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dc.contributor.authorSanderson, R Den
dc.contributor.authorTurnbull, Jeremy Een
dc.contributor.authorGallagher, John Ten
dc.contributor.authorLander, A Den
dc.date.accessioned2010-04-09T13:29:52Z
dc.date.available2010-04-09T13:29:52Z
dc.date.issued1994-05-06
dc.identifier.citationFine structure of heparan sulfate regulates syndecan-1 function and cell behavior. 1994, 269 (18):13100-6 J. Biol. Chem.en
dc.identifier.issn0021-9258
dc.identifier.pmid8175735
dc.identifier.urihttp://hdl.handle.net/10541/96176
dc.description.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.
dc.language.isoenen
dc.subjectCultured Tumour Cellsen
dc.subject.meshAnimals
dc.subject.meshBinding Sites
dc.subject.meshCarbohydrate Conformation
dc.subject.meshCell Adhesion
dc.subject.meshCollagen
dc.subject.meshHeparitin Sulfate
dc.subject.meshHumans
dc.subject.meshMice
dc.subject.meshMultiple Myeloma
dc.subject.meshStructure-Activity Relationship
dc.subject.meshTumor Cells, Cultured
dc.titleFine structure of heparan sulfate regulates syndecan-1 function and cell behavior.en
dc.typeArticleen
dc.contributor.departmentDepartment of Pathology, University of Arkansas for Medical Sciences, Little Rock 72205.en
dc.identifier.journalThe Journal of Biological Chemistryen
html.description.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.


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