A gene knockout corroborates the integral function of cellular retinol-binding protein in retinoid metabolism.

Abstract

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.

• Authors: J L Napoli
• Journal: Nutrition reviews (Nutr Rev) Vol. 58 Issue 8 Pg. 230-6 (Aug 2000) ISSN: 0029-6643 [Print] United States
• PMID: 10946560 (Publication Type: Journal Article, Review)

Chemical References

• Amino Acids
• Retinoids
• Retinol-Binding Proteins
• Retinol-Binding Proteins, Cellular
• Vitamin A

Topics

• Amino Acids (genetics, metabolism)
• Animals
• Mice
• Mice, Knockout
• Retinoids (metabolism)
• Retinol-Binding Proteins (genetics, metabolism)
• Retinol-Binding Proteins, Cellular
• Vitamin A (metabolism)