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A Membrane Receptor for Retinol Binding Protein Mediates Cellular Uptake of Vitamin A
Riki Kawaguchi,1,2
Jiamei Yu,1
Jane Honda,1
Jane Hu,2
Julian Whitelegge,3,4
Peipei Ping,1,5
Patrick Wiita,1
Dean Bok,2,4,6
Hui Sun1,2,4*
Abstract:
Vitamin A has diverse biological functions. It is transportedin the blood as a complex with retinol binding protein (RBP),but the molecular mechanism by which vitamin A is absorbed bycells from the vitamin ARBP complex is not clearly understood.We identified in bovine retinal pigment epithelium cells STRA6,a multitransmembrane domain protein, as a specific membranereceptor for RBP. STRA6 binds to RBP with high affinity andhas robust vitamin A uptake activity from the vitamin ARBPcomplex. It is widely expressed in embryonic development andin adult organ systems. The RBP receptor represents a majorphysiological mediator of cellular vitamin A uptake.
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. 6 Department of Neurobiology, David Geffen School of Medicine at UCLA, 650 Charles E. Young Drive South, Los Angeles, CA 90095, USA.
Note added in proof: A recent human genetic study (41) foundthat mutations in the human STRA6 gene are associated with widespreadbirth defects in multiple organ systems. This is consistentwith the expression of STRA6 and the diverse functions of vitaminA in embryonic development.
* To whom correspondence should be addressed. E-mail: hsun{at}mednet.ucla.edu
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