title: Distinct effects of recombinant tenascin-R domains in neuronal cell functions and identification of the domain interacting with the neuronal recognition molecule F3/11.
abstract: 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 III (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.
authors.affiliation: Department of Neurobiology, Swiss Federal Institute of Technology, Hönggerberg, Zurich, Switerland.
authors.forename: Z C
authors.initials: ZC
authors.lastname: Xiao
authors.forename: J
authors.initials: J
authors.lastname: Taylor
authors.forename: D
authors.initials: D
authors.lastname: Montag
authors.forename: G
authors.initials: G
authors.lastname: Rougon
authors.forename: M
authors.initials: M
authors.lastname: Schachner
mesh_terms: D000818:Animals; D016466:CHO Cells / Q000187:drug effects; D002448:Cell Adhesion / Q000187:drug effects; D015816:Cell Adhesion Molecules, Neuronal / Q000502:physiology*; D016764:Cell Polarity; D058966:Contactins; D006224:Cricetinae; D004815:Epidermal Growth Factor / Q000737:chemistry / Q000378:metabolism; D005982:Glutathione Transferase / Q000494:pharmacology; D051379:Mice; D008813:Mice, Inbred ICR; D019006:Neural Cell Adhesion Molecules / Q000502:physiology*; D016501:Neurites / Q000187:drug effects / Q000502:physiology; D009474:Neurons / Q000187:drug effects* / Q000502:physiology*; D010446:Peptide Fragments / Q000494:pharmacology*; D051381:Rats; D011956:Receptors, Cell Surface / Q000502:physiology; D011993:Recombinant Fusion Proteins / Q000494:pharmacology; D011994:Recombinant Proteins; D019063:Tenascin / Q000737:chemistry / Q000378:metabolism / Q000494:pharmacology*; D014162:Transfection
chemical_list: D015816:Cell Adhesion Molecules, Neuronal; D058966:Contactins; D019006:Neural Cell Adhesion Molecules; D010446:Peptide Fragments; D011956:Receptors, Cell Surface; D011993:Recombinant Fusion Proteins; D011994:Recombinant Proteins; D019063:Tenascin; C074638:tenascin R; D004815:Epidermal Growth Factor; D005982:Glutathione Transferase