Abstract
O-GlcNAcylation is an O-linked β-N-acetylglucosamine (O-GlcNAc) moiety linked to the serine or threonine residues in proteins. O-GlcNAcylation is a dynamic post-translational modification involved in a wide range of biological processes and diseases such as cancer. This modification can increase and decrease the activity of enzymes as well as interfere with protein stability and interaction. The modulatory capacity of O-GlcNAcylation, as well as protein phosphorylation, is of paramount importance in the regulation of metabolism and intracellular signaling of tumor cells. Thus, understanding the regulation of O-GlcNAcylation in tumor cells and their difference compared to non-tumor cells may elucidate new mechanisms related to tumor generation and development, could provide a new marker to diagnosis and prognosis in patients with cancer and indicate a new target to cancer chemotherapy.
Highlights
O-linked β-N -acetylglucosamine (O-GlcNAc) was discovered 30 years ago [1]
O-GlcNAc transferase (OGT) in non-transformed HPDE prostate cells did not affect their proliferation [35]. These results indicate that O-GlcNAcylation is important for tumor cell growth and cancer cells appear to be susceptible to loss of OGT, suggesting that this enzyme may be a potential future therapeutic target in chemotherapy
DIRECTIONS Taken together, O-GlcNAc appears to be important in tumor biology, and altered O-GlcNAcylation is an event found in many types of cancer
Summary
O-linked β-N -acetylglucosamine (O-GlcNAc) was discovered 30 years ago [1]. Unlike “traditional glycosylation,” O-GlcNAc is not elongated into more complex structures and is localized mainly in nucleocytoplasmic compartments. PROSTATE CANCER Lynch and colleagues [26] showed that O-GlcNAc and OGT levels are higher and OGA/OGT ratios are lower in tumor cells than in normal cells lines.
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