Synthesis of interphotoreceptor retinoid-binding protein (IRBP) by monkey retina in organ culture: effect of monensin |
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Authors: | B Wiggert L Lee P J O'Brien G J Chader |
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Affiliation: | Laboratory of Vision Research, National Eye Institute, National Institutes of Health, Bethesda, MD 20205 USA |
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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. |
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Keywords: | IRBP Interphotoreceptor Retinoid-Binding Protein PE pigment epithelium IPS interphotoreceptor space IPM interphotoreceptor matrix SDS sodium dodecylsulfate |
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