Protein thyroid hormones

The steroid hormones act on cytoplasmic receptors, and the resulting complex moves to the nucleus to influence DNA transcription of proteins. Thyroid hormone directly enters the nucleus where it alters DNA, causing production of. certain enzymes. A particular chemical may have more than one receptor type (e.g., alpha and beta receptors). Epinephrine, for instance, acts on alpha-1 receptors to produce vasoconstriction, and on beta-2 receptors to produce vasodilation. 

Most proteins Thyroid hormones Maternal IgM, IgA Maternal and fetal erythrocytes... 

H5. Hamolsky, M. W., Stein, M., Fischer, D. B., and Freedberg, A. 8., Further studies of factors affecting the plasma protein-thyroid hormone complex. Endocrinology 68, 662-670 (1961). 

Once thyroid hormone enters a cell, it binds temporarily with a spt plasmic protein. Thyroid hormone molecules migrate to the nucleus chondria, where they bind to receptors. In the nucleus the binding hormone initiates the transcription of genes that play crucial roles i of cellular processes, such as those that code for growth hormone a ATPase. In mitochondria, thyroid hormones promote oxygen consur increased fatty acid oxidation. (The mechanism by which this latter pro< is not understood.)... 

Hamolsky, M. W., A. Golodetz, and A. S. Freedberg. 1959. The plasma protein-thyroid hormone complex in man. IB. Further studies on the use of the in vitro red blood cell uptake of Ij3j triiodothyronine as a diagnostic test of thyroid function. Journal of Clinical Endrocrinology and Metabolism 19 101-116. 

Amino acid-derived hormones include the catecholamines, epinephrine and norepinephrine (qv), and the thyroid hormones, thyroxine and triiodothyronine (see Thyroid AND ANTITHYROID PREPARATIONS). Catecholamines are synthesized from the amino acid tyrosine by a series of enzymatic reactions that include hydroxylations, decarboxylations, and methylations. Thyroid hormones also are derived from tyrosine iodination of the tyrosine residues on a large protein backbone results in the production of active hormone. 

Metabolic Functions. The functions of the thyroid hormones and thus of iodine are control of energy transductions (121). These hormones increase oxygen consumption and basal metaboHc rate by accelerating reactions in nearly all cells of the body. A part of this effect is attributed to increase in activity of many enzymes. Additionally, protein synthesis is affected by the thyroid hormones (121,122). 

Only small amounts of free T are present in plasma. Most T is bound to the specific carrier, ie, thyroxine-binding protein. T, which is very loosely bound to protein, passes rapidly from blood to cells, and accounts for 30—40% of total thyroid hormone activity (121). Most of the T may be produced by conversion of T at the site of action of the hormone by the selenoenzyme deiodinase (114). That is, T may be a prehormone requiring conversion to T to exert its metaboHc effect (123). 

The class III cytokine receptor family includes two TNE receptors, the low affinity NGE receptor and 7-ceU surface recognition sites that appear to play a role in proliferation, apoptosis, and immunodeficiency. TNE-a (- 17, 000 protein) is produced by astrocytes and microglia and can induce fever, induce slow-wave sleep, reduce feeding, stimulate prostaglandin synthesis, stimulate corticotrophin-releasing factor and prolactin secretion, and reduce thyroid hormone secretion. TNE-a stimulates IL-1 release, is cytotoxic to oligodendrocytes, and reduces myelination this has been impHcated in multiple sclerosis and encephalomyelitis. Astrocyte TNE-a receptors mediate effects on IL-6 expression and augment astrocytic expression of MHC in response to other stimulants such as lEN-y. 

Using any of the carrier proteins available in highly purified form, eg, TBG or TBPA, a convenient and accurate quantitative determination of and is possible by displacement of radioiodinated or T. This procedure enables their quick determination at low concentrations even in the presence of coundess other substances that occur in body duids (31). In a similar fashion, intact cell nuclei or solubilized proteins from rat fiver cell nuclei, which display high affinities for thyroid hormones, especially T, have been used to establish relative binding affinities of many thyromimetic compounds (7). 

Thyroid autonomy appears as a solitary toxic nodule or toxic multinodular goitre. In toxic thyroid, the nodule s synthesis and secretion of thyroid hormones is autonomous from the thyroid-stimulating hormone (TSH), which is produced in the pituitary gland. Accordingly TSH is suppressed and the extranodular thyroid tissue is functionally downregulated. Thyroid autonomy occurs frequently in iodine-deficient countries, whereas it is much less common in iodine-sufficient areas. Constitu-tively activating mutations in the TSH receptor and in the Gs a protein are the major molecular aetiology of toxic thyroid nodules. 

Thyroxine (3, 5, 3,5-L-teraiodothyronine, T4) is a thyroid hormone, which is transformed in peripheral tissues by the enzyme 5 -monodeiodinase to triiodothyronine. T4 is 3-8 times less active than triiodothyronine. T4 circulates in plasma bound to plasma proteins (T4-binding globulin, T4-binding prealbumin and albumin). It is effective in its free non-protein-bound form, which accounts for less than 1%. Its half-life is about 190 h. 

Triiodothyronine (3, 5,3-L-triiodothyronine, T3) is a thyroid hormone. It is producedby outer ring deiodination of thyroxine (T4) in peripheral tissues. The biologic activity of T3 is 3-8 times higher than that of T4. T3 is 99.7% protein-bound and is effective in its free non-protein-bound form. The half-life of triiodothyronine is about 19 h. The daily tur nover of T3 is 75%. Triiodothyronine acts via nuclear receptor binding with subsequent induction of protein synthesis. Effects of thyroid hormones are apparent in almost all organ systems. They include effects on the basal metabolic rate and the metabolisms of proteins, lipids and carbohydrates. 

Thyrotropin (TSH) regulates the production and secretion of thyroid hormones as well as thyroid epithelial cell growth via the TSH receptor. The TSH receptor belongs to the family of G protein-coupled receptors. It is composed of 764 amino acids. The receptor contains a long hydrophilic region orientated towards the exterior of the cell (ectodomain), 7 hydrophobic transmembrane domains and a short cytoplasmic region. 

Bartalina L Thyroid hormone-binding proteins update 1994. En-docr Rev 1994 13 140. 

POTTER s M, FERTILE J and BERBER-JIMENEZ M D (1996) Soy protein concentrate and isolated soy protein similarly lower blood serum cholesterol hut differently affect thyroid hormones in hamsters. J Nutr. 126 (8) 2007-11. 

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