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Fine structure of heparan sulfate regulates syndecan-1 function and cell behavior
Two 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 MP...
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Published in: | The Journal of biological chemistry 1994-05, Vol.269 (18), p.13100-13106 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Two 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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ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)36804-7 |