Partial characterization of a specific high affinity binding macromolecule for 24R,25 dihydroxyvitamin D3 in differentiating skeletal mesenchyme

D. Sömjen, G. J. Sömjen, A. Harell, G. L. Mechanic, I. Binderman

Research output: Contribution to journalArticlepeer-review

Abstract

Cytosol preparations and cells from 6-day old cultured differentiating chick limb-bud mesenchyme, which consist of a high proportion of chondrocytes, were shown to specifically bind 24R,25 dihydroxycholecalciferol. Nuclei from identical cultures also showed specific binding for 24R,25 dihydroxycholecalciferol. On the contrary, similar preparations of limb-bud mesenchyme cells (6-day old cultures) pretreated on day one by 5-bromodesoxyuridine which induced a fibroblast phenotypic expression, failed to show any specific binding for either 24R,25 or 1α,25 dihydroxycholecalciferol. Pronase treatment of the cytosol indicated that the receptor was protein-like in nature. The chromatographic properties of the protein-receptor on diethylaminoethyl cellulose and Sephadex G-100 columns were similar to those of the protein receptor found for 1α,25 dihydroxycholecalciferol. This report is the first demonstration that a cytosol protein receptor for 24R,25 dihydroxycholecalciferol exists in developing skeletal tissue. 24,25 dihydroxyvitamin D3 but not any of the other metabolites was shown to induce DNA synthesis after 24 h by almost two-fold and protein synthesis after 5 h by 240%. These results suggest an important physiological role for 24R,25 dihydroxyvitamin D3 in the development of skeletal tissue.

Original languageEnglish
Pages (from-to)644-651
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume106
Issue number2
DOIs
StatePublished - 31 May 1982

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