Lens Glycoproteins: Biosynthesis in Cultured Epithelial Cells of Bovine Lens

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Abstract
Radioactivity from [3H]glucosamine is rapidly incorporated into cellular fractions of lens epithelial cells cultured in vitro. The incorporated isotope appears largely in glycoproteins of the cell surface that are exposed to trypsin and are released into a soluble form by proteolysis of intact cells. Glycoproteins are also secreted by cultured cells and can be recovered in the culture fluids. Sodium dodecylsulphate – polyacrylamide gel electrophoresis shows that a range of glycoproteins with apparent molecular weights from approximately 14000 to 120000 are present. The relationships of these glycoproteins to collagen and the non‐collagenous glycoproteins of lens basement membranes are discussed. A plasma membrane fraction obtained from non‐trypsinised lens epithelial cells contains one major glycoprotein of apparent molecular weight 120000. A major non‐glycosylated polypeptide of molecular weight about 38000 detectable by Bloemendal et al.(1972) in plasma membranes of differentiated lens fibre cells was not prominent in lens epithelial cell membranes. Examination of lens basement membranes extracted in various ways failed to reveal major glycoproteins of low molecular weight. Higher molecular weight glycoproteins, some of them related to collagen, were present.

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