Formation of heparan sulfate or chondroitin/dermatan sulfate on recombinant domain I of mouse perlecan expressed in Chinese hamster ovary cells.

Recombinant domain I of mouse perlecan was expressed in Chinese hamster ovary (CHO K1) cells and affinity purified on Ni-agarose. Gel chromatography followed by characterization of glycosaminoglycans by the use of glycosaminoglycan lyases showed that the recombinant proteoglycans contained, on average, three glycosaminoglycan chains of heparan sulfate or chondroitin/dermatan sulfate of approximately 12 kDa median size. These data demonstrate that domain I has functional sites for attachment of glycosaminoglycans and indicate that the glycosaminoglycan chains of native perlecan are grouped at its N-terminal end. This, in turn, suggests that the likely function of domain I in perlecan would be to provide for the addition of glycosaminoglycan chains to the core protein.