HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zacharias, U. Articles by Rathjen, F. G. Search for Related Content PubMed PubMed Citation Articles by Zacharias, U. Articles by Rathjen, F. G. Social Bookmarking                      What's this?

J Biol Chem, Vol. 274, Issue 34, 24357-24365, August 20, 1999

Functional Interactions of the Immunoglobulin Superfamily Member F11 Are Differentially Regulated by the Extracellular Matrix Proteins Tenascin-R and Tenascin-C

From the Max-Delbrück-Centrum für Molekulare Medizin, Robert-Rössle-Str. 10, D-13122 Berlin, Germany

The axon-associated protein F11 is a GPI-anchored member of the immunoglobulin superfamily that promotes axon outgrowth and that shows a complex binding pattern toward multiple cell surface and extracellular matrix proteins including tenascin-R and tenascin-C. In this study, we demonstrate that tenascin-R and tenascin-C differentially modulate cell adhesion and neurite outgrowth of tectal cells on F11. While soluble tenascin-R increases the number of attached cells and the percentage of cells with neurites on immobilized F11, tenascin-C stimulates cell attachment to a similar extent but decreases neurite outgrowth. The cellular receptor interacting with F11 has been previously identified as NrCAM; however, in the presence of tenascin-R or tenascin-C cell attachment and neurite extension are independent of NrCAM. Antibody perturbation experiments indicate that ₁ integrins instead of NrCAM function as receptor for neurite outgrowth of tectal cells on an F11·TN-R complex. Cellular binding assays support the possibility that the interaction of F11 to NrCAM is blocked in the presence of tenascin-R and tenascin-C. Furthermore, a sandwich binding assay demonstrates that tenascin-R and tenascin-C are able to form larger molecular complexes and to link F11 polypeptides by forming a molecular bridge.

These results suggest that the molecular interactions of F11 might be regulated by the presence of tenascin-R and tenascin-C.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				U. Zacharias and U. Rauch Competition and cooperation between tenascin-R, lecticans and contactin 1 regulate neurite growth and morphology. J. Cell Sci., August 15, 2006; 119(Pt 16): 3456 - 3466. [Abstract] [Full Text] [PDF]

				M. Conacci-Sorrell, A. Kaplan, S. Raveh, N. Gavert, T. Sakurai, and A. Ben-Ze'ev The Shed Ectodomain of Nr-CAM Stimulates Cell Proliferation and Motility, and Confers Cell Transformation Cancer Res., December 15, 2005; 65(24): 11605 - 11612. [Abstract] [Full Text] [PDF]

				J. Falk, O. Thoumine, C. Dequidt, D. Choquet, and C. Faivre-Sarrailh NrCAM Coupling to the Cytoskeleton Depends on Multiple Protein Domains and Partitioning into Lipid Rafts Mol. Biol. Cell, October 1, 2004; 15(10): 4695 - 4709. [Abstract] [Full Text] [PDF]

				M. I. More, F.-P. Kirsch, and F. G. Rathjen Targeted ablation of NrCAM or ankyrin-B results in disorganized lens fibers leading to cataract formation J. Cell Biol., July 9, 2001; 154(1): 187 - 196. [Abstract] [Full Text] [PDF]

				J. Trotter, C. Klein, and E.-M. Kramer GPI-Anchored Proteins and Glycosphingolipid-Rich Rafts: Platforms for Adhesion and Signaling Neuroscientist, August 1, 2000; 6(4): 271 - 284. [Abstract] [PDF]

				S. Schumacher, M. Jung, U. Norenberg, A. Dorner, R. Chiquet-Ehrismann, C. A. O. Stuermer, and F. G. Rathjen CALEB Binds via Its Acidic Stretch to the Fibrinogen-like Domain of Tenascin-C or Tenascin-R and Its Expression Is Dynamically Regulated after Optic Nerve Lesion J. Biol. Chem., March 2, 2001; 276(10): 7337 - 7345. [Abstract] [Full Text] [PDF]