Fine structure of heparan sulfate regulates syndecan-1 function and cell behavior.
AffiliationDepartment of Pathology, University of Arkansas for Medical Sciences, Little Rock 72205.
MetadataShow full item record
AbstractTwo myeloma cell lines, MPC-11 and P3X63Ag8.653 (P3), have almost identical amounts of syndecan-1 at their cell surface. The syndecan-1 molecules from both lines are similar in size, have indistinguishable core proteins, and have similarly sized heparan sulfate chains. Nevertheless, syndecan-1 on MPC-11 mediates cell adhesion to type I collagen, whereas P3 cells do not bind collagen. Affinity co-electrophoresis reveals that intact syndecan-1 isolated from P3 cells binds collagen poorly and that syndecan-1 heparan sulfate isolated from MPC-11 has a 20-fold higher affinity for collagen than syndecan-1 heparan sulfate from P3. Analysis of disaccharide composition and oligosaccharide mapping also reveals differences between MPC-11 and P3 heparan sulfate. Most notably, the level of N-sulfation and 2-O-sulfation is higher, and 6-O-sulfation lower, in syndecan-1 heparan sulfate from MPC-11 than from P3. Interestingly, levels of total sulfation of syndecan-1 heparan sulfate from MPC-11 and P3 are similar (75.6 and 72.6 sulfates/100 disaccharides, respectively), indicating that the difference in their affinity for collagen is not due to a difference in net charge. These data indicate that the fine structure of heparan sulfate can differ on identical proteoglycan core proteins, and these differences can control fundamental cellular properties such as cell-matrix adhesion.
CitationFine structure of heparan sulfate regulates syndecan-1 function and cell behavior. 1994, 269 (18):13100-6 J. Biol. Chem.
JournalThe Journal of Biological Chemistry
- Cell surface syndecan-1 on distinct cell types differs in fine structure and ligand binding of its heparan sulfate chains.
- Authors: Kato M, Wang H, Bernfield M, Gallagher JT, Turnbull JE
- Issue date: 1994 Jul 22
- Adhesion of B lymphoid (MPC-11) cells to type I collagen is mediated by integral membrane proteoglycan, syndecan.
- Authors: Sanderson RD, Sneed TB, Young LA, Sullivan GL, Lander AD
- Issue date: 1992 Jun 15
- Participation of syndecan 2 in the induction of stress fiber formation in cooperation with integrin alpha5beta1: structural characteristics of heparan sulfate chains with avidity to COOH-terminal heparin-binding domain of fibronectin.
- Authors: Kusano Y, Oguri K, Nagayasu Y, Munesue S, Ishihara M, Saiki I, Yonekura H, Yamamoto H, Okayama M
- Issue date: 2000 May 1
- Syndecan-1 and -4 synthesized simultaneously by mouse mammary gland epithelial cells bear heparan sulfate chains that are apparently structurally indistinguishable.
- Authors: Zako M, Dong J, Goldberger O, Bernfield M, Gallagher JT, Deakin JA
- Issue date: 2003 Apr 11
- Heparan sulfate chains from glypican and syndecans bind the Hep II domain of fibronectin similarly despite minor structural differences.
- Authors: Tumova S, Woods A, Couchman JR
- Issue date: 2000 Mar 31