Characterisation of a retinoic-acid-binding component from F9 embryonal-carcinoma-cell nuclei.
When F9 murine-embryonal-carcinoma cells were incubated with all-trans-[3H]retinoic acid, approximately 10% of the tritium label taken up by the cells was recovered in the nuclei. Sonication or DNase I digestion followed by extraction with 0.6 M NaCl released 20-40% of the nuclear-associated retinoic acid. Analysis of these extracts showed that retinoic acid was bound to protein sedimenting at 4 S. This nuclear retinoic-acid-binding component bound all-trans- and 13-cis-retinoic acid with comparable affinity whereas retinol competed less efficiently for binding. These results suggest that F9 embryonal-carcinoma cells contain a nuclear binding protein for retinoic acid that is distinct from the cellular retinoic-acid-binding protein.
Daly
A K
AK
Department of Dermatology, University of Newcastle-upon-Tyne, England.
Redfern
C P
CP
D000818:Animals; D001665:Binding Sites; D002352:Carrier Proteins / Q000032:analysis; D002467:Cell Nucleus / Q000032:analysis*; D002478:Cells, Cultured; D002499:Centrifugation, Density Gradient; D002851:Chromatography, High Pressure Liquid; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D051379:Mice; D018168:Receptors, Retinoic Acid; D013347:Subcellular Fractions / Q000032:analysis; D013724:Teratoma / Q000032:analysis*; D014212:Tretinoin / Q000378:metabolism*; D014407:Tumor Cells, Cultured
D002352:Carrier Proteins; D018168:Receptors, Retinoic Acid; D014212:Tretinoin