FORMATION OF HEPARAN-SULFATE OR CHONDROITIN XDERMATAN 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. (C) 1995 Academic Press, Inc.