[Regulation of 1,25(OH)2D3 (calcitriol) receptor by vitamin B6].
In vitamin B6-deficient rats the concentration of in vivo occupied nuclear and total cellular receptors of 1.25(OH)2D3 increases 1.3-1.7 times, whereas the binding of in vitro occupied receptors to DNA-cellulose increases by 40%. Pyridoxal-5'-phosphate (PLP) added in vitro to solubilized receptors of 1.25(OH)2D3 lowers the ligand binding by 15-25% but causes no dissociation of hormone-receptor complexes formed in vivo. The association of in vitro occupied receptors of 1.25(OH)2D3 with DNA-cellulose is suppressed by PLP (3.5-4.5-fold). It has been shown for the first time that vitamin B6 is a physiological regulator of 1.25(OH)2D3 receptor binding by chromatin and DNA which diminish the concentration of occupied receptors and thus suppress the hormonal response.
Sergeev
M N
MN
Spirichev
V B
VB
D000818:Animals; D001667:Binding, Competitive; D002117:Calcitriol / Q000378:metabolism*; D066298:In Vitro Techniques; D007413:Intestinal Mucosa / Q000378:metabolism; D007421:Intestine, Small / Q000378:metabolism; D008297:Male; D011732:Pyridoxal Phosphate / Q000494:pharmacology; D011869:Radioligand Assay; D051381:Rats; D011919:Rats, Inbred Strains; D018167:Receptors, Calcitriol; D011987:Receptors, Steroid / Q000187:drug effects / Q000378:metabolism*; D026681:Vitamin B 6 Deficiency / Q000378:metabolism*
D018167:Receptors, Calcitriol; D011987:Receptors, Steroid; D011732:Pyridoxal Phosphate; D002117:Calcitriol
Reguliatsii retseptsii 1,25(OH)2D3 (kal'tsitriola) vitaminom B6.