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Thyroid Hormone Synthesis
Last Updated: 2019-09-12
Thyroid hormone synthesis is a process that occurs in the thyroid gland in humans that results in the production of thyroid hormones which regulate many different processes in the body, such as metabolism, temperature regulation and growth/development. Thyroid hormone synthesis begins in the nucleus of a thyroid follicular cell, as thyroglobulin synthesis occurs here and is transported to the endoplasmic reticulum. From there, thyroglobulin transported through endocytosis into the intracellular space, and then transported through exocytosis to the follicle colloid. There, thyroglobulin is joined by iodide that has been transported from the blood, through the thyroid follicular cell and arrived in the the follicle colloid using pendrin, and hydrogen peroxide to be catalyzed by thyroid peroxidase, creating thyroglobulin + iodotyrosine. Then, iodide, hydrogen peroxide and thyroidperoxidase create thyroglobulin + 3,5-diiodo-L-tyrosine. Thyroglobulin+3,5-diiodo-L-tyrosine then joins with hydrogen peroxide and thyroid peroxidase to create thyroglobulin + 2-aminoacrylic acid and thyroglobulin+liothyronine. Thyroglobulin + liothyronine then goes through two processes, the first being its transportation into the cell and undergoing of proteolysis, which is followed by liothyronine being transported into the bloodstream. The second process is thyroglobulin + liothyronine being catalyzed by thyroid peroxidase and resulting in the production of thyroglobulin + thyroxine. Thyroglobulin + thyroxine is then transported back into the cell, undergoes proteolysis, and thyroxine alone is transported back out of the cell and into the bloodstream.
Thyroid Hormone Synthesis References
Mercken L, Simons MJ, Swillens S, Massaer M, Vassart G: Primary structure of bovine thyroglobulin deduced from the sequence of its 8,431-base complementary DNA. Nature. 1985 Aug 15-21;316(6029):647-51. doi: 10.1038/316647a0.Pubmed: 3855243
Mercken L, Simons MJ, De Martynoff G, Swillens S, Vassart G: Presence of hormonogenic and repetitive domains in the first 930 amino acids of bovine thyroglobulin as deduced from the cDNA sequence. Eur J Biochem. 1985 Feb 15;147(1):59-64. doi: 10.1111/j.1432-1033.1985.tb08718.x.Pubmed: 3855750
de Martynoff G, Pohl V, Mercken L, van Ommen GJ, Vassart G: Structural organization of the bovine thyroglobulin gene and of its 5'-flanking region. Eur J Biochem. 1987 May 4;164(3):591-9. doi: 10.1111/j.1432-1033.1987.tb11168.x.Pubmed: 3032624
Dull TJ, Uyeda C, Strosberg AD, Nedwin G, Seilhamer JJ: Molecular cloning of cDNAs encoding bovine and human lactoperoxidase. DNA Cell Biol. 1990 Sep;9(7):499-509. doi: 10.1089/dna.1990.9.499.Pubmed: 2222811
Cals MM, Mailliart P, Brignon G, Anglade P, Dumas BR: Primary structure of bovine lactoperoxidase, a fourth member of a mammalian heme peroxidase family. Eur J Biochem. 1991 Jun 15;198(3):733-9. doi: 10.1111/j.1432-1033.1991.tb16073.x.Pubmed: 2050150
Watanabe S, Murata S, Kumura H, Nakamura S, Bollen A, Moguilevsky N, Shimazaki K: Bovine lactoperoxidase and its recombinant: comparison of structure and some biochemical properties. Biochem Biophys Res Commun. 2000 Aug 11;274(3):756-61. doi: 10.1006/bbrc.2000.3217.Pubmed: 10924350
Davis AR, Mascolo PL, Bunger PL, Sipes KM, Quinn MT: Cloning and sequencing of the bovine flavocytochrome b subunit proteins, gp91-phox and p22-phox: comparison with other known flavocytochrome b sequences. J Leukoc Biol. 1998 Jul;64(1):114-23. doi: 10.1002/jlb.64.1.114.Pubmed: 9665285
This pathway was propagated using PathWhiz - Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0000716
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