Thyroid Hormone Receptors Bind to an Element in the Connexin43 Promoter
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Anke Stock
Abstract
Thyroid hormones stimulate gap junctional communication in rat liver WB-F344 epithelial cells, elevating connexin43 mRNA and protein levels. In the present work we analysed connexin43 expression in liver and heart samples from thyroid hormone-treated Wistar rats. Connexin43 mRNA was elevated 2.1-fold in rat liver samples as compared to controls, while there was no change in heart. Thyroid hormone response elements in the rat connexin43 promoter region were examined; a candidate sequence, including a binding site for ligand-dependent transcription factors, was identified at position −480 to −464. This putative regulatory element, rCx−480, contains a direct repeat structure separated by three base pairs (DR3-type element). In electrophoretic mobility shift assays using in vitro translated proteins, the rCx−480 element formed stronger complexes with thyroid hormone receptor α/retinoid X receptor α heterodimers than with vitamin D receptor/retinoid X receptor α heterodimers. In transfected Cos-7 cells, promoter activation was observed via this element after treatment with 3,3′,5-triiodo-L-thyronine. Loss of binding was seen when the 3′ half-site or the spacer region of the rCx−480 element were experimentally mutated, while a stronger binding was observed with mutations introduced in the 5′ halfsite.
Copyright © 2000 by Walter de Gruyter GmbH & Co. KG
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- The Ubiquitin System and the N-End Rule Pathway
- Paper of the Year 1999: Award to Igor Stagljar
- A Clockwork Organ
- The Transgeneticists Toolbox: Novel Methods for the Targeted Modification of Eukaryotic Genomes
- Interdependence of Filamentous Actin and Microtubules for Asymmetric Cell Division
- Genetic Analysis of Mammalian Cyclin-Dependent Kinases and Their Inhibitors
- Phosphorylcholine Substituents in Nematodes: Structures, Occurrence and Biological Implications
- Selenium in Biology: Facts and Medical Perspectives
- The Role of Se, Mo and Fe in the Structure and Function of Carbon Monoxide Dehydrogenase
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