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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

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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. and Hubert, M. and Bruemmendorf, T. and 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 (U.S.A.)
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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