scholarly journals Synthetic and Plant Derived Thyroid Hormone Analogs

10.5772/35134 ◽  
2012 ◽  
Author(s):  
Suzana T. Cunha Lima ◽  
Travis L. ◽  
Edson D.
Keyword(s):  
Thyroid Hormone ◽  
Hormone Analogs

scholarly journals Bioactivity of Thyroid Hormone Analogs at Cancer Cells

2018 ◽  
Vol 9 ◽  
Author(s):  
Paul J. Davis ◽  
Heng-Yuan Tang ◽  
Aleck Hercbergs ◽  
Hung-Yun Lin ◽  
Kelly A. Keating ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Cancer Cells ◽  
Hormone Analogs

scholarly journals In Vivo Activity of the Thyroid Hormone Receptor β- and α-Selective Agonists GC-24 and CO23 on Rat Liver, Heart, and Brain

Endocrinology ◽  
2011 ◽  
Vol 152 (3) ◽  
pp. 1136-1142 ◽  
Author(s):  
Carmen Grijota-Martínez ◽  
Eric Samarut ◽  
Thomas S. Scanlan ◽  
Beatriz Morte ◽  
Juan Bernal
Keyword(s):  
Thyroid Hormone ◽  
Hormone Receptor ◽  
Target Genes ◽  
Thyroid Hormone Receptor ◽  
Receptor Subtype ◽  
Receptor Subtypes ◽  
Genetic Modifications ◽  
Hormone Analogs ◽  
Thyroid Hormone Receptor Β

Thyroid hormone analogs with selective actions through specific thyroid hormone receptor (TR) subtypes are of great interest. They might offer the possibility of mimicking physiological actions of thyroid hormone with receptor subtype or tissue specificity with therapeutic aims. They are also pharmacological tools to dissect biochemical pathways mediated by specific receptor subtypes, in a complementary way to mouse genetic modifications. In this work, we studied the in vivo activity in developing rats of two thyroid hormone agonists, the TRβ-selective GC-24 and the TRα-selective CO23. Our principal goal was to check whether these compounds were active in the rat brain. Analog activity was assessed by measuring the expression of thyroid hormone target genes in liver, heart, and brain, after administration to hypothyroid rats. GC-24 was very selective for TRβ and lacked activity on the brain. On the other hand, CO23 was active in liver, heart, and brain on genes regulated by either TRα or TRβ. This compound, previously shown to be TRα-selective in tadpoles, displayed no selectivity in the rat in vivo.

Thyroid Hormone, Hormone Analogs, and Angiogenesis

2015 ◽  
pp. 353-362 ◽  
Author(s):  
Paul J. Davis ◽  
Thangirala Sudha ◽  
Hung-Yun Lin ◽  
Shaker A. Mousa
Keyword(s):  
Thyroid Hormone ◽  
Hormone Analogs

Molecular orbital studies of thyroid hormone analogs

1973 ◽  
Vol 95 (26) ◽  
pp. 8518-8525 ◽  
Author(s):  
Peter A. Kollman ◽  
Wallace J. Murray ◽  
Merrill E. Nuss ◽  
Eugene C. Jorgensen ◽  
Steve. Rothenberg
Keyword(s):  
Thyroid Hormone ◽  
Molecular Orbital ◽  
Hormone Analogs

Thyromimetic Activity of Methylene-Bridged Thyroid Hormone Analogs

Endocrinology ◽  
1973 ◽  
Vol 92 (1) ◽  
pp. 243-250 ◽  
Author(s):  
STACY PSYCHOYOS ◽  
S. MA DANIEL ◽  
ANDREW J. CZERNIK ◽  
HELEN SCHLANGEL BOWERS ◽  
CHARLOTTE D. ATKINS ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Hormone Analogs

Translational implications of nongenomic actions of thyroid hormone initiated at its integrin receptor

2009 ◽  
Vol 297 (6) ◽  
pp. E1238-E1246 ◽  
Author(s):  
Paul J. Davis ◽  
Faith B. Davis ◽  
Hung-Yun Lin ◽  
Shaker A. Mousa ◽  
Min Zhou ◽  
...  
Keyword(s):  
Thyroid Hormone ◽  
Cell Surface ◽  
Tumor Cell ◽  
Cell Biology ◽  
Thyroid Hormone Receptor ◽  
Integrin Αvβ3 ◽  
Integrin Receptor ◽  
Cell Functions ◽  
Mediated Effects ◽  
Hormone Analogs

A thyroid hormone receptor on integrin αvβ3 that mediates cell surface-initiated nongenomic actions of thyroid hormone on tumor cell proliferation and on angiogenesis has been described. Transduction of the hormone signal into these recently recognized proliferative effects is by extracellular-regulated kinases 1/2 (ERK1/2). Other nongenomic actions of the hormone may be transduced by phosphatidylinositol 3-kinase (PI3K) and are initiated in cytoplasm or at the cell surface. PI3K-mediated effects are important to angiogenesis or other recently appreciated cell functions but apparently not to tumor cell division. For those actions of thyroid hormone [l-thyroxine (T4) and 3,3′-5-triiodo-l-thyronine (T3)] that begin at the integrin receptor, tetraiodothyroacetic acid (tetrac) is an inhibitor of and probe for the participation of the receptor in downstream intracellular events. In addition, tetrac has actions initiated at the integrin receptor that are unrelated to inhibition of the effects of T4 and T3 but do involve gene transcription in tumor cells. Discussed here are the implications of translating these nongenomic mechanisms of thyroid hormone analogs into clinical cancer cell biology, tumor-related angiogenesis, and modulation of angiogenesis that is not related to cancer.

Ontogenesis of thyroid hormone receptor in foetal lambs

1987 ◽  
Vol 116 (2) ◽  
pp. 205-210 ◽  
Author(s):  
Beatriz Ferreiro ◽  
Juan Bernal ◽  
Brian J. Potter
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Hormone Receptor ◽  
Binding Capacity ◽  
Sedimentation Coefficient ◽  
Receptor Sites ◽  
Nuclear Extracts ◽  
Hormone Analogs ◽  
Neuroblast Proliferation ◽  
The Brain ◽  
Foetal Lamb

Abstract. Affinity and concentration of T3 receptor sites have been measured in nuclear extracts from the brain, lung, and liver of foetal lamb tissues at 50, 82 and 100 days of gestational age. Control experiments indicated that the concentration of sites was similar when nuclear extracts or purified nuclei were used, and that maximal binding capacity was obtained after 2 h of incubation at 22°C. The pattern of receptor binding affinity when different thyroid hormone analogs were used in competition assays with [125I]T3 was T3 > 3,5,3'-triiodothyroacetic acid (Triac) > T4 in the lung and brain. In the liver, Triac had the same affinity as T3. The sedimentation coefficient of the receptor was 3.6 S in lung. There were minor changes of receptor affinity in the brain, but not in the lung or liver, during development with the highest value at 82 days. Receptor concentration increased twice from 50 to 82 days. Since in the brain this is the period of neuroblast proliferation, the results suggest that thyroid hormone is required for proper foetal lamb development and, in particular, for neuroblast proliferation and/or differentiation.

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