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PMID: 7615642 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

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.

The Journal of cell biology ·Vol. 130 ·No. 2 ·1995-07-00 ·Pages 473-84

Nörenberg U, Hubert M, Brümmendorf T, Tárnok A, Rathjen FG

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.

MeSH Terms
Animals Binding Sites Cell Adhesion Cell Adhesion Molecules, Neuronal/chemistry,metabolism Cell Line Cells, Cultured Chick Embryo Contactins Extracellular Matrix Proteins/chemistry,metabolism Neural Cell Adhesion Molecules Neurites/physiology,ultrastructure Recombinant Fusion Proteins/metabolism Retina/cytology,embryology Tenascin Transfection
Chemicals
Cell Adhesion Molecules, Neuronal Contactins Extracellular Matrix Proteins Neural Cell Adhesion Molecules Recombinant Fusion Proteins Tenascin tenascin R
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Nörenberg U
Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
Hubert M
Brümmendorf T
Tárnok A
Rathjen F G
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
DOI
10.1083/jcb.130.2.473
Published
1995-07-00
Pages
473-84
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2199939
Subset
IM
External Links
PubMed source DOI: 10.1083/jcb.130.2.473 PMC Full Text View journal details
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