期刊
SCIENCE
卷 315, 期 5813, 页码 820-825出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1136244
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资金
- NEI NIH HHS [5T32EY07026] Funding Source: Medline
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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