Selenium-dependent regulation of type I 5'-deiodinase expression.
Selenite concentration regulates activity and expression of the p27 substrate-binding subunit of type I 5'deiodinase (5'-D) and of a protein labeled with bromoacetylthyroxin (BrAcT4), or p30, with yet unknown function in a porcine-kidney epithelial cell line (LLC-PK1) cultured in serum-free medium. p27 is metabolically labeled by 75-selenite and affinity labeled by BrAc[125I]T4. Compared with glutathione peroxidase, expression of the p27 5'D subunit (5'-DI) is observed at 10-fold-lower concentrations of selenium in the growth medium, suggesting an intracellular hierarchy of selenite utilization. Selenium deficiency retards cell growth and prevents 5'-DI expression and may thus impair thyroid hormone action in vivo.
Oertel
M
M
Abteilung Klinische Endokrinologie, Medizinische Hochschule Hannover, Germany.
Gross
M
M
Rokos
H
H
Köhrle
J
J
D000345:Affinity Labels; D000818:Animals; D002460:Cell Line; D005979:Glutathione Peroxidase / Q000378:metabolism; D007453:Iodide Peroxidase / Q000378:metabolism*; D007668:Kidney; D012643:Selenium / Q000494:pharmacology*; D012644:Selenium Radioisotopes; D013552:Swine; D013974:Thyroxine / Q000031:analogs & derivatives / Q000378:metabolism
D000345:Affinity Labels; D012644:Selenium Radioisotopes; C015042:N-bromoacetylthyroxine; D007453:Iodide Peroxidase; D005979:Glutathione Peroxidase; D012643:Selenium; D013974:Thyroxine