July 1987
Volume 28, Issue 7
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Articles  |   July 1987
A 31,000-dalton protein released by cultured human retinal pigment epithelium.
Investigative Ophthalmology & Visual Science July 1987, Vol.28, 1213-1218. doi:
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      R B Edwards, J T Brandt, G S Hardenbergh; A 31,000-dalton protein released by cultured human retinal pigment epithelium.. Invest. Ophthalmol. Vis. Sci. 1987;28(7):1213-1218.

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      © ARVO (1962-2015); The Authors (2016-present)

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Abstract

Confluent primary cultures of human retinal pigment epithelium (RPE) were incubated for 3-14 hr with 35S-methionine, 3H-leucine, or 2-3H-mannose, and the released proteins were analyzed by SDS-polyacrylamide gel electrophoresis. A 31,000-dalton protein constituted 10-70% of the released radioactive proteins. The peak was degraded by pronase and its synthesis was inhibited by cycloheximide. The incorporation of 2-3H-mannose into this protein, and its inhibition by tunicamycin, showed that the protein is glycosylated. Monensin (10(-5) M) also inhibited the release of the 31,000-dalton glycoprotein. The released 31,000-dalton glycoprotein from human RPE comigrated on gels with a protein present in extracts of human interphotoreceptor matrix, raising the possibility that the released protein corresponds to a component of the matrix.

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