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Regulation of the selenoprotein SelS by glucose deprivation and endoplasmic reticulum stress – SelS is a novel glucose‐regulated protein
Author(s) -
Gao Yuan,
Feng Helen C,
Walder Ken,
Bolton Kristy,
Sunderland Terry,
Bishara Natalie,
Quick Melissa,
Kantham Lakshmi,
Collier Greg R
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(04)00296-0
Subject(s) - glucose regulated protein , endoplasmic reticulum , unfolded protein response , tunicamycin , endocrinology , medicine , chemistry , thapsigargin , downregulation and upregulation , oxidative stress , biology , microbiology and biotechnology , biochemistry , gene
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.