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STRUCTURAL AND FUNCTIONAL CHARACTERIZATION OF TENASCIN‐R (RESTRICTIN), AN EXTRACELLULAR MATRIX GLYCOPROTEIN OF GLIAL CELLS AND NEURONS
Author(s) -
Nörenberg Ursel,
Hubert Michael,
Rathjen Fritz G.
Publication year - 1996
Publication title -
international journal of developmental neuroscience
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.761
H-Index - 88
eISSN - 1873-474X
pISSN - 0736-5748
DOI - 10.1016/0736-5748(96)00009-3
Subject(s) - tenascin , fibronectin , extracellular matrix , neurite , tenascin c , glycoprotein , extracellular , microbiology and biotechnology , biology , chemistry , biochemistry , in vitro
Tenascin‐R (TN‐R) is an extracellular matrix protein associated with the surface of neurons and glial cells. Immunohistological studies reveal that TN‐R shows a restricted expression pattern in the developing nervous system. TN‐R is the smallest member of the tenascin family and is composed of four structural motifs: a cysteine‐rich segment at the N‐terminus is followed by 4.5 EGF‐like repeats. This region is followed by 9 consecutive fibronectin type III (FNIII)‐like domains and at the C‐terminus TN‐R is related to the β‐ and γ‐ chains of fibrinogen. TN‐R forms oligomeric structures as revealed by rotary shadowing electron microscopy of immunoaffinity‐purified TN‐R. TN‐R interacts with the axon‐associated F11 protein which results in an enhancement of F11 mediated neurite extension in in vitro assays. In short‐term adhesion assays it was found that neural but not fibroblastic cells attach effectively on immobilized TN‐R. The cell attachment site within TN‐R was allocated to FNIII domain 8 while the site interacting with the F11 protein could be mapped to FNIII domain 2–3.