DISTINCT EFFECTS OF RECOMBINANT TENASCIN-C DOMAINS ON NEURONAL CELL-ADHESION, GROWTH CONE GUIDANCE, AND NEURONAL POLARITY

Using a set of recombinantly expressed proteins, distinct domains of t he mouse extracellular matrix glycoprotein tenascin-C, hereafter calle d tenascin, have been identified to confer adhesion, anti-adhesion, an d changes in morphology of neuronal cells, In shortterm adhesion assay s (1 hr), cerebellar and hippocampal neurons adhered to several domain s, 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 te nascin itself, Although no shortterm adhesion to the EGF repeats conta ining fragment could be detected under the conditions used, it was ant i-adhesive for neuronal cell bodies and repellent for growth cone adva nce and neuritogenesis, FN III repeats 3-5 were repellent only for gro wth cones but not for neuronal cell bodies, Neurite outgrowth promotin g activities at early stages and induction of a polarized neuronal mor phology at later stages of differentiation were associated with the EG F repeats and the FN III repeats 6-8. These observations suggest diffe rential effects of particular domains of the tenascin molecule on dist inct cellular compartments, i.e., cell body, axon and dendrite, and ex istence of multiple neuronal receptors with distinct intracellular sig naling features. (C) 1996 Wiley-Liss, Inc.