Oncotarget

Research Papers:

GP73 N-glycosylation at Asn144 reduces hepatocellular carcinoma cell motility and invasiveness

Kai Jiang, Wei Li, Qinle Zhang, Guoquan Yan, Kun Guo, Shu Zhang _ and Yinkun Liu

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Oncotarget. 2016; 7:23530-23541. https://doi.org/10.18632/oncotarget.8120

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Abstract

Kai Jiang1,3, Wei Li2, Qinle Zhang2, Guoquan Yan2, Kun Guo1, Shu Zhang1, Yinkun Liu1,2

1Liver Cancer Institute, Zhongshan Hospital, Fudan University, Key Laboratory of Carcinogenesis and Cancer Invasion, Ministry of Education, Shanghai, China

2Cancer Research Center, Institutes of Biomedical Sciences, Fudan University, Shanghai, China

3Interdisciplinary Research Center on Biology and Chemistry, Shanghai Institute of Organic Chemistry, Chinese Academy of Sciences, Shanghai, China

Correspondence to:

Shu Zhang, e-mail: zhang.shu@zs-hospital.sh.cn

Keywords: Golgi protein 73, N-glycan, hepatocellular carcinoma

Received: October 13, 2015     Accepted: February 28, 2016     Published: March 16, 2016

ABSTRACT

Golgi Protein 73 (GP73) is a potential liver disease glycobiomarker warranting comprehensive analyses of its glycan structure and glycosylation function. In this study, we used mass spectrometry to identify glycosylation sites and the glycan structure, high-throughput lectin microarray to provide rapid and sensitive profiling of glycoconjugates, and site-directed mutagenesis to clarify the impact of glycans on target glycoproteins in vivo. We identified three GP73 N-glycosylation sites: Asn109, Asn144 and Asn398. We found five glycoforms on Asn144, including biantennary, triantennary and fucosylated glycans. Removal of N-glycans at Asn144 enhanced the motility and invasiveness of hepatocellular carcinoma cells, possibly due to inhibition of cell adhesion related to the changes of cell membrane glycosylation. This study increases our understanding of the functional relevance of GP73 glycosylation and suggests that Asn144-deleted GP73 can influence the progression and metastasis of hepatocellular carcinoma.


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