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Distinct effects of recombinant tenascin‐C domains on neuronal cell adhesion, growth cone guidance, and neuronal polarity
Author(s) -
Dörries U.,
Taylor J.,
Xiao Z.,
Lochter A.,
Montag D.,
Schachner M.
Publication year - 1996
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/(sici)1097-4547(19960215)43:4<420::aid-jnr4>3.0.co;2-h
Subject(s) - growth cone , fibronectin , tenascin , neurite , microbiology and biotechnology , biology , cell adhesion , extracellular matrix , cell adhesion molecule , neural cell adhesion molecule , adhesion , tenascin c , axon , cell , chemistry , genetics , in vitro , organic chemistry
Using a set of recombinantly expressed proteins, distinct domains of the mouse extracellular matrix glycoprotein tenascin‐C, hereafter called tenascin, have been identified to confer adhesion, anti‐adhesion, and changes in morphology of neuronal cells. In short‐term adhesion assays (1 hr), cerebellar and hippocampal neurons adhered to several domains, encompassing the fibronectin type III‐like (FN III) repeats 1–2 and 6–8, as well as to the alternatively spliced FN III repeats and to tenascin itself. Although no short‐term adhesion to the EGF repeats containing fragment could be detected under the conditions used, it was anti‐adhesive for neuronal cell bodies and repellent for growth cone advance and neuritogenesis. FN III repeats 3–5 were repellent only for growth cones but not for neuronal cell bodies. Neurite outgrowth promoting activities at early stages and induction of a polarized neuronal morphology at later stages of differentiation were associated with the EGF repeats and the FN III repeats 6–8. These observations suggest differential effects of particular domains of the tenascin molecule on distinct cellular compartments, i.e., cell body, axon and dendrite, and existence of multiple neuronal receptors with distinct intracellular signaling features. © 1996 Wiley‐Liss, Inc.