JBC, Vol. 251, Issue 3, 730-733, Feb, 1976
Biosynthesis of basement membrane collagen by rabbit corneal endothelium in vitro
N. A. Kefalides, J. D. Cameron,, E. A. Tomichek and M. Yanoff
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-galactosyl-hydroxy[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.
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