Identification and partial characterization of two major proteins of Mr 47,000 synthesized by bovine retinal endothelial cells in culture

A E Canfield, A M Schor, D C West, S L Schor, M E Grant

    Research output: Contribution to journalArticle

    5 Citations (Scopus)

    Abstract

    Biosynthetic experiments with cultured bovine retinal endothelial cells have identified a glycoprotein of Mr 47,000 (Gp47) as a major component secreted into the medium. Gp47 is a non-collagenous glycoprotein with a pI of 4.6-5.5, which does not bind to either gelatin-Sepharose or heparin-Sepharose but is retained by concanavalin A-Sepharose. The Mr of this species decreases to approx. 42,000 in the presence of tunicamycin, indicating that it contains asparagine-linked oligosaccharides. A second protein of Mr 47,000 (P47) is present in the cell layer/matrix of these cultured cells. The electrophoretic mobility of P47 remains unaltered when synthesized in the presence of tunicamycin. Peptide-mapping experiments using N-chlorosuccinimide and Staphylococcus aureus V8 proteinase demonstrate that Gp47 and P47 are distinct proteins, and are not related to colligin, a membrane-bound collagen-receptor protein of similar size, or to SPARC, a major secreted product of parietal endodermal cells and sparse cultures of aortic endothelial cells.

    Original languageEnglish
    Pages (from-to)121-9
    Number of pages9
    JournalThe Biochemical journal
    Volume246
    Issue number1
    DOIs
    Publication statusPublished - 15 Aug 1987

    Keywords

    • Animals
    • Cattle
    • Cells, Cultured
    • Chromatography, Affinity
    • Electrophoresis, Polyacrylamide Gel
    • Endothelium/metabolism
    • Eye Proteins/biosynthesis
    • Isoelectric Focusing
    • Molecular Weight
    • Peptide Mapping
    • Retina/metabolism

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