Endoplasmic Reticulum Stress Decreases Intracellular Thyroid Hormone Activation via an eIF2a-Mediated Decrease in Type 2 Deiodinase Synthesis

• Published in: Molecular endocrinology (Baltimore, Md.) Vol. 25; no. 12; pp. 2065 - 2075
• Main Authors: Arrojo e Drigo, Rafael, Fonseca, Tatiana L, Castillo, Melany, Salathe, Matthias, Simovic, Gordana, Mohácsik, Petra, Gereben, Balazs, Bianco, Antonio C
• Format: Journal Article
• Language: English
• Published: United States Endocrine Society 01.12.2011; Oxford University Press
• Subjects: Animals; Cell Line; Cystic Fibrosis - enzymology; Down-Regulation; Endoplasmic Reticulum Stress; Epithelial Cells - metabolism; Eukaryotic Initiation Factor-2 - metabolism; Gene Expression; Humans; Iodide Peroxidase - genetics; Iodide Peroxidase - metabolism; Iodothyronine Deiodinase Type II; Mice; Original Research; Proteasome Endopeptidase Complex - metabolism; Protein Stability; Proteolysis; Respiratory Mucosa - metabolism; Respiratory Mucosa - pathology; Signal Transduction; Thapsigargin; Thyroxine - metabolism; Transcription Factor CHOP - metabolism; Triiodothyronine - biosynthesis; Tunicamycin; Thyroid hormone

Cells respond rapidly to endoplasmic reticulum (ER) stress by blocking protein translation, increasing protein folding capacity, and accelerating degradation of unfolded proteins via ubiquitination and ER-associated degradation pathways. The ER resident type 2 deiodinase (D2) is normally ubiquitinat...