HCC), haematological malignancies, colorectal cancer, breast cancer, and other cancers. Potential topics include, but are not limited to: aberrant glycan expression in cancer cells, glycan as biomarkers in clinical diagnosis, functional roles of glycosyltransferase and glycosidases in cancer progression, advanced strategies in glycomics and glycoproteomics.
Theoretically, glycosylation is finished mainly by liver and B-lymphocyte. Four of the well-characterized glycosylation changes in cancer development and metastasis are bisecting, branching, fucosylation and sialylation. As one of the most abundant components of circulating glycoproteins, IgG is becoming a candidate target protein for glycosylation analysis. The structural character of immunoglobulins in monoclonal gammopathy which is characterized by B cell clonal expansion, as well as that in other malignancies, might indicate disease development and progression (Gao CF, et al.). Similarly, liver diseases including HCC are also among the hot targets for glycosylation exploration. New glycan markers for liver fibrosis, cirrhosis, carcinogenesis and metastasis were increasingly recognized (Gao CF, Lu HJ, Li Z, et al); The large retrospective clinical assessment of core-fucosylated α-fetoprotein (AFP-L3) in a cohort over 10 000 cases of HCC by Gao's team would show the virtue efficacy of core-fucosylated AFP as tumor marker in clinical diagnosis and followed up monitoring. The mechanism behind the aberrant glycosylation in EMT, tumor metastasis investigated by Guan's team indicated the Akt pathways and glycosylation of CD147 involved.
Last but not least, Prof Lu's team has developed a series of novel strategies (e.g. functional nanomaterial assisted enrichment and mass spectrometric analysis), making the detection of low abundant proteins and post translational modification proteins especially glycoproteins in complex background became more sensitive and selective. The sensitivity was increased more than 2 orders of magnitudes and the selectivity was improved 2-3 orders of magnitudes. These strategies were successfully used for high-throughput analysis of the biomarkers of diseases and Lu's team were invited to write several important reviews (ChemSoc Rev, Nat Sci Rev et al.).
Conclusively, glycomics is a mystery waiting for mining. Glycomic era is believed to be on the way coming next to genomic and proteomic in following five to ten years.
The topic "glycomics and cancer" is believed to be interesting to the readers and we believe the translation of the research finding is not far away for clinical application.
Keywords: Glycosylation, biomarker, hepatocellular carcinoma, breast cancer, colon rectal cancer
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