Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2004-4-5
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Enzyme Inhibitors, http://linkedlifedata.com/resource/pubmed/chemical/Glucose, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Hydrogen Peroxide, http://linkedlifedata.com/resource/pubmed/chemical/Luciferases, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Oxidants, http://linkedlifedata.com/resource/pubmed/chemical/Proteins, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Selenoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Thapsigargin, http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin, http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
9
pubmed:volume
563
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
185-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed-meshheading:15063746-Amino Acid Sequence, pubmed-meshheading:15063746-Carcinoma, Hepatocellular, pubmed-meshheading:15063746-Cell Line, Tumor, pubmed-meshheading:15063746-Cell Survival, pubmed-meshheading:15063746-Endoplasmic Reticulum, pubmed-meshheading:15063746-Enzyme Inhibitors, pubmed-meshheading:15063746-Gene Expression Regulation, Neoplastic, pubmed-meshheading:15063746-Genes, Reporter, pubmed-meshheading:15063746-Glucose, pubmed-meshheading:15063746-HSP70 Heat-Shock Proteins, pubmed-meshheading:15063746-Humans, pubmed-meshheading:15063746-Hydrogen Peroxide, pubmed-meshheading:15063746-Luciferases, pubmed-meshheading:15063746-Membrane Proteins, pubmed-meshheading:15063746-Molecular Sequence Data, pubmed-meshheading:15063746-Mutagenesis, Insertional, pubmed-meshheading:15063746-Oxidants, pubmed-meshheading:15063746-Promoter Regions, Genetic, pubmed-meshheading:15063746-Proteins, pubmed-meshheading:15063746-RNA, Messenger, pubmed-meshheading:15063746-Selenoproteins, pubmed-meshheading:15063746-Sequence Homology, Amino Acid, pubmed-meshheading:15063746-Stress, Physiological, pubmed-meshheading:15063746-Thapsigargin, pubmed-meshheading:15063746-Time Factors, pubmed-meshheading:15063746-Tunicamycin
pubmed:year
2004
pubmed:articleTitle
Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress - SelS is a novel glucose-regulated protein.
pubmed:affiliation
Metabolic Research Unit, School of Health Sciences, Deakin University, Pigdons Road, Waurn Ponds, Vic. 3217, Australia. gao@deakin.edu.au
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't