title: Resistance against apoptosis by the cellular prion protein is dependent on its glycosylation status in oral HSC-2 and colon LS 174T cancer cells.
abstract: Most studies have focused on the role of the cellular prion protein (PrP(C)) in neurodegenerative diseases, whereas the function of this ubiquitous protein outside the nervous system remains elusive. Therefore, the anti-apoptotic property of PrP(C) in oral squamous cell carcinoma (HSC-2) and colon adenocarcinoma (LS 174T) was evaluated in this study, by stable shRNA knockdown and overexpression, respectively. PrP(C) confers resistance against oxidative stress-apoptosis as indicated by MTT assay, Annexin V-FITC/PI and DCFH-DA staining, but this property is abolished upon N-glycosylation inhibition by tunicamycin. Our results indicate that the inhibition of glycosylation in cancer cells overexpressing PrP(C) could represent a potential therapeutic target.
authors: Department of Biomedical Science, Faculty of Science, Universiti Tunku Abdul Rahman, Perak Campus, Kampar, Perak, Malaysia.
authors: Yeannie Hui-Yeng
authors: YH
authors: Yap
authors: Yee-How
authors: YH
authors: Say
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology; D000975:Antioxidants / Q000378:metabolism; D017209:Apoptosis; D045744:Cell Line, Tumor; D002470:Cell Survival; D003110:Colonic Neoplasms / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006031:Glycosylation; D006367:HeLa Cells; D006801:Humans; D008928:Mitochondria / Q000378:metabolism; D009062:Mouth Neoplasms / Q000378:metabolism*; D018384:Oxidative Stress; D011328:Prions / Q000737:chemistry*; D017382:Reactive Oxygen Species; D013778:Tetrazolium Salts / Q000494:pharmacology; D013844:Thiazoles / Q000494:pharmacology; D013997:Time Factors; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D000900:Anti-Bacterial Agents; D000975:Antioxidants; D011328:Prions; D017382:Reactive Oxygen Species; D013778:Tetrazolium Salts; D013844:Thiazoles; D014415:Tunicamycin; C022616:thiazolyl blue