title: Glial cell interactions with tenascin-C: adhesion and repulsion to different tenascin-C domains is cell type related.
abstract: The multimodular glycoprotein tenascin-C is transiently expressed, predominantly by glial cells, during the development of the central and peripheral nervous systems. This extracellular matrix glycoprotein is involved in the control of cell adhesion, neuron migration and neurite outgrowth. Distinct functional properties for neuronal cell types have been attributed to separate tenascin-C domains using antibody perturbation studies and in vitro experiments on tenascin-C fragments. In order to study potential roles of tenascin-C for glial cell biology, a library of recombinant tenascin-C domains was used in a bioassay in vitro. Embryonic day 14 astrocytes, various astroglial-derived cell lines (C6, A7 and Neu7) and oligodendroglial-derived cell types (Oli-neu and G26-20) were examined in an adhesion assay and compared to the neuroblastoma cell line N2A. A binding site for most cell types, except for A7 and N2A, could be assigned to the first three fibronectin type III domains. Repulsive properties could be mapped to three different sites the epidermal growth factor-like repeats, fibronectin type III repeats 4 and 5 and to the alternatively spliced region of the molecule. The responses to these repulsive sites varied according to the cell type. These data are consistent with the interpretation that different cell types express distinct sets of tenascin-C receptors which might regulate cellular responses via distinct second messenger pathways.
authors.affiliation: Department of Neurobiology, University of Heidelberg, Germany.
authors.forename: A
authors.initials: A
authors.lastname: Scholze
authors.forename: B
authors.initials: B
authors.lastname: Götz
authors.forename: A
authors.initials: A
authors.lastname: Faissner
mesh_terms: D000818:Animals; D002448:Cell Adhesion / Q000502:physiology; D002478:Cells, Cultured; D051379:Mice; D009447:Neuroblastoma / Q000378:metabolism; D009457:Neuroglia / Q000378:metabolism / Q000502:physiology*; D009836:Oligodendroglia / Q000502:physiology; D011994:Recombinant Proteins / Q000737:chemistry / Q000378:metabolism; D019063:Tenascin / Q000737:chemistry / Q000502:physiology*
chemical_list: D011994:Recombinant Proteins; D019063:Tenascin