title: A correlation between altered O-GlcNAcylation, migration and with changes in E-cadherin levels in ovarian cancer cells.
abstract: O-GlcNAcylation is a dynamic and reversible posttranslational modification of nuclear and cytoplasmic proteins. In recent years, the roles of O-GlcNAcylation in several human malignant tumors have been investigated, and O-GlcNAcylation was found to be linked to cellular features relevant to metastasis. In this study, we modeled four diverse ovarian cancer cells and investigated the effects of O-GlcNAcylation on ovarian cancer cell migration. We found that total O-GlcNAcylation level was elevated in HO-8910PM cells compared to OVCAR3 cells. Additionally, through altering the total O-GlcNAcylation level by OGT silencing or OGA inhibition, we found that the migration of OVCAR3 cells was dramatically enhanced by PUGNAc and Thiamet G treatment, and the migration ability of HO-8910PM cells was significantly inhibited by OGT silencing. Furthermore, we also found that the expression of E-cadherin, an O-GlcNAcylated protein in ovarian cancer cells, was reduced by OGA inhibition in OVCAR3 cells and elevated by OGT silencing in HO-8910PM cells. These results indicate that O-GlcNAcylation could enhance ovarian cancer cell migration and decrease the expression of E-cadherin. Our studies also suggest that O-GlcNAcylation might become another potential target for the therapy of ovarian cancer.
authors.affiliation: Department of Obstetrics and Gynecology, The Second Affiliated Hospital of Chongqing Medical University, 76 Lin Jiang Road, Chongqing 400010, PR China.
authors.forename: Feng-zhen
authors.initials: FZ
authors.lastname: Jin
authors.forename: Chao
authors.initials: C
authors.lastname: Yu
authors.forename: De-zhang
authors.initials: DZ
authors.lastname: Zhao
authors.forename: Ming-jun
authors.initials: MJ
authors.lastname: Wu
authors.forename: Zhu
authors.initials: Z
authors.lastname: Yang
mesh_terms: D000117:Acetylglucosamine / Q000031:analogs & derivatives / Q000378:metabolism* / Q000494:pharmacology; D015703:Antigens, CD; D015153:Blotting, Western; D015820:Cadherins / Q000235:genetics / Q000378:metabolism*; D051177:Catenins / Q000235:genetics / Q000378:metabolism; D002448:Cell Adhesion; D045744:Cell Line, Tumor; D002465:Cell Movement / Q000187:drug effects*; D005260:Female; D020868:Gene Silencing; D006031:Glycosylation; D006801:Humans; D046912:Multiprotein Complexes / Q000235:genetics / Q000378:metabolism; D017351:N-Acetylglucosaminyltransferases / Q000378:metabolism*; D010051:Ovarian Neoplasms / Q000378:metabolism / Q000473:pathology*; D010091:Oximes / Q000494:pharmacology; D048448:Phenylcarbamates / Q000494:pharmacology; D011714:Pyrans / Q000494:pharmacology; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D034741:RNA, Small Interfering / Q000235:genetics / Q000378:metabolism; D013844:Thiazoles / Q000494:pharmacology; D014162:Transfection; D051176:beta Catenin / Q000235:genetics / Q000378:metabolism; D000095002:Delta Catenin
chemical_list: D015703:Antigens, CD; C513384:CDH1 protein, human; D015820:Cadherins; D051177:Catenins; D046912:Multiprotein Complexes; D010091:Oximes; D048448:Phenylcarbamates; D011714:Pyrans; D012333:RNA, Messenger; D034741:RNA, Small Interfering; D013844:Thiazoles; D051176:beta Catenin; C572247:thiamet G; C068836:N-acetylglucosaminono-1,5-lactone O-(phenylcarbamoyl)oxime; D017351:N-Acetylglucosaminyltransferases; C449880:O-GlcNAc transferase; D000117:Acetylglucosamine; D000095002:Delta Catenin