O-GlcNAcylation is increased in prostate cancer tissues and enhances malignancy of prostate cancer cells

• Published in: Molecular medicine reports Vol. 10; no. 2; pp. 897 - 904
• Main Authors: GU, YUCHAO, GAO, JIANGANG, HAN, CUIFANG, ZHANG, XINLING, LIU, HAIYAN, MA, LEINA, SUN, XIAOQING, YU, WENGONG
• Format: Journal Article
• Language: English
• Published: Greece D.A. Spandidos 01.08.2014; Spandidos Publications; Spandidos Publications UK Ltd
• Subjects: Acetylglucosamine - metabolism; Benign; Cadherins; Cadherins - metabolism; Catenins - metabolism; Cell adhesion & migration; Cell growth; Cell Line, Tumor; Cell Movement; Cytoskeleton; Cytoskeleton - metabolism; Development and progression; E-cadherin; Epithelial cells; Genetic aspects; Humans; Hyperplasia; Immunohistochemistry; Invasiveness; Liver; Liver cancer; Liver Neoplasms - metabolism; Liver Neoplasms - pathology; Male; Malignancy; Membranes; Metabolism; N-Acetylglucosamine; N-Acetylglucosaminyltransferases - genetics; N-Acetylglucosaminyltransferases - metabolism; O-GlcNAc; O-GlcNAcylation; Pancreatic cancer; Pancreatic Neoplasms - metabolism; Pancreatic Neoplasms - pathology; Physiological aspects; Promoter Regions, Genetic; Prostate cancer; Prostatic Neoplasms - metabolism; Prostatic Neoplasms - pathology; Proteins; Serine; Threonine; β-Catenin; China; United States > US
• ISSN: 1791-2997; 1791-3004
• DOI: 10.3892/mmr.2014.2269

O-GlcNAc is an O-linked β-N-acetylglucosamine moiety attached to the side-chain hydroxyl of a serine or threonine residue in numerous cytoplasmic and nuclear proteins. In this study, we detected the level of O-GlcNAc in prostate, liver and pancreatic cancer tissues, and found that the global O-GlcNAc modification also known as O-GlcNAcylation, is specifically increased in prostate cancer tissues compared to corresponding adjacent tissues. In addition, we found that global O-GlcNAcylation is increased in prostate cancer cells and not in benign prostatic hyperplasia (BPH) epithelial cells. O-GlcNAc enhanced the anchorage-independent growth and the migratory/invasive ability of prostate cancer cells. More importantly, we provide here, for the first time to the best of our knowledge, direct evidence that increased O-GlcNAcylation induces malignant transformation of nontumorigenic (BPH) cells. Furthermore, our study suggested that inhibiting the formation of the E-cadherin/catenin/cytoskeleton complex may underly the O-GlcNAc-induced prostate cancer progression. Overall, these findings indicated that O-GlcNAcylation is increased in prostate, but not in liver and pancreatic cancer tissues, and that O-GlcNAc can enhance the malignancy of prostate cancer cells.