Characterization, Localization, and Biosynthesis of an Interstitial Retinol‐Binding Glycoprotein in the Human Eye

S. ‐L Fong, Gregory I Liou, R. A. Landers, R. A. Alvarez, F. Gonzalez‐Fernandez, P. A. Glazebrook, D. M.K. Lam, C. D.B. Bridges

Research output: Contribution to journalArticle

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Abstract

Abstract: Human eyes contain an Mr 135K retinol‐binding protein that is analogous to interstitial retinol‐binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I‐concanavalin A, 125I‐wheat germ agglutinin and 125I‐Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol‐binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.

Original languageEnglish (US)
Pages (from-to)1667-1676
Number of pages10
JournalJournal of Neurochemistry
Volume42
Issue number6
DOIs
StatePublished - Jan 1 1984

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Biosynthesis
Glycoproteins
Retina
Proteins
Wheat Germ Agglutinins
Fucose
Agglutinins
Hemagglutinins
Vitamin A
Oligosaccharides
Immunoprecipitation
Lectins
Pigments
Leucine
Haplorhini
Immunoglobulins
Blood Proteins
Carrier Proteins
Epithelium
Immunohistochemistry

Keywords

  • Glycoprotein
  • Human
  • Interphotoreceptor matrix
  • Monkey
  • Pigment epithelium
  • Retina
  • Retinol
  • Retinol‐binding protein

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience

Cite this

Fong, S. L., Liou, G. I., Landers, R. A., Alvarez, R. A., Gonzalez‐Fernandez, F., Glazebrook, P. A., ... Bridges, C. D. B. (1984). Characterization, Localization, and Biosynthesis of an Interstitial Retinol‐Binding Glycoprotein in the Human Eye. Journal of Neurochemistry, 42(6), 1667-1676. https://doi.org/10.1111/j.1471-4159.1984.tb12758.x

Characterization, Localization, and Biosynthesis of an Interstitial Retinol‐Binding Glycoprotein in the Human Eye. / Fong, S. ‐L; Liou, Gregory I; Landers, R. A.; Alvarez, R. A.; Gonzalez‐Fernandez, F.; Glazebrook, P. A.; Lam, D. M.K.; Bridges, C. D.B.

In: Journal of Neurochemistry, Vol. 42, No. 6, 01.01.1984, p. 1667-1676.

Research output: Contribution to journalArticle

Fong, SL, Liou, GI, Landers, RA, Alvarez, RA, Gonzalez‐Fernandez, F, Glazebrook, PA, Lam, DMK & Bridges, CDB 1984, 'Characterization, Localization, and Biosynthesis of an Interstitial Retinol‐Binding Glycoprotein in the Human Eye', Journal of Neurochemistry, vol. 42, no. 6, pp. 1667-1676. https://doi.org/10.1111/j.1471-4159.1984.tb12758.x
Fong, S. ‐L ; Liou, Gregory I ; Landers, R. A. ; Alvarez, R. A. ; Gonzalez‐Fernandez, F. ; Glazebrook, P. A. ; Lam, D. M.K. ; Bridges, C. D.B. / Characterization, Localization, and Biosynthesis of an Interstitial Retinol‐Binding Glycoprotein in the Human Eye. In: Journal of Neurochemistry. 1984 ; Vol. 42, No. 6. pp. 1667-1676.
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abstract = "Abstract: Human eyes contain an Mr 135K retinol‐binding protein that is analogous to interstitial retinol‐binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I‐concanavalin A, 125I‐wheat germ agglutinin and 125I‐Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol‐binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.",
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N2 - Abstract: Human eyes contain an Mr 135K retinol‐binding protein that is analogous to interstitial retinol‐binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I‐concanavalin A, 125I‐wheat germ agglutinin and 125I‐Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol‐binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.

AB - Abstract: Human eyes contain an Mr 135K retinol‐binding protein that is analogous to interstitial retinol‐binding protein (IRBP) in the subretinal space of bovine eyes. It is a glycoprotein, because it binds 125I‐concanavalin A, 125I‐wheat germ agglutinin and 125I‐Lens culinaris hemagglutinin. It does not bind Ricinus communis agglutinin I. After desialation, it binds Ricinus communis agglutinin I, but loses its capacity to bind wheat germ agglutinin. These observations, coupled with the known specificities of these lectins, suggest that at least one of the oligosaccharide chains is a sialated, biantennary complex type containing fucose. Both by direct analysis of dissected ocular tissues and by immunocytochemistry it was shown that human interstitial retinol binding protein is an extracellular protein that is confined predominantly to the subretinal space. Monkey retinas incubated in vitro in medium containing [3H]leucine were shown to synthesize and secrete this protein into the medium, a conclusion that was confirmed by immunoprecipitation with an immunoglobulin fraction prepared from rabbit antibovine IRBP serum. Virtually no other labeled proteins were detectable in the medium. It is concluded that interstitial retinol‐binding protein meets many of the requirements for a putative transport protein implicated in the transfer of retinol between the pigment epithelium and retina during the visual cycle, and that the neural retina may play an important role in regulating its amount in the subretinal space.

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