Effects of Zinc and Other Divalent Metals on Deoxyribonucleic Acid Binding and Hormone-Binding Activity of Human al Thyroid Hormone Receptor Expressed inEscherichia coli*

Endocrinology ◽  
1991 ◽  
Vol 129 (6) ◽  
pp. 3027-3033 ◽  
Author(s):  
TAKAHIDE MIYAMOTO ◽  
AKIHIRO SAKURAI ◽  
LESLIE J. DEGROOT
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Deoxyribonucleic Acid ◽  
Thyroid Hormone Receptor ◽  
Binding Activity ◽  
Inescherichia Coli ◽  
Hormone Binding ◽  
Divalent Metals

scholarly journals Loss of thyroid hormone receptor activity in primary cultured rat hepatocytes is reversed by 2-mercaptoethanol

1992 ◽  
Vol 281 (3) ◽  
pp. 669-673 ◽  
Author(s):  
N Yamamoto ◽  
A Inoue ◽  
K P Takahashi ◽  
Q Li ◽  
H Nakamura ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Hormone Receptors ◽  
Thyroid Hormone Receptor ◽  
Primary Cultures ◽  
Rat Hepatocytes ◽  
Binding Activity ◽  
Dependent Manner ◽  
Hormone Binding ◽  
Level Of Activity

In primary cultures of rat hepatocytes, specific thyroid-hormone-binding activity diminished with time and was hardly detectable at 24 h. In accordance with the loss of 3,5,3′-tri-iodothyronine (T3) binding, responses to the hormone disappeared, as indicated by low induction of the thyroid-hormone-responsive gene S14. In contrast, thyroid hormone receptor proteins were present, as determined by immunostaining with a specific antibody against the receptor. Thus the loss of T3 binding was due to receptor inactivation. After various attempts to restore the T3-binding activity, we found that 2-mercaptoethanol, a reducing agent, when added to the culture medium restored the hormone binding activity in a dose- and time-dependent manner. The observed kinetics and experiments using cycloheximide suggested that mercaptoethanol prevented inactivation of the newly synthesized receptors. Oxidoreductive conditions within cells may have a role in determining the level of activity of thyroid hormone receptors.

scholarly journals Nuclear factors specifically favor thyroid hormone binding to c-ErbAα1 protein (thyroid hormone receptor α) over-expressed in E. coli

FEBS Letters ◽  
1995 ◽  
Vol 358 (2) ◽  
pp. 137-141 ◽  
Author(s):  
Malika Daadi ◽  
Christelle Lenoir ◽  
Alexandra Dace ◽  
Jeannine Bonne ◽  
Michèle Teboul ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Hormone Binding ◽  
E Coli ◽  
Nuclear Factors ◽  
Thyroid Hormone Receptor Α

Modification of Deoxyribonucleic Acid-Thyroid Hormone Receptor Interaction by Histones*

Endocrinology ◽  
1987 ◽  
Vol 121 (3) ◽  
pp. 893-899 ◽  
Author(s):  
KAZUO ICHIKAWA ◽  
STEVEN BENTLEY ◽  
MARTIN FEE ◽  
LESLIE J. DEGROOT
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Deoxyribonucleic Acid ◽  
Thyroid Hormone Receptor ◽  
Receptor Interaction

Purification of human c-erb A β protein

1991 ◽  
Vol 7 (2) ◽  
pp. 123-129 ◽  
Author(s):  
K. Ichikawa ◽  
K. Hashizume ◽  
Y. Nishii ◽  
T. Takeda ◽  
M. Kobayashi ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Column Chromatography ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Gel Filtration ◽  
Binding Activity ◽  
Human Thyroid ◽  
E Coli ◽  
Ammonium Sulphate Precipitation ◽  
Β Protein

ABSTRACT Human thyroid hormone receptor (c-erb A protein) produced by Escherichia coli expression vector plasmid was purified sequentially using polyethylenimine precipitation of DNA, hydroxylapatite column chromatography, ammonium sulphate precipitation, Sephacryl S-300 gel filtration and mono Q-Sepharose column chromatography. These column procedures resulted in 41.3-fold purification of 3,5,3′-tri-iodo-l-thyronine (T3) binding activity over the initial E. coli extract. Purified protein as well as crude preparation showed high-affinity binding to T3. The c-erb A protein enriched by column purification was further purified by electroelution after electrophoresis. Rabbit antibody against the c-erb A protein was prepared and used for the Western blotting analysis. The antibody recognized c-erb A protein but not the bacterial proteins in crude E. coli extract. When partially purified rat hepatic nuclear thyroid hormone receptor was analysed, a 56kDa receptor was specifically recognized by the antibody.

Fatty acyl-CoA binding activity of the nuclear thyroid hormone receptor

1993 ◽  
Vol 51 (4) ◽  
pp. 458-464 ◽  
Author(s):  
Qiulin Li ◽  
Naoki Yamamoto ◽  
Seiji Morisawa ◽  
Akira Inoue
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Thyroid Hormone Receptor ◽  
Fatty Acyl ◽  
Binding Activity
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