| Literature DB >> 17255476 |
Riki Kawaguchi1, Jiamei Yu, Jane Honda, Jane Hu, Julian Whitelegge, Peipei Ping, Patrick Wiita, Dean Bok, Hui Sun.
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.Entities:
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Year: 2007 PMID: 17255476 DOI: 10.1126/science.1136244
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728