Nuclear and cytoplasmic binding components for vitamin D metabolites

Peter F. Brumbaugh, Mark R. Haussler

Research output: Contribution to journalArticle

54 Scopus citations

Abstract

Specific binding of 1α,25-dihydroxyvitamin D3 to macromolecular components of small intestinal nuclei and cytosol is demonstrated. The nuclear 1α,25-dihydroxyvitamin D3 complex can be extracted from chromatin by 0.3 M KCl and sediments at 3.7S in sucrose density gradients. The cytoplasmic 1α,25-dihydroxyvitamin D3-binding components also sediment at 3.7S, identically to the nuclear complex under the ultracentrifugation procedures employed. Macromolecular binding components with a high affinity for 25-hydroxyvitamin D3 (Kd = 4.5 × 10-9 M) were also identified in intestinal cytosol which differ from the 1α,25-hydroxyvitamin D3 receptor in that: 1) they sediment at 5-6S in sucrose gradients, 2) they are observed in organs other than the intestine, and 3) while they do bind 1α,25-dihydroxyvitamin D3 at higher concentrations than 25-hydroxyvitamin D3, they are not observed to transfer either 25-hydroxyvitamin D3 or 1α,25-dihydroxyvitamin D3 to the nucleus, in vitro.

Original languageEnglish (US)
Pages (from-to)353-362
Number of pages10
JournalLife Sciences
Volume16
Issue number3
DOIs
StatePublished - Feb 1 1975

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)
  • Pharmacology, Toxicology and Pharmaceutics(all)

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