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Science 22 September 1978:
Vol. 201. no. 4361, pp. 1126 - 1129
DOI: 10.1126/science.210507
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Articles

Science, Vol 201, Issue 4361, 1126-1129
Copyright © 1978 by American Association for the Advancement of Science

articles

Mitochondrial thyroid hormone receptor: localization and physiological significance

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

Binding studies of thyroid hormone to submitochondrial fractions from rat liver suggest that the component responsible for high-affinity, low-capacity (saturable) binding of hormones arises from the inner mitochondrial membrane. The partially purified component, approximately 150,000 daltons, appears to be half protein and half lipid, largely phospholipids, tentatively identified as lecithin, phosphatidyl ethanolamine, and cardiolipin. A similar hormone-binding macromolecule was found in mitochondria from rabbit kidney, from human liver and kidney, and from rat kidney, myocardium, skeletal muscle, intestinal mucosa, whole small intestine, adipose tissue, and lung. It was absent from mitochondria of adult rat brain, spleen, and testis, organs calorigenically unresponsive to thyroid hormones injected in vivo, but was present in mitochondria from brains of rats 12 days old and younger. The organ distribution of the hormone-binding protein and its presence in neonatal brain mitochondria supports the biological relevance of the mitochondrial component as a thyroid hormone receptor.


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A 43-kDa Protein Related to c-Erb A [IMAGE]1 Is Located in the Mitochondrial Matrix of Rat Liver.
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Rapid effect of triiodothyronine on the mitochondrial pathway in rat liver in vivo.
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