title: Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated protein.
abstract: SelS is a newly identified selenoprotein and its gene expression is up-regulated in the liver of Psammomys obesus after fasting. We have examined whether SelS is regulated by glucose deprivation and endoplasmic reticulum (ER) stress in HepG2 cells. Glucose deprivation and the ER stress inducers tunicamycin and thapsigargin increased SelS gene expression and protein content several-fold in parallel with glucose-regulated protein 78. The overexpression of SelS increased Min6 cell resistance to oxidative stress-induced toxicity. These results indicate that SelS is a novel member of the glucose-regulated protein family and its function is related to the regulation of cellular redox balance.
authors.affiliation: Metabolic Research Unit, School of Health Sciences, Deakin University, Pigdons Road, Waurn Ponds, Vic. 3217, Australia. gao@deakin.edu.au
authors.forename: Yuan
authors.initials: Y
authors.lastname: Gao
authors.forename: Helen C
authors.initials: HC
authors.lastname: Feng
authors.forename: Ken
authors.initials: K
authors.lastname: Walder
authors.forename: Kristy
authors.initials: K
authors.lastname: Bolton
authors.forename: Terry
authors.initials: T
authors.lastname: Sunderland
authors.forename: Natalie
authors.initials: N
authors.lastname: Bishara
authors.forename: Melissa
authors.initials: M
authors.lastname: Quick
authors.forename: Lakshmi
authors.initials: L
authors.lastname: Kantham
authors.forename: Greg R
authors.initials: GR
authors.lastname: Collier
mesh_terms: D000595:Amino Acid Sequence; D006528:Carcinoma, Hepatocellular / Q000235:genetics / Q000473:pathology; D045744:Cell Line, Tumor; D002470:Cell Survival; D004721:Endoplasmic Reticulum / Q000187:drug effects / Q000502:physiology*; D004791:Enzyme Inhibitors / Q000494:pharmacology; D015972:Gene Expression Regulation, Neoplastic; D017930:Genes, Reporter; D005947:Glucose / Q000378:metabolism*; D018840:HSP70 Heat-Shock Proteins; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology; D008156:Luciferases / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins; D008969:Molecular Sequence Data; D016254:Mutagenesis, Insertional; D016877:Oxidants / Q000494:pharmacology; D011401:Promoter Regions, Genetic; D011506:Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D012333:RNA, Messenger / Q000378:metabolism; D051140:Selenoproteins; D017386:Sequence Homology, Amino Acid; D013312:Stress, Physiological / Q000378:metabolism*; D019284:Thapsigargin / Q000494:pharmacology; D013997:Time Factors; D014415:Tunicamycin / Q000494:pharmacology
chemical_list: D004791:Enzyme Inhibitors; D018840:HSP70 Heat-Shock Proteins; D008565:Membrane Proteins; D016877:Oxidants; D011506:Proteins; D012333:RNA, Messenger; D051140:Selenoproteins; C018551:glucose-regulated proteins; D014415:Tunicamycin; D019284:Thapsigargin; D006861:Hydrogen Peroxide; D008156:Luciferases; D005947:Glucose