Synthesis of interphotoreceptor retinoid-binding protein (IRBP) by monkey retina in organ culture: effect of monensin

Biochemical and Biophysical Research Communications
B WiggertG J Chader

Abstract

Whole monkey retinas were incubated in short-term organ culture with either radiolabeled amino acids or glucosamine. Soluble retinal proteins and proteins in the culture medium were analyzed by SDS-poly-acrylamide gel electrophoresis. Fluorography showed that the interphotoreceptor retinoid-binding protein (IRBP), a 146,000 Mr glycoprotein localized in the extracellular matrix, is synthesized by the neural retina and rapidly secreted into the medium. Secretion is blocked by 10-5M monensin. No significant IRBP synthesis was observed in the pigment-epithelium-choroid complex. IRBP is thus the major component synthesized and secreted by the neural retina into the interphotoreceptor space. This, and its affinity for retinoid makes it a prime candidate for an extracellular retinoid transport vehicle.

References

Dec 1, 1978·The Journal of Cell Biology·A TartakoffM Détraz
Jan 6, 1977·Nature·D R BergsmaC J Chader
Jan 4, 1979·Biochimica Et Biophysica Acta·B WiggertG J Chader
Nov 1, 1977·The Journal of Experimental Medicine·A M Tartakoff, P Vassalli
Sep 1, 1983·The Journal of Cell Biology·A H Bunt-Milam, J C Saari

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Citations

Sep 30, 1985·Biochemical and Biophysical Research Communications·D J BarrettJ M Nickerson
Jan 1, 1985·Neurochemistry International·C D BridgesR L Font
Jan 1, 1986·Neurochemistry International·C D BridgesR A Alvarez
Jan 1, 1988·Neurochemistry International·B WiggertG J Chader
Jan 1, 1988·Eye·A ShallalS al-Mahdawi
Sep 1, 1986·The Journal of Experimental Zoology·C D BridgesS L Fong

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