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(Received for publication, December 18, 1995, and in revised form, April 18, 1996)
From the Division of Nutritional Sciences, Savage Hall, Cornell
University, Ithaca, New York 14853-6301
Rapid transport of retinoids across the
interphotoreceptor matrix is a critical part of the visual cycle, since
it serves to replenish bleached rhodopsin with its chromophore
11-cis-retinal. The transport of retinoids in the
interphotoreceptor matrix is believed to be mediated by the
interphotoreceptor retinoid-binding protein (IRBP), a protein that, in
addition to possessing two retinoid-binding sites, associates in
vivo with long chain fatty acids. Here, the interrelationships
between binding of the two types of ligands to IRBP were studied. The
composition of fatty acids associated with IRBP in bovine retina was
determined, and it was found that polyunsaturated fatty acids
constitute a significant fraction of those. It was further found that
docosahexaenoic acid, but not palmitic acid, induced a rapid and
specific release of 11-cis-retinal from one of the
protein's retinoid-binding sites. Based on these results and on the
additional observation that a steep concentration gradient of
docosahexaenoic acid exists between photoreceptor and pigment
epithelium cells, a model for the mechanism by which IRBP may target
11-cis-retinal to photoreceptor cells is proposed.
Volume 271, Number 34,
Issue of August 23, 1996
pp. 20507-20515
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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