Binding of contactin/F11 to the fibronectin type III domains 5 and 6 of tenascin is inhibited by heparin

FEBS Letters

Winterhalter, Kaspar H.¹  Ferber, Philippe¹  Weber, Peter¹  Fischer, René¹  Vaughan, Lloyd¹ 

[1]Laboratorium für Biochemie I, Universitätsstrasse 16, ETH-Zentrum, CH-8092 Zürich, Switzerland

关键词: Contactin/F11;    Tenascin;    Glycosaminoglycan;    Heparin;    HBS;    HEPES-buffered saline;    TNfnxx;    fibronectin type III domain xx of tenascin-C;    RU;    response units;    LMWH;    low molecular weight heparin;    CAM;    cell adhesion molecule;    GPI;    glycosylphosphatidylinositol;    CN;    contactin/F11;   

DOI  :  10.1016/0014-5793(96)00609-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown