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头颈部鳞状细胞癌中蛋白质糖基化的变化

Changes in Protein Glycosylation in Head and Neck Squamous Cell Carcinoma.

作者信息

Liao Chengcheng, An Jiaxing, Tan Zhangxue, Xu Fangping, Liu Jianguo, Wang Qian

机构信息

Oral Disease Research Key Laboratory of Guizhou Tertiary Institution, School of Stomatology, Zunyi Medical University, Zunyi 563006, China.

Department of Gastroenterology, Affiliated Hospital of Zunyi Medical University, Zunyi 563000, China.

出版信息

J Cancer. 2021 Jan 1;12(5):1455-1466. doi: 10.7150/jca.51604. eCollection 2021.

DOI:10.7150/jca.51604
PMID:33531990
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7847636/
Abstract

Glycosylation is an important posttranslational modification of proteins, and it has a profound influence on diverse life processes. An abnormal polysaccharide structure and mutation of the glycosylation pathway are closely correlated with human cancer progression. Glycoproteins such as EGFR, E-cadherin, CD44, PD-1/PD-L1, B7-H3 and Muc1 play important roles in the progression of head and neck squamous cell carcinoma (HNSCC), and their levels of glycosylation and changes in glycosyl structure are closely linked to HNSCC progression and malignant transformation. The regulation of protein glycosylation in HNSCC provides potential strategies to control cancer stem cell (CSC) subgroup expansion, epithelial-mesenchymal transition (EMT), tumor-related immunity escape and autophagy. Glycoproteins with altered glycosylation can be used as biomarkers for the early diagnosis, monitoring and prognostication of HNSCC. However, the glycobiology of cancer is still a new field that needs to be deeply studied, especially in HNSCC.

摘要

糖基化是蛋白质重要的翻译后修饰,对多种生命过程有深远影响。多糖结构异常和糖基化途径突变与人类癌症进展密切相关。表皮生长因子受体(EGFR)、E-钙黏蛋白、CD44、程序性死亡受体1/程序性死亡配体1(PD-1/PD-L1)、B7-H3和黏蛋白1(Muc1)等糖蛋白在头颈部鳞状细胞癌(HNSCC)进展中起重要作用,其糖基化水平和糖基结构变化与HNSCC进展及恶性转化密切相关。HNSCC中蛋白质糖基化的调控为控制癌症干细胞(CSC)亚群扩增、上皮-间质转化(EMT)、肿瘤相关免疫逃逸和自噬提供了潜在策略。糖基化改变的糖蛋白可作为HNSCC早期诊断、监测和预后的生物标志物。然而,癌症糖生物学仍是一个需要深入研究的新领域,尤其是在HNSCC中。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/48d9f65ac38e/jcav12p1455g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/25f2199c9bd8/jcav12p1455g001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/48d9f65ac38e/jcav12p1455g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/25f2199c9bd8/jcav12p1455g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/be0d91488317/jcav12p1455g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/0503ad250813/jcav12p1455g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/b9ad/7847636/48d9f65ac38e/jcav12p1455g004.jpg

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