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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
MeSH terms
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Acyltransferases / metabolism
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Amino Acid Sequence
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Animals
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Blood-Retinal Barrier
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COS Cells
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Cattle
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Cell Line
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Cell Line, Tumor
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Cell Membrane / metabolism
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Chlorocebus aethiops
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Embryonic Development
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Endocytosis
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Humans
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Molecular Sequence Data
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Mutation, Missense
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Pigment Epithelium of Eye / metabolism*
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Placenta / metabolism
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Receptors, Cell Surface / metabolism*
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Retinal Vessels / metabolism
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Retinol-Binding Proteins / metabolism*
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Spleen / metabolism
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Transfection
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Vitamin A / metabolism*
Substances
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Receptors, Cell Surface
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Retinol-Binding Proteins
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retinol binding protein receptor
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Vitamin A
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Acyltransferases
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lecithin-retinol acyltransferase