| First Author | Tapanadechopone P | Year | 1999 |
| Journal | Biochem Biophys Res Commun | Volume | 265 |
| Issue | 3 | Pages | 680-90 |
| PubMed ID | 10600481 | Mgi Jnum | J:58735 |
| Mgi Id | MGI:1349538 | Doi | 10.1006/bbrc.1999.1714 |
| Citation | Tapanadechopone P, et al. (1999) Localization of glycosaminoglycan substitution sites on domain V of mouse perlecan. Biochem Biophys Res Commun 265(3):680-90 |
| abstractText | Perlecan, the predominant basement membrane proteoglycan, has previously been shown to contain glycosaminoglycans attached at serine residues, numbers 65, 71, and 76, in domain I. However, the C-terminal domains IV and V of this molecule may also be substituted with glycosaminoglycan chains, but the exact substitution sites were not identified. The amino acid sequence of mouse perlecan reveals many ser-gly sequences in these domains that are possible sites for glycosaminoglycan substitution. We expressed recombinant domain IV and/or V of mouse perlecan in COS-7 cells and analyzed glycosaminoglycan substitution. Both heparan sulfate and chondroitin sulfate chains could be detected on recombinant domain V. One site, ser-gly-glu (serine residue 3593), toward the C-terminal region of domain V is a substitution site for heparan sulfate. When this sequence was absent, chondroitin/dermatan sulfate substitution was deleted, and the likely site for this galactosaminoglycan substitution was ser-gly-ala-gly (serine residue 3250) on domain V. Copyright 1999 Academic Press. |
