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Biosynthesis and Metabolism of Retinoic Acid: Roles of CRBP and CRABP in Retinoic Acid: Roles of CRBP and CRABP in Retinoic Acid Homeostasis^{1, 2,}

Department of Biochemistry, School of Medicine and Biomedical Sciences, SUNY-Buffalo, Buffalo, NY, 14214

The enzymes that constitute the pathway of retinoic acid biosynthesis and metabolism may recognize retinoid binding proteins as effectors and substrates. Apocellular retinol-binding protein (CRBP) stimulates a bile-salt independent membrane-bound retinyl ester hydrolase resulting in the hydrolysis of endogenous retinyl esters and the formation of holoCRBP. HoloCRBP delivers retinol to a microsomal nicotinamide-adenine dinucleotide phosphate-dependent dehydrogenase, protects it from artifactual oxidation and denies enzymes that cannot recognize the binding protein access to retinol. The retinal synthesized may be transferred from the microsomes to the cytosol by CRBP. A cytosolic retinal dehydrogenase has been purified that produces retinoic acid from retinal generated by microsomes in the presence of CRBP and from the complex CRBP-retinal itself. Thus, CRBP(type I) seems to channel retinoids through the reactions of retinoic acid synthesis via a series of protein-protein interactions. Cellular retinoic acid-binding protein (type I) facilitates retinoic acid metabolism by sequestering it and by acting as a low Km substrate, thereby also modulating the steady-state concentrations of retinoic acid.

KEY WORDS: • retinoic acid • CRABP • CRBP • dehydrogenase • retinal • retinol

¹ Presented as part of a symposium, "Retinoids: Cellular Metabolism and Activation," given at the 76th Annual Meeting of the Federation of American Societies for Experimental Biology, Anaheim, CA, April 7, 1992. This conference was sponsored by the American Institute of Nutrition and was supported by grants from the R. W. Johnson Pharmaceutical Research Institute and Hoffman-La Roche, Inc. Guest editor for this symposium was A. Catharine Ross, Departments of Biochemistry and Pediatrics, Medical College of Pennsylvania, Philadelphia, PA 19129.

² This work was supported by USPHS NIH grant DK36870.

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