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 [(35)S]sulphate, [(3)H]glucosamine and [(3)H]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 800kDa. The molecular mass of chondroihnase ABC-digested core protein exhibited heterogeneity, ranging from 250 to 400kDa, and the glycosaminoglycan chains had an average molecular mass of approximately 42kDa. 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.