scholarly journals Erratum: Vitamin A Affects Flatfish Development in a Thyroid Hormone Signaling and Metamorphic Stage Dependent Manner

2017 ◽  
Vol 8 ◽  
Author(s):  
Keyword(s):  
Thyroid Hormone ◽  
Vitamin A ◽  
Dependent Manner ◽  
Hormone Signaling ◽  
Metamorphic Stage

scholarly journals Vitamin A Affects Flatfish Development in a Thyroid Hormone Signaling and Metamorphic Stage Dependent Manner

2017 ◽  
Vol 8 ◽  
Author(s):  
Ignacio Fernández ◽  
Juan B. Ortiz-Delgado ◽  
Maria J. Darias ◽  
Francisco Hontoria ◽  
Karl B. Andree ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Vitamin A ◽  
Dependent Manner ◽  
Hormone Signaling ◽  
Metamorphic Stage

Effects on thyroid hormone metabolism and depletion of lung vitamin a in rats by airborne particulate matter

1993 ◽  
Vol 38 (4) ◽  
pp. 419-434 ◽  
Author(s):  
G. A. H. Heussen ◽  
G. J. Schefferlie ◽  
M. J. G. Talsma ◽  
H. van Til ◽  
M. J. W. Dohmen ◽  
...  
Keyword(s):  
Particulate Matter ◽  
Thyroid Hormone ◽  
Vitamin A ◽  
Airborne Particulate Matter ◽  
Airborne Particulate ◽  
Hormone Metabolism ◽  
Thyroid Hormone Metabolism

scholarly journals Thyroid Hormone Signaling in the Mouse Retina

PLoS ONE ◽  
2016 ◽  
Vol 11 (12) ◽  
pp. e0168003 ◽  
Author(s):  
Patrick Arbogast ◽  
Frédéric Flamant ◽  
Pierre Godement ◽  
Martin Glösmann ◽  
Leo Peichl
Keyword(s):  
Thyroid Hormone ◽  
Mouse Retina ◽  
Hormone Signaling

A conserved C-terminal sequence that is deleted in v-ErbA is essential for the biological activities of c-ErbA (the thyroid hormone receptor)

1993 ◽  
Vol 13 (6) ◽  
pp. 3675-3685
Author(s):  
F Saatcioglu ◽  
P Bartunek ◽  
T Deng ◽  
M Zenke ◽  
M Karin
Keyword(s):  
Amino Acid ◽  
Thyroid Hormone ◽  
Transcriptional Activation ◽  
Thyroid Hormone Receptor ◽  
Retinoic Acid Receptor ◽  
Biological Activities ◽  
Erythroid Differentiation ◽  
Dependent Manner ◽  
Transcriptional Interference ◽  
Terminal Sequence

The thyroid hormone (T3) receptor type alpha, the c-ErbA alpha proto-oncoprotein, stimulates transcription of T3-dependent promoters, interferes with AP-1 activity, and induces erythroid differentiation in a ligand-dependent manner. The v-ErbA oncoprotein does not bind hormone and has lost all of these activities. Using c-ErbA/v-ErbA chimeras, we found that a deletion of 9 amino acids, conserved among many members of the nuclear receptor superfamily, which are located at the extreme carboxy terminus of c-ErbA alpha is responsible for loss of both transactivation and transcriptional interference activities. Single, double, and triple amino acid substitutions within this region completely abolished T3-dependent transcriptional activation, interference with AP-1 activity, and decreased T3 binding by c-ErbA alpha. However, the lower T3 binding by these mutants does not fully account for the loss of transactivation and transcriptional interference, since a c-ErbA/v-ErbA chimera which was similarly reduced in T3 binding activity has retained both of these functions. Deletion of homologous residues in the retinoic acid receptor alpha (RAR alpha) resulted in a similar loss of transactivation and transcriptional interference activities. The ability of c-ErbA alpha to induce differentiation of transformed erythroblasts is also impaired by all of the mutations introduced into the conserved carboxy-terminal sequence. We conclude that this 9-amino-acid conserved region is essential for normal biological function of c-ErbA alpha and RAR alpha and possibly other T3 and RA receptors.

Protective role of vitamins A, C, and E against the genotoxic damage induced by aflatoxin B1 in cultured human lymphocytes

2009 ◽  
Vol 25 (3) ◽  
pp. 183-188 ◽  
Author(s):  
L Alpsoy ◽  
G Agar ◽  
M Ikbal
Keyword(s):  
Vitamin A ◽  
Vitamin C ◽  
Human Lymphocytes ◽  
Mutagenic Effect ◽  
Treated Group ◽  
Protective Role ◽  
Effective Concentration ◽  
Dependent Manner ◽  
Protective Effects ◽  
Aflatoxin B

In this study, we aimed to evaluate the effect of vitamins A, C, and E against aflatoxin B1 (AFB1) on blood cultures in relation to induction of sister chromatid exchange (SCE). The results indicated genotoxic and mutagenic damage in cultured human lymphocytes exposed to AFB1. The results showed that 5 μM concentration of AFB1 increased SCE. When vitamins A, C, and E were added to AFB1, the frequency of SCE decreased. These results suggest that vitamins A, C, and E could effectively inhibit AFB1-induced SCE, which may partially responsible for its mutagenic effect of AFB1. Besides, the protective effect of vitamins A, C, and E against AFB1 was increased in a dose-dependent manner (i.e., as the doses increased, their protective effects also increased). There was a significant decrease in the SCE frequency in AFB1-treated group compared with the groups receiving AFB1 and also vitamins A, C, and E. The most effective concentration was 100 microM vitamin C, and the lowest effective concentration was 0.5 microM vitamin A. Vitamin C has the most effective concentration of 100 μM, and vitamin A has the lowest effective concentration of 0.5 μM. The order of the decreasing effect of the SCE frequency of vitamins was as follows: vitamin C > vitamin E > vitamin A.

scholarly journals microRNA and thyroid hormone signaling in cardiac and skeletal muscle

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Duo Zhang ◽  
Yan Li ◽  
Shengnan Liu ◽  
Yu-cheng Wang ◽  
Feifan Guo ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Thyroid Hormone ◽  
Hormone Signaling
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