Characteristics of [3H]1α, 25-(OH)2D3 binding to nuclear fractions from rat pituitary adenoma GH3 cells

Harris A. Gelbard*, Paula H. Stern, David C. U'Prichard

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

3 Scopus citations

Abstract

Specific high affinity binding sites for [3H]1α, 25-dihydroxy-vitamin D3 were observed in nuclear fractions of rat pituitary adenoma GH3 cells. Crude nuclear (P1) sites demonstrated a pharmacological specificity for vitamin D3 metabolites and analogues that was in accord with the characteristics of 1α, 25-dihydroxyvitamin D3 receptors in recognized target organs. GH3 cells grown in serum-containing medium contained significant amounts of 1α, 25-dihydroxy-vitamin D3 in a P1 extract, whereas no 1α, 25-dihydroxyvitamin D3 was detectable in P1 extracts from cells cultured in the absence of serum. Binding of [3H]1α, 25-dihydroxyvitamin D3 to the P1 fraction was unaffected by prior depletion of intracellular 1α, 25-dihydroxyvitamin D3, suggesting that association of [3H]1α, 25-dihydroxyvitamin D3 to nuclear sites is not attributable to translocation of a cytosolic hormone-receptor complex and molecular exchange. The results support the concept that 1α, 25-dihydroxyvitamin D3 has a physiological role in mediating pituitary hormone secretion.

Original languageEnglish (US)
Pages (from-to)1051-1056
Number of pages6
JournalLife Sciences
Volume29
Issue number10
DOIs
StatePublished - Sep 7 1981

ASJC Scopus subject areas

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

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