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 hamste r ovary (CHO K1) cells and affinity purified on Ni-agarose, Gel chroma tography followed by characterization of glycosaminoglycans by the use of glycosaminoglycan lyases showed that the recombinant proteoglycans contained, on average, three glycosaminoglycan chains of heparan sulf ate or chondroitin/dermatan sulfate of approximately 12 kDa median siz e. These data demonstrate that domain I has functional sites for attac hment of glycosaminoglycans and indicate that the glycosaminoglycan ch ains of native perlecan are grouped at its N-terminal end. This, in tu rn, suggests that the likely function of domain I in perlecan would be to provide for the addition of glycosaminoglycan chains to the core p rotein. (C) 1995 Academic Press, Inc.