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Investigative Ophthalmology & Visual Science, Vol 28, 1213-1218, Copyright © 1987 by Association for Research in Vision and Ophthalmology

ARTICLES AND REPORTS

A 31,000-dalton protein released by cultured human retinal pigment epithelium

RB Edwards, JT Brandt and GS Hardenbergh

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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Copyright © 1987 by the Association for Research in Vision and Ophthalmology