A Membrane Receptor for Retinol Binding Protein Mediates Cellular Uptake of Vitamin A
University of California, Los Angeles · Doheny Eye Institute · +1 more institution
Abstract
Vitamin A has diverse biological functions. It is transported in the blood as a complex with retinol binding protein (RBP), but the molecular mechanism by which vitamin A is absorbed by cells from the vitamin A-RBP complex is not clearly understood. We identified in bovine retinal pigment epithelium cells STRA6, a multitransmembrane domain protein, as a specific membrane receptor for RBP. STRA6 binds to RBP with high affinity and has robust vitamin A uptake activity from the vitamin A-RBP complex. It is widely expressed in embryonic development and in adult organ systems. The RBP receptor represents a major physiological mediator of cellular vitamin A uptake.
Citation impact
- FWCI
- 21.26
- Percentile
- 100%
- References
- 39
Authors
9- RKRiki Kawaguchi
University of California, Los Angeles, Doheny Eye Institute, Polish Academy of Sciences
- JYJiamei Yu
University of California, Los Angeles, Doheny Eye Institute, Polish Academy of Sciences
- JHJane Honda
University of California, Los Angeles, Doheny Eye Institute, Polish Academy of Sciences
- JHJane Hu
University of California, Los Angeles, Doheny Eye Institute, Polish Academy of Sciences
- JPJulian P. Whitelegge
University of California, Los Angeles, Doheny Eye Institute, Polish Academy of Sciences
Topics & keywords
- Retinol binding protein
- Retinol
- Chemistry
- Vitamin
- Membrane
- Receptor
- Transport protein
- Cell biology