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Full-Text Articles in Medicine and Health Sciences
The Type 2 Iodothyronine Deiodinase Is Essential For Adaptive Thermogenesis In Brown Adipose Tissue, Lucia A. De Jesus, Suzy D. Carvalho, Mirian O. Ribeiro, Mark Schneider, Sung-Woo Kim, John W. Harney, P. Reed Larsen, Antonio C. Bianco
The Type 2 Iodothyronine Deiodinase Is Essential For Adaptive Thermogenesis In Brown Adipose Tissue, Lucia A. De Jesus, Suzy D. Carvalho, Mirian O. Ribeiro, Mark Schneider, Sung-Woo Kim, John W. Harney, P. Reed Larsen, Antonio C. Bianco
Dartmouth Scholarship
Type 2 iodothyronine deiodinase (D2) is a selenoenzyme, the product of the recently cloned cAMP-dependent Dio2 gene, which increases 10- to 50-fold during cold stress only in brown adipose tissue (BAT). Here we report that despite a normal plasma 3,5,3′-triiodothyronine (T3) concentration, cold-exposed mice with targeted disruption of the Dio2 gene (Dio2–/–) become hypothermic due to impaired BAT thermogenesis and survive by compensatory shivering with consequent acute weight loss. This occurs despite normal basal mitochondrial uncoupling protein 1 (UCP1) concentration. In Dio2–/– brown adipocytes, the acute norepinephrine-, CL316,243-, or forskolin-induced increases in lipolysis, UCP1 mRNA, and …
Distinct Retrieval And Retention Mechanisms Are Required For The Quality Control Of Endoplasmic Reticulum Protein Folding, Shilpa Vashist, Woong Kim, William J. Belden, Eric D. Spear, Charles Barlowe, Davis T.W. Ng
Distinct Retrieval And Retention Mechanisms Are Required For The Quality Control Of Endoplasmic Reticulum Protein Folding, Shilpa Vashist, Woong Kim, William J. Belden, Eric D. Spear, Charles Barlowe, Davis T.W. Ng
Dartmouth Scholarship
Proteins destined for the secretory pathway must first fold and assemble in the lumen of endoplasmic reticulum (ER). The pathway maintains a quality control mechanism to assure that aberrantly processed proteins are not delivered to their sites of function. As part of this mechanism, misfolded proteins are returned to the cytosol via the ER protein translocation pore where they are ubiquitinated and degraded by the 26S proteasome. Previously, little was known regarding the recognition and targeting of proteins before degradation. By tracking the fate of several mutant proteins subject to quality control, we demonstrate the existence of two distinct sorting …