Identification of N-Glycosylation in Hepatocellular Carcinoma Patients’ Serum with a Comparative Proteomic ApproachReport as inadecuate




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Aim

This study is to explore the different expressions of serum N-glycoproteins and glycosylation sites between hepatocellular carcinoma HCC patients and healthy controls.

Method

We combined high abundant proteins depletion and hydrophilic affinity method to enrich the glycoproteins. Through liquid chromatography-tandem mass spectrometry LC-MS-MS, we extensively surveyed different expressions of glycosylation sites and glycoproteins between the two groups.

Result

This approach identified 152 glycosylation sites and 54 glycoproteins expressed differently between HCC patients and healthy controls. With the absolute values of Pearson coefficients of at least 0.8, eight proteins were identified significantly up or down regulated in HCC serum. Those proteins are supposed to be involved in several biological processes, cellular components and molecular functions of hepatocarcinogenesis. Several of them had been reported abnormally regulated in several kinds of malignant tumors, and may be promising biomarkers of HCC.

Conclusion

Our work provides a systematic and quantitative method of glycoproteomics and demonstrates some key changes in clinical HCC serum. These proteomic signatures may help to unveil the underlying mechanisms of hepatocarcinogenesis and may be useful for the exploration of candidate biomarkers.



Author: Yingnan Huang , Hao Wu , Ruyi Xue, Taotao Liu, Ling Dong, Jun Yao, Yang Zhang, Xizhong Shen

Source: http://plos.srce.hr/



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