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| Item Type: | Article |
|---|---|
| Title: | Characterization of functional domains of the tenascin-R (restrictin) polypeptide: cell attachment site, binding with F11 and enhancement of F11 mediated neurite outgrowth by tenascin-R |
| Creators Name: | Noerenberg, U., Hubert, M., Bruemmendorf, T., Tarnok, A. and Rathjen, F.G. |
| Abstract: | The extracellular matrix glycoprotein tenascin-R (TN-R) is a multidomain protein implicated in neural cell adhesion. To analyze the structure-function relationship of the different domains of TN-R, several recombinant TN-R fragments were expressed in bacterial cells. Two distinct binding regions were localized on the TN-R polypeptide: a region binding the axon-associated immunoglobulin (Ig)-like F11 protein and a cell attachment site. The binding region of the glycosylphosphatidylinositol (GPI)-anchored F11 was allocated to the second and third fibronectin type III (FNIII)-like domain within TN-R. By using a mutant polypeptide of F11 containing only Ig-like domains, a direct interaction between the Ig-like domains of F11 and FNIII-like domains 2-3 of TN-R was demonstrated. The interaction of TN-R with F11 in in vitro cultures enhanced F11-mediated neurite outgrowth, suggesting that the combined action of F11 and TN-R might be of regulatory influence on axon extension. A cell attachment region was identified in the FNIII-like domain eight of TN-R by domain-specific antibodies and fusion constructs. This site is distinct from the F11 binding site within TN-R. |
| Keywords: | Binding Sites, Cell Adhesion, Cell Line, Contactins, Cultured Cells, Extracellular Matrix Proteins, Neural Cell Adhesion Molecules, Neurites, Neuronal Cell Adhesion Molecules, Recombinant Fusion Proteins, Retina, Tenascin, Transfection, Animals, Chickens |
| Source: | Journal of Cell Biology |
| ISSN: | 0021-9525 |
| Publisher: | Rockefeller University Press |
| Volume: | 130 |
| Number: | 2 |
| Page Range: | 473-484 |
| Date: | July 1995 |
| Additional Information: | Copyright (c) 1995 by The Rockefeller University Press |
| Official Publication: | http://www.jcb.org/cgi/content/abstract/130/2/473 |
| PubMed: | View item in PubMed |
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