Effect of pyridoxal 5'-phosphate on the 1,25-dihydroxyvitamin D3 receptor system.

doi:10.3177/JNSV.29.533

Paper

Effect of pyridoxal 5'-phosphate on the 1,25-dihydroxyvitamin D3 receptor system.

Published Oct 1, 1983 · F. Shimura, M. Watanabe, J. Shimura

Journal of nutritional science and vitaminology

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5

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Abstract

The effect of pyridoxal 5'-phosphate on the 1,25-dihydroxyvitamin D3 receptor system has been studied by using pig intestinal chromatin. Pyridoxal 5'-phosphate did not affect the binding of 1,25-dihydroxyvitamin D3 to its receptor extracted from chromatin with hypertonic KCl, although in the presence of pyridoxal 5'-phosphate 1,25-dihydroxyvitamin D3-receptor complexes were not readily precipitated with polyethylene glycol. In contrast, pyridoxal 5'-phosphate showed a potency to dissociate the 1,25-dihydroxyvitamin D3 receptor from chromatin in a dose-dependent manner. A low concentration of pyridoxal 5'-phosphate was as effective as hypertonic KCl in dissociating the receptor from chromatin, while pyridoxine, p-nitrophenyl phosphate, or inorganic phosphate was much less effective. These observations suggest the inhibitory effect of pyridoxal 5'-phosphate on the recognition of 1,25-dihydroxyvitamin D3 by its receptor system.

In Vitro Study

Study Snapshot

Pyridoxal 5'-phosphate inhibits the recognition of 1,25-dihydroxyvitamin D3 by its receptor system, suggesting its potential role in regulating vitamin D3 metabolism.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

Effect of pyridoxal 5'-phosphate on the 1,25-dihydroxyvitamin D3 receptor system.

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References

Effect of vitamin D status on the equilibrium between occupied and unoccupied 1,25-dihydroxyvitamin D intestinal receptors in the chick.

The equilibrium between occupied and unoccupied 1,25-dihydroxyvitamin D intestinal receptors in chicks is determined by a simple equilibrium between serum 1,25-OH-D(3) and unoccupied receptors, with a positive correlation between occupied receptor and calcium binding protein levels.

Extraction of nuclear androgen receptors from rat prostate with different reagents

Androgen receptors in rat prostate can be effectively extracted from nuclei using certain reagents with a strongly negatively charged group and a less polar or hydrophobic region, influencing their sedimentation values and precipitability with protamine sulphate.

Effect of pyridoxal phosphate on the androgen receptor from rat prostate: inhibition of receptor aggregation and receptor binding to nuclei and to DNA-cellulose.

Pyridoxal phosphate inhibits androgen receptor binding to DNA-cellulose and prostate nuclei, preventing receptor aggregation in low salt gradients.

Pyridoxine deficiency influences the behavior of the glucocorticoid . receptor complex.

Pyridoxine deficiency increases activatable hepatic glucocorticoid receptor complexes and accelerates their translocation to nuclei in vitro, suggesting a potential role in glucocorticoid-induced liver injury.

Effects of pyridoxal 5'-phosphate on uterine estrogen receptor. II. Inhibition of estrogen . receptor transformation.

Pyridoxal 5'-phosphate inhibits estrogen receptor transformation from nonactivated to activated form in cytosol, potentially affecting its activation and translocation to the nucleus.

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