O-GlcNAcylation enhances anaplastic thyroid carcinoma malignancy

O-linked N-acetylglucosamine (O-GlcNAc) glycosylation (O-GlcNAcylation), a dynamic post-translational modification of nuclear and cytoplasmic proteins, may have a critical role in the regulation of biological cell processes and human cancer. O-GlcNAcylation is dynamically regulated by O-GlcNAc trans...

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Bibliographic Details
Published in:Oncology letters 2016-07, Vol.12 (1), p.572-578
Main Authors: CHENG, YU, LI, HONGLUN, LI, JIANLIN, LI, JISHENG, GAO, YAN, LIU, BAODONG
Format: Article
Language:English
Subjects:
Apoptosis
Breast cancer
Cancer therapies
Care and treatment
Cell culture
Cell cycle
Development and progression
Genetic aspects
Glucosamine
Glycosylation
Health aspects
invasion
Lymphatic system
Metabolism
Metastasis
migration
Motility
O-linked N-acetylglucosamine glycosylation
O-linked N-acetylglucosamine transferase
Oncology
Plasmids
Post-translational modification
proliferation
Protein expression
Proteins
Rodents
Signal transduction
Studies
Thyroid cancer
thyroid carcinoma
Tumors
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Summary:O-linked N-acetylglucosamine (O-GlcNAc) glycosylation (O-GlcNAcylation), a dynamic post-translational modification of nuclear and cytoplasmic proteins, may have a critical role in the regulation of biological cell processes and human cancer. O-GlcNAcylation is dynamically regulated by O-GlcNAc transferase (OGT) and O-GlcNAc hydrolase (OGA). Accumulating evidence suggests that O-GlcNAcylation is involved in a variety of types of human cancer. However, the exact role of O-GlcNAcylation in tumor pathogenesis or progression remains to be established. Computed tomography scans of patients with anaplastic thyroid carcinoma (ATC) reveal a rapid growth rate and invasion. The present study demonstrated that O-GlcNAcylation accelerates the progression of ATC. The global O-GlcNAc level of intracellular proteins was increased by overexpression of OGT or downregulation of OGA activity with the specific inhibitor Thiamet-G. By contrast, the global O-GlcNAc level was decreased by silencing of OGT. MTT assay indicated that O-GlcNAcylation significantly promotes cell proliferation. Furthermore, O-GlcNAcylation enhanced cellular biological functions, such as colony formation ability, migration and invasion, of ATC cells in vitro. The findings of the present study suggest that O-GlcNAcylation is associated with malignant properties of thyroid cancer, and may be a potential target for the diagnosis and treatment of thyroid cancer.
ISSN:1792-1074
1792-1082
DOI:10.3892/ol.2016.4647