Thyroid hormones
Thyroid hormones are two hormones produced and released by the thyroid gland, namely triiodothyronine (T) and thyroxine (T). They are tyrosine-based hormones that are primarily responsible for regulation of metabolism. T and T are partially composed of iodine. A deficiency of iodine leads to decreased production of T and T, enlarges the thyroid tissue and will cause the disease known as simple goitre. The major form of thyroid hormone in the blood is thyroxine (T), which has a longer half-life than T. In humans, the ratio of T to T released into the blood is approximately 14:1. T is converted to the active T (three to four times more potent than T) within cells by deiodinases (5'-iodinase). These are further processed by decarboxylation and deiodination to produce iodothyronamine (Ta) and thyronamine (Ta). All three isoforms of the deiodinases are selenium-containing enzymes, thus dietary selenium is essential for T production. Edward Calvin Kendall was responsible for the isolation of thyroxine in 1915.
Thyroxine-binding globulin
Thyroxine-binding globulin (TBG) is a globulin that binds thyroid hormones in circulation. It is one of three transport proteins (along with transthyretin and serum albumin) responsible for carrying the thyroid hormones thyroxine (T) and triiodothyronine (T) in the bloodstream. Of these three proteins, TBG has the highest affinity for T and T but is present in the lowest concentration. Despite its low concentration, TBG carries the majority of T in the blood plasma. Due to the very low concentration of T and T in the blood, TBG is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, TBG has a single binding site for T/T. TBG is synthesized primarily in the liver as a 54-kDa protein. In terms of genomics, TBG is a serpin; however, it has no inhibitory function like many other members of this class of proteins.