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Distinct Effects of Recombinant Tenascin‐R Domains in Neuronal Cell Functions and Identification of the Domain Interacting with the Neuronal Recognition Molecule F3/11
Author(s) -
Xiao Zhicheng,
Taylor Joanne,
Montag Dirk,
Rougon Geneviève,
Schachner Melitta
Publication year - 1996
Publication title -
european journal of neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.346
H-Index - 206
eISSN - 1460-9568
pISSN - 0953-816X
DOI - 10.1111/j.1460-9568.1996.tb01262.x
Subject(s) - neurite , tenascin , fibronectin , extracellular matrix , microbiology and biotechnology , extracellular , glycoprotein , cell adhesion molecule , cell adhesion , biology , receptor , tenascin c , neural cell adhesion molecule , immunoglobulin superfamily , chemistry , biochemistry , cell , in vitro
We have identified distinct domains of the rat extracellular matrix glycoprotein tenascin‐R using recombinant fragments of the molecule that confer neuronal cell functions. In short‐term adhesion assays (0.5 h), cerebellar neurons adhered best to the fragment representing the fibrinogen knob (FG), but also the fibronectin type Ill (FN) repeats 1‐2 and 6‐8. FG, FN1‐2 and FN3‐5 were the most repellent fragments for neuronal cell bodies. Neurites and growth cones were strongly repelled from areas coated with fragments containing the cysteine‐rich stretch and the EGF‐like domains (EGF‐L), FN1‐2, FN3‐5 and FG. Polarization of morphology of hippocampal neurons was exclusively associated with FG, while EGF‐L prevented neurite outgrowth altogether. The binding site of the neuronal receptor for tenascin‐R, the immunoglobulin superfamily adhesion molecule F3/11, was localized to EGF‐L. The combined observations show distinct, but also overlapping functions for the different tenascin‐R domains. They further suggest the existence of multiple neuronal tenascin‐R receptors which influence the response of neurons to their extracellular matrix environment.