Biosynthesis of versican by rat dental pulp cells in culture

The biosynthesis of proteoglycans by these cultured pulp cells was investigated by metabolic labelling, using [35S]sulphate, [3H]glucosamine and [3H]leucine as precursors. Versican-like large proteoglycan, decorin- and biglycan-like small proteoglycans and a small amount of sulphated protein were released into the culture medium. Heparan sulphate species were also identified in cell-layer extracts. Versican-like proteoglycan had an average molecular mass of approximately 800 kDa. The molecular mass of chondroihnase ABC-digested core protein exhibited heterogeneity, ranging from 250 to 400 kDa, and the glycosaminoglycan chains had an average molecular mass of approximately 42 kDa. These results indicate the presence of 10–13 glycosaminoglycan chains per core protein, consistent with the characteristics of versican. This glycosaminoglycan chain contained approximately 63% 4-sulphated disaccharides.