A Membrane Receptor for Retinol Binding Protein Mediates Cellular Uptake of Vitamin A

Author:

Kawaguchi Riki12345,Yu Jiamei12345,Honda Jane12345,Hu Jane12345,Whitelegge Julian12345,Ping Peipei12345,Wiita Patrick12345,Bok Dean12345,Sun Hui12345

Affiliation:

1. Department of Physiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.

2. Jules Stein Eye Institute, David Geffen School of Medicine at UCLA, 100 Stein Plaza, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.

3. Pasarow Mass Spectrometry Laboratory, Semel Institute, David Geffen School of Medicine at UCLA, 760 Westwood Plaza, Los Angeles, CA 90024, USA.

4. Brain Research Institute, UCLA, Los Angeles, CA 90095, USA.

5. Department of Medicine, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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4. D. S. Goodman, in The Retinoids, M. B. Sporn, A. B. Boberts, D. S. Goodman, Eds. (Academic Press, New York, 1984), vol. 2, pp. 41–88.

5. Transport and Storage of Vitamin A

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