Previous studies have shown that sulphated proteoglycans are integral components of basement membranes. We have used mouse parietal yolk sac cells as a model system for our studies. These cells produce several basement membrane components, including a heparan sulphate proteoglycan and a chondroitin sulphate proteoglycan. The structure of the heparan sulphate proteoglycan has been described previously. The chondroitin sulphate proteoglycan has an Mr of 200 000-300 000 and contains 10-20 chondroitin sulphate chains (Mr = 14 000-16 000), attached to a core protein that on polyacrylamide gel electrophoresis appears as a doublet (with Mr = 34 000 and 27 000). Further structural analysis suggests that the majority of the polysaccharide chains are clustered around one segment of the core protein. The polysaccharide chains carry sulphate residues predominantly attached to C-4 of the galactosamine unit. More than 60% of the uronic acid residues are of the glucuronic configuration, the rest being iduronic acid. The parietal yolk sac cells secrete about equal amounts of the two proteoglycans into the culture medium, whereas heparan sulphate proteoglycan is the predominant proteoglycan found in the extracellular matrix of these cells. This proteoglycan appears to be anchored in the matrix by interactions involving the core protein rather than the polysaccharide chains.
|Original language||English (US)|
|Number of pages||16|
|Journal||Ciba Foundation symposium|
|State||Published - 1984|
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