Retinoid-binding proteins.
Much has been learned during the past decade about the specific retinoid-binding proteins that exist in plasma and in the intracellular compartment in a number of tissues. Vitamin A is mobilized from liver stores and transported in plasma in the form of the lipid alcohol retinol, bound to a specific transport protein, retinol-binding protein (RBP). A great deal is now known about the chemical structure, metabolism, and biologic roles of RBP. A number of tissues of rats, humans, and other species contain soluble binding proteins with specificity for either retinol (cellular retinol-binding protein, CRBP) or retinoic acid (cellular retinoic acid-binding protein, CRABP). These intracellular proteins have been purified from several tissues and partly characterized. This paper provides a concise review of our current knowledge about the three retinoid-binding proteins, RBP, CRBP, and CRABP.
D000818:Animals; D002352:Carrier Proteins / Q000378:metabolism*; D002417:Cattle; D055598:Chemical Phenomena; D002621:Chemistry; D004285:Dogs; D006801:Humans; D008099:Liver / Q000378:metabolism; D008297:Male; D051379:Mice; D008970:Molecular Weight; D009363:Neoplasm Proteins / Q000378:metabolism*; D009369:Neoplasms / Q000378:metabolism; D011863:Radioimmunoassay; D051381:Rats; D018168:Receptors, Retinoic Acid; D012177:Retinol-Binding Proteins / Q000378:metabolism*; D054840:Retinol-Binding Proteins, Cellular; D054839:Retinol-Binding Proteins, Plasma; D013737:Testis / Q000378:metabolism
D002352:Carrier Proteins; D009363:Neoplasm Proteins; D018168:Receptors, Retinoic Acid; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D054839:Retinol-Binding Proteins, Plasma