A gene knockout corroborates the integral function of cellular retinol-binding protein in retinoid metabolism.
Continually expanding evidence has moved inexorably toward establishing key functions for cellular retinol-binding protein (CRBP) in retinoid metabolism. These experimental data integrate into a model of CRBP as a chaperone that protects retinol from the cellular milieu and interacts with certain retinoid-metabolizing enzymes. Mutant mice with an inactivated CRBP gene show decreased liver retinyl ester storage, a shorter elimination half-life of liver retinoids, and predisposition to vitamin A deficiency. No morphologic phenotype was observed until vitamin A was exhausted. Although the mechanisms underlying diminished vitamin A in the CRBP-null mice have not been elucidated, the observations support the model of CRBP as a chaperone of retinoid metabolism.
Napoli
J L
JL
Department of Nutritional Sciences and Toxicology, University of California, Berkeley 94720-3104, USA.
D000596:Amino Acids / Q000235:genetics* / Q000378:metabolism; D000818:Animals; D051379:Mice; D018345:Mice, Knockout; D012176:Retinoids / Q000378:metabolism*; D012177:Retinol-Binding Proteins / Q000235:genetics / Q000378:metabolism*; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A / Q000378:metabolism
D000596:Amino Acids; D012176:Retinoids; D012177:Retinol-Binding Proteins; D054840:Retinol-Binding Proteins, Cellular; D014801:Vitamin A