Biosynthesis of basement membrane collagen by rabbit corneal endothelium in vitro

N. A. Kefalides, J. D. Cameron, E. A. Tomichek, M. Yanoff

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The synthesis of collagen has been demonstrated in endothelial cells of Descemet's membrane isolated from rabbit cornea. Incorporation of [14C]proline and [14C]lysine into nondialyzable protein was measured in the medium and cell fraction after incubating Descemet's membrane for up to 5 hours. In the [14C]collagen synthesized by the endothelium, 15% of the hydroxy[14C]proline was present as the 3 isomer. About 98% of the hydroxy[14C]lysine in the 14C labeled protein found in the medium was glycosylated; 95% of the glycosylated hydroxy[14C]lysine was in the form of the disaccharide glucosyl galactosylhydroxy[14C]lysine. Time course experiments with [14C]proline indicated that there was a delay of about 60 min before significant amounts of [14C]collagen were secreted into the medium. The initial polypeptides of [14C]collagen synthesized by the corneal endothelium had an apparent molecular weight of 155,000. The chemical and physical properties of the [14C]collagen synthesized by rabbit corneal endothelium are consistent with those of basement membrane collagen synthesized by other cell types.

Original languageEnglish (US)
Pages (from-to)730-733
Number of pages4
JournalJournal of Biological Chemistry
Issue number3
StatePublished - 1976


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