Structural and functional characterization of tenascin-R (restrictin), an extracellular matrix glycoprotein of glial cells and neurons.
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 beta- and gamma- 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.
Nörenberg
U
U
Max-Delbrück-Centrum für Molekulare Medizin, Berlin, Germany.
Hubert
M
M
Rathjen
F G
FG
D000818:Animals; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D002450:Cell Communication / Q000502:physiology; D002645:Chickens / Q000502:physiology*; D002845:Chromatography; D003001:Cloning, Molecular; D004247:DNA / Q000096:biosynthesis; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000502:physiology*; D005434:Flow Cytometry; D006493:Heparin / Q000737:chemistry; D007150:Immunohistochemistry; D008854:Microscopy, Electron; D016501:Neurites / Q000502:physiology / Q000648:ultrastructure; D009457:Neuroglia / Q000737:chemistry / Q000378:metabolism*; D009474:Neurons / Q000737:chemistry / Q000378:metabolism* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000096:biosynthesis; D012685:Sepharose / Q000737:chemistry; D019063:Tenascin / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*
D015815:Cell Adhesion Molecules; D016326:Extracellular Matrix Proteins; D011994:Recombinant Proteins; D019063:Tenascin; C074638:tenascin R; D006493:Heparin; D004247:DNA; D012685:Sepharose