Abstract
The structural basis for the interaction between tenascin-C and the neuronal cell adhesion molecule, contactin/F11, was investigated using plasmon surface resonance technology. The binding site on tenascin-C for contactin/F11 is shown to span the two fibronectin type III homology domains 5 and 6. Either domain alone is insufficient for binding. Heparin, heparan sulfate and dermatan sulfate inhibit this interaction through binding to a conserved heparin-binding site on domain 5. In contrast, chondroitin sulfates A and C have no such effect.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Animals
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Antibodies, Monoclonal
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Binding Sites
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Cell Adhesion Molecules, Neuronal*
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Chick Embryo
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Contactins
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Dermatan Sulfate / pharmacology
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Extracellular Matrix / metabolism
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Fibronectins / chemistry
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Fibronectins / metabolism*
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Glycosaminoglycans / pharmacology
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Heparin / pharmacology*
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Heparitin Sulfate / pharmacology
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Membrane Glycoproteins / metabolism
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Nerve Tissue Proteins / metabolism*
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Neural Cell Adhesion Molecules / metabolism*
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Protein Binding / drug effects
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Recombinant Fusion Proteins / metabolism
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Tenascin / chemistry
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Tenascin / metabolism*
Substances
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Antibodies, Monoclonal
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Cell Adhesion Molecules, Neuronal
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Contactins
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Fibronectins
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Glycosaminoglycans
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Membrane Glycoproteins
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Nerve Tissue Proteins
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Neural Cell Adhesion Molecules
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Recombinant Fusion Proteins
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Tenascin
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Dermatan Sulfate
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Heparin
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Heparitin Sulfate