A membrane receptor for retinol binding protein mediates cellular uptake of vitamin A

R Kawaguchi, J Yu, J Honda, J Hu, J Whitelegge… - Science, 2007 - science.org
R Kawaguchi, J Yu, J Honda, J Hu, J Whitelegge, P Ping, P Wiita, D Bok, H Sun
Science, 2007science.org
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 …
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.
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