Thyroid hormone and the mitochondrial population in the rat heart

1988 ◽  
Vol 11 (8) ◽  
pp. 559-565 ◽  
Author(s):  
P. Martino de Rosaroll ◽  
V. Di Maio ◽  
M. Valente ◽  
S. Di Meo ◽  
T. De Leo
Keyword(s):  
Thyroid Hormone ◽  
Rat Heart ◽  
Mitochondrial Population

scholarly journals Influence of thyroid hormone on the in vitro translational activity of specific mRNAs in the rat heart.

1983 ◽  
Vol 258 (12) ◽  
pp. 7738-7745 ◽  
Author(s):  
W H Dillmann ◽  
A Barrieux ◽  
W E Neeley ◽  
P Contreras
Keyword(s):  
Thyroid Hormone ◽  
Rat Heart ◽  
Translational Activity ◽  
Specific Mrnas

scholarly journals Thyroid hormone increases beta‐catenin levels through PI3K in rat heart in vivo and in vitro

2008 ◽  
Vol 22 (S1) ◽  
Author(s):  
Marcela Sorelli Carneiro‐Ramos ◽  
Gabriela Placoná Diniz ◽  
Maria Luiza Morais Barreto‐Chaves ◽  
Anselmo Sigari Moriscot
Keyword(s):  
Thyroid Hormone ◽  
Rat Heart ◽  
Beta Catenin

scholarly journals Selective labelling and inactivation of creatine kinase isoenzymes by the thyroid hormone derivative N-bromoacetyl-3,3′,5-tri-iodo-l-thyronine

1993 ◽  
Vol 291 (2) ◽  
pp. 463-472 ◽  
Author(s):  
M Wyss ◽  
T Wallimann ◽  
J Köhrle
Keyword(s):  
Creatine Kinase ◽  
Thyroid Hormone ◽  
Thyroid Hormones ◽  
Rat Heart ◽  
Covalent Modification ◽  
Regulation Of Transcription ◽  
Selective Labelling ◽  
Mitochondrial Fractions

Besides their well-known regulation of transcription by binding to nuclear receptors, thyroid hormones have been suggested to have direct effects on mitochondria. In a previous study, incubation of rat heart mitochondria with 125I-labelled N-bromoacetyl-3,3′,5-tri-iodo-L-thyronine (BrAcT3), a thyroid hormone derivative with an alkylating side chain, resulted in the selective labelling of a protein doublet around M(r) 45,000 on SDS/polyacrylamide gels [Rasmussen, Köhrle, Rokos and Hesch (1989) FEBS Lett. 255, 385-390]. Now, this protein doublet has been identified as mitochondrial creatine kinase (Mi-CK). Immunoblotting experiments with the cytoplasmic and mitochondrial fractions of rat heart, brain and liver, as well as inactivation studies with the purified chicken CK isoenzymes have further demonstrated that all four CK isoenzymes (Mia-, Mib-, M- and B-CK) are indeed selectively labelled by BrAcT3. However, in contrast with their bromoalkyl derivatives, thyroid hormones themselves did not compete for CK labelling, suggesting that not the thyroid hormone moiety but rather the bromoacetyl-driven alkylation of the highly reactive ‘essential’ thiol group of CK accounts for this selective labelling. Therefore the assumption that CK isoenzymes are thyroid-hormone-binding proteins has to be dismissed. Instead, bromoacetyl-based reagents may allow a very specific covalent modification and inactivation of CK isoenzymes in vitro and in vivo.

scholarly journals Thyroid Hormone Regulates Hyperpolarization-Activated Cyclic Nucleotide-Gated Channel (HCN2) mRNA in the Rat Heart

1999 ◽  
Vol 85 (6) ◽  
pp. 498-503 ◽  
Author(s):  
Janusz Pachucki ◽  
Lynn A. Burmeister ◽  
P. Reed Larsen
Keyword(s):  
Thyroid Hormone ◽  
Cyclic Nucleotide ◽  
Rat Heart ◽  
Gated Channel

Amiodarone and thyroid hormone metabolism in the rat heart

1992 ◽  
Vol 126 (5) ◽  
pp. 475
Author(s):  
Liv S Bjørn-Hansen Gøtzsche ◽  
Niels Boye
Keyword(s):  
Thyroid Hormone ◽  
Rat Heart ◽  
Hormone Metabolism ◽  
Thyroid Hormone Metabolism
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