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Vitamin D-binding protein (DBP), also/originally known as gc-globulin (group-specific component), is a protein that in humans is encoded by the GC gene. [ 5 ] [ 6 ] DBP is genetically the oldest member of the albuminoid family and appeared early in the evolution of vertebrates.
Metabolites produced from vitamin D 2 tend to bind less well to the vitamin D-binding protein. [3] Vitamin D 3 can alternatively be hydroxylated to calcifediol by sterol 27-hydroxylase, an enzyme coded for by gene CYP27A1, but vitamin D 2 cannot. [3] Ergocalciferol can be directly hydroxylated at position 24 by the enzyme coded for by CYP27A1. [3]
Transcription of the CYP24A1 gene is markedly inducible by 1,25-(OH) 2 D 3 binding to the vitamin D receptor. [6] The gene has a strong, positive vitamin D response element in the promoter . Through regulation of CYP24A1 expression, a negative feedback control system is created to limit the effects of 1,25-(OH) 2 D 3 .
Vitamin D-binding protein (DBP)(also referred to as Gc-globulin) is synthesized primarily in the liver. This entry outlines the domain III of DBP. Domain III (amino acid 379–458) is G-actin binding region located in the C-terminal. Domain (amino acids 373 to 403). This protein is found ubiquitously in vivo in significant quantities and can be ...
The Institute of Medicine in 2010 recommended a maximum uptake of vitamin D of 4000 IU/d, finding that the dose for lowest observed adverse effect level is 40,000 IU daily for at least 12 weeks, [25] and that there was a single case of toxicity above 10 000 IU after more than seven years of daily intake; this case of toxicity occurred in ...
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Calcifediol binds in the blood to vitamin D-binding protein (also known as gc-globulin) and is the main circulating vitamin D metabolite. [4] [5] Calcifediol has an elimination half-life of around 15 to 30 days. [4] [9] Calcifediol is further hydroxylated at the 1-alpha-position in the kidneys to form 1,25-(OH) 2 D 3, calcitriol.
Calbindins are three different calcium-binding proteins: calbindin, calretinin and S100G. They were originally described as vitamin D-dependent calcium-binding proteins in the intestine and kidney of chicks and mammals. They are now classified in different subfamilies as they differ in the number of Ca 2+ binding EF hands.
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