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Versican interacts with chemokines and modulates cellular responses.
J Hirose1, H Kawashima, O Yoshie
1Department of Bioregulation, Biomedical Research Center, Osaka University Graduate School of Medicine, 2-2, Yamada-Oka, Suita 565-0871, Japan.
The Journal of Biological Chemistry
|November 18, 2000
Summary
Versican, a proteoglycan, binds chemokines through its glycosaminoglycans (GAGs). Unlike other GAGs, versican inhibits chemokine-induced cell activation, suggesting a regulatory role in immune responses.
Area of Science:
- Biochemistry
- Immunology
- Cell Biology
Background:
- Versican is a large chondroitin sulfate proteoglycan known to bind L-selectin.
- Proteoglycans play diverse roles in cellular processes and molecular interactions.
Purpose of the Study:
- To investigate the interaction between versican and chemokines.
- To determine the role of versican's glycosaminoglycans (GAGs) in chemokine binding and function.
- To examine versican's effect on chemokine-induced cellular responses.
Main Methods:
- Biochemical assays to assess binding between versican, GAGs, and chemokines.
- Enzymatic digestion of versican with chondroitinase.
- Cellular assays measuring integrin activation and calcium (Ca2+) mobilization in response to secondary lymphoid tissue chemokine (SLC).
Main Results:
- Versican binds chemokines, and this interaction is mediated by its GAG chains.
- Heparan sulfate (HS) supports SLC-induced integrin activation and Ca2+ mobilization.
- Versican and chondroitin sulfate B (CS B) inhibit these SLC-induced cellular responses in a dose-dependent manner.
Conclusions:
- Different proteoglycans have distinct functions in regulating chemokine activity.
- Versican, via its GAG chains, can negatively regulate the function of SLC, impacting immune cell migration and activation.