Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 2 September 1977:
Vol. 197. no. 4307, pp. 996 - 999
DOI: 10.1126/science.196334
Prev | Table of Contents | Next

Articles

Science, Vol 197, Issue 4307, 996-999
Copyright © 1977 by American Association for the Advancement of Science

articles

Thyroid hormone action: the mitochondrial pathway

K Sterling, PO Milch, MA Brenner, and JH Lazarus

The subcellular compartments have been investigated to compare proteins capable of binding triiodothyronine and thyroxine; specific binders have been found in cytosol, nuclei, and mitochondria from rat liver and kidney. The binding protein from the inner mitochondrial membrane had the highest association constant (greater than 10(11) liters per mole), suggesting possible direct hormone action on the mitochondria. Binding of hormone analogs was found to be related to known physiological potency, and stereospecific discrimination between L- and D-thyroxine was observed. The saturable receptor was found in the mitochondrial membranes of rat liver, kidney, myocardium, and skeletal muscle but not in mitochondria from the unresponsive tissues: brain, spleen, and testis. Oxidative phosphorylation by mitochondrial vesicles from hypothyroid rats increased after the addition of physiological concentrations of triiodothyronine, which corroborated direct hormone action on mitochondria.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Thyroid hormone (T3) rapidly activates p38 and AMPK in skeletal muscle in vivo.
I. Irrcher, D. R. Walkinshaw, T. E. Sheehan, and D. A. Hood (2008)
J Appl Physiol 104, 178-185
   Abstract »    Full Text »    PDF »
Comparing thyroid and insect hormone signaling.
T. Flatt, L. L. Moroz, M. Tatar, and A. Heyland (2006)
Integr. Comp. Biol. 46, 777-794
   Abstract »    Full Text »    PDF »
A Variant Form of the Nuclear Triiodothyronine Receptor c-ErbAalpha 1 Plays a Direct Role in Regulation of Mitochondrial RNA Synthesis.
F. Casas, P. Rochard, A. Rodier, I. Cassar-Malek, S. Marchal-Victorion, R. J. Wiesner, G. Cabello, and C. Wrutniak (1999)
Mol. Cell. Biol. 19, 7913-7924
   Abstract »    Full Text »    PDF »
Age-Related Changes in the Thyroid Hormone Effects on Malondialdehyde-Modified Proteins in the Rat Heart.
J. Chehade, J. Kim, J. L. Pinnas, and A. D. Mooradian (1999)
Experimental Biology and Medicine 222, 59-64
   Abstract »    Full Text »
A 43-kDa Protein Related to c-Erb A [IMAGE]1 Is Located in the Mitochondrial Matrix of Rat Liver.
C. Wrutniak, I. Cassar-Malek, S. Marchal, A. Rascle, S. Heusser, J.-M. Keller, J. Fléchon, M. Daua, J. Samarut, J. Ghysdael, et al. (1995)
J. Biol. Chem. 270, 16347-16354
   Abstract »    Full Text »    PDF »
The Effects of Xenobiotics on the Structure and Function of Thyroid Follicular and C-Cells.
C. C. Capen and S. L. Martin (1989)
Toxicol Pathol 17, 266-293
   Abstract »    PDF »
Rapid effect of triiodothyronine on the mitochondrial pathway in rat liver in vivo.
K Sterling, M. Brenner, and T Sakurada (1980)
Science 210, 340-342
   Abstract »    PDF »
Mitochondrial thyroid hormone receptor: localization and physiological significance.
K Sterling, J. Lazarus, P. Milch, T Sakurada, and M. Brenner (1978)
Science 201, 1126-1129
   Abstract »    PDF »
Fasting decreases triiodothyronine receptor capacity.
G. Schussler and J Orlando (1978)
Science 199, 686-688
   Abstract »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)