Vitamin a transport between retina and pigment epithelium-an interstitial protein carrying endogenous retinol (interstitial retinol-binding protein)

Gregory I Liou, C. D.B. Bridges, S. L. Fong, R. A. Alvarez, F. Gonzalez-Fernandez

Research output: Contribution to journalArticle

146 Citations (Scopus)

Abstract

We have demonstrated and partially characterized an interstitial retinol-binding protein (IRBP) confined to bovine interphotoreceptor matrix (IPM). The native protein is a concanavalin A-binding glycoprotein with a mol. wt of 260 k as measured by gel-filtration and size-exclusion high-performance liquid chromatography. On SDS-gels, its mol. wt is 140-145 k. Since the protein is glycosylated, this value is probably too high. Hence the native protein may be a dimer consisting of two identical subunits. The endogenous ligand has been analyzed by high-performance liquid chromatography-it consists mainly of all-trans retinol. Occasionally, retinal and 11-cis retinol are also associated with it. The amount of retinol bound to IRBP increases when the eyes are illuminated. The total binding capacity was estimated to represent 4-5% of the retinol released from a total rhodopsin bleach. We have established that, like serum retinol-binding protein, IRBP can also bind retinoic acid, although it has not been established that retinoic acid is an endogenous ligand. The fluorescence emission λmax for IRBP with its native ligand is at 470 nm and the excitation λmax for this fluorescence is at 333 nm. Other retinoid carriers in the interphotoreceptor matrix have molecular weights of about 15 and 33 k. These probably correspond to cellular retinol- and retinal-binding proteins, respectively. Since both proteins have been identified in the pigment epithelium and retina cytosols, their presence in the IPM could be a result of cell damage. We conclude that interstitial retinol-binding protein is the best candidate for a transport protein carrying retinol between the rod outer segments and the pigment epithelium.

Original languageEnglish (US)
Pages (from-to)1457-1467
Number of pages11
JournalVision Research
Volume22
Issue number12
DOIs
StatePublished - Jan 1 1982

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Vitamin A
Vitamins
Retina
Epithelium
Ligands
Tretinoin
Proteins
Fluorescence
Cellular Retinol-Binding Proteins
High Pressure Liquid Chromatography
Rod Cell Outer Segment
Retinol-Binding Proteins
Rhodopsin
Retinoids
Cytosol
Gel Chromatography
Carrier Proteins
Molecular Weight
Gels
interstitial retinol-binding protein

ASJC Scopus subject areas

  • Ophthalmology
  • Sensory Systems

Cite this

Vitamin a transport between retina and pigment epithelium-an interstitial protein carrying endogenous retinol (interstitial retinol-binding protein). / Liou, Gregory I; Bridges, C. D.B.; Fong, S. L.; Alvarez, R. A.; Gonzalez-Fernandez, F.

In: Vision Research, Vol. 22, No. 12, 01.01.1982, p. 1457-1467.

Research output: Contribution to journalArticle

Liou, Gregory I ; Bridges, C. D.B. ; Fong, S. L. ; Alvarez, R. A. ; Gonzalez-Fernandez, F. / Vitamin a transport between retina and pigment epithelium-an interstitial protein carrying endogenous retinol (interstitial retinol-binding protein). In: Vision Research. 1982 ; Vol. 22, No. 12. pp. 1457-1467.
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N2 - We have demonstrated and partially characterized an interstitial retinol-binding protein (IRBP) confined to bovine interphotoreceptor matrix (IPM). The native protein is a concanavalin A-binding glycoprotein with a mol. wt of 260 k as measured by gel-filtration and size-exclusion high-performance liquid chromatography. On SDS-gels, its mol. wt is 140-145 k. Since the protein is glycosylated, this value is probably too high. Hence the native protein may be a dimer consisting of two identical subunits. The endogenous ligand has been analyzed by high-performance liquid chromatography-it consists mainly of all-trans retinol. Occasionally, retinal and 11-cis retinol are also associated with it. The amount of retinol bound to IRBP increases when the eyes are illuminated. The total binding capacity was estimated to represent 4-5% of the retinol released from a total rhodopsin bleach. We have established that, like serum retinol-binding protein, IRBP can also bind retinoic acid, although it has not been established that retinoic acid is an endogenous ligand. The fluorescence emission λmax for IRBP with its native ligand is at 470 nm and the excitation λmax for this fluorescence is at 333 nm. Other retinoid carriers in the interphotoreceptor matrix have molecular weights of about 15 and 33 k. These probably correspond to cellular retinol- and retinal-binding proteins, respectively. Since both proteins have been identified in the pigment epithelium and retina cytosols, their presence in the IPM could be a result of cell damage. We conclude that interstitial retinol-binding protein is the best candidate for a transport protein carrying retinol between the rod outer segments and the pigment epithelium.

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