Vitamin A receptors. Retinoic acid binding in ocular tissues.
Analysis of the sucrose-density-gradient patterns of the 110 000g supernatant fractions of adult and foetal retina and pigment epithelium showed them to contain a limited number of highly specific binding sites ('receptors') for [3H]retinoic acid that sediment at approx. 2S. Binding in pigment epithelium is higher than in any tissue yet reported. A 5S binding component is also observed and is probably due to serum contamination. Fractionation studies indicate that [3H]retinoic acid binding in the retina is lower in the photoreceptor units than in the retinal inner layers. This is in contrast with previous results that show greater [3H]retinol binding in photoreceptors. Studies with dystrophic human and rat retinas, which lack the photoreceptor layers, confirm that [3H]retinoic acid binding is greater in the non-photoreceptor layers of the retina. No specific [3H]retinoic acid binding is found in corneal epithelium, although endothelium and the conjunctiva demonstrate specific 2S binding. Such differences in retinol and retinoic acid binding may indicate different roles for the two compounds in ocular tissues.
D000818:Animals; D001665:Binding Sites; D002417:Cattle; D002499:Centrifugation, Density Gradient; D002642:Chick Embryo; D002645:Chickens; D003315:Cornea / Q000378:metabolism; D005123:Eye / Q000196:embryology / Q000378:metabolism*; D000882:Haplorhini; D006801:Humans; D010857:Pigment Epithelium of Eye / Q000378:metabolism; D051381:Rats; D011955:Receptors, Drug / Q000378:metabolism; D012160:Retina / Q000378:metabolism; D012162:Retinal Degeneration / Q000378:metabolism; D014212:Tretinoin / Q000378:metabolism*; D014801:Vitamin A / Q000031:analogs & derivatives*
D011955:Receptors, Drug; D014801:Vitamin A; D014212:Tretinoin