» Articles » PMID: 28315783

Role of Protein Glycosylation in Cancer Metastasis

Overview
Specialty Oncology
Date 2017 Mar 20
PMID 28315783
Citations 118
Authors
Affiliations
Soon will be listed here.
Abstract

Although altered glycosylation has been detected in human cancer cells decades ago, only investigations in the last years have enormously increased our knowledge about the details of protein glycosylation and its role in tumour progression. Many proteins, which are heavily glycosylated, i.e. adhesion proteins or proteases, play an important role in cancer metastasis that represents the crucial and frequently life-threatening step in progression of most tumour types. Compared to normal tissue, tumour cells often show altered glycosylation patters with appearance of new tumour-specific antigens. In this review, we give an overview about the role of glycosylation in tumour metastasis, describing recent results about O-glycans, N-glycans and glycosaminoglycans. We show that glycan structures, glycosylated proteins and glycosylation enzymes have influence on different steps of the metastatic process, including epithelial-mesenchymal transition (EMT), migration, invasion/intravasation and extravasation of tumour cells. Regarding the important role of cancer metastasis for patients survival, further knowledge about the consequences of altered glycosylation patterns in tumour cells is needed which might eventually lead to the development of novel therapeutic approaches.

Citing Articles

Intact glycopeptide analysis of human prostate tissue reveals site-specific heterogeneity of protein glycosylation in prostate cancer.

Kapp K, Garcia-Marques F, Totten S, Bermudez A, Tanimoto C, Brooks J Glycobiology. 2025; 35(4).

PMID: 40036572 PMC: 11899575. DOI: 10.1093/glycob/cwaf010.


Glycosylation profiling of triple-negative breast cancer: clinical and immune correlations and identification of LMAN1L as a biomarker and therapeutic target.

Yu Q, Zhong H, Zhu X, Liu C, Zhang X, Wang J Front Immunol. 2025; 15:1521930.

PMID: 39867909 PMC: 11759290. DOI: 10.3389/fimmu.2024.1521930.


In-situ profiling of glycosylation on single cells with surface plasmon resonance imaging.

Liu X, Ma J, Zhang Y, Xu Y, Wang Y, Yang D Nat Commun. 2025; 16(1):1000.

PMID: 39856037 PMC: 11759948. DOI: 10.1038/s41467-025-56390-z.


Thyroid Carcinoma Glycoproteins Express Altered -Glycans with 3-O-Sulfated Galactose Residues.

Broekhuis J, Lu D, Aryal R, Matsumoto Y, Pepi L, Chaves N Biomolecules. 2025; 14(12.

PMID: 39766189 PMC: 11727208. DOI: 10.3390/biom14121482.


STT3-mediated aberrant N-glycosylation of CD24 inhibits paclitaxel sensitivity in triple-negative breast cancer.

Wang J, Zhang H, Zhu G, Zhao L, Shi J, Dai Z Acta Pharmacol Sin. 2024; .

PMID: 39668180 DOI: 10.1038/s41401-024-01419-0.