Tenascin‐R is expressed by Schwann cells in the peripheral nervous system
- 22 March 2001
- journal article
- research article
- Published by Wiley in Journal of Neuroscience Research
- Vol. 64 (1) , 70-78
- https://doi.org/10.1002/jnr.1055
Abstract
The extracellular matrix glycoprotein tenascin‐R (TN‐R) has been implicated in a variety of cell‐matrix interactions involved in the molecular control of axon guidance and neural cell migration during development and regeneration of the central nervous system (CNS). Whereas TN‐R is amply expressed in the early postnatal and adult mammalian CNS, the protein has so far not been detected in different compartments of the peripheral nervous system (PNS). Here we provide first evidence that TN‐R (predominantly TN‐R 160 isoform) is transiently expressed in the sciatic nerve of late embryonic (E14–18) and neonatal mice, while at later developmental stages, both protein and mRNA are downregulated. In vitro, TN‐R protein was found to be expressed by both undifferentiated and neuronally differentiated PC12 cells and by L1‐positive Schwann cells (SC), but not by other neural and non‐neural cell types in cell cultures derived from embryonic (E17/18) hindlimbs and neonatal sciatic nerves. In the developing PNS, TN‐R expression correlated with axon growth and SC migration during the period of skeletal muscle innervation. Based on different in vitro approaches, we found that the substrate‐bound glycoprotein selectively inhibits the fibronectin‐dependent: (1) neurite outgrowth from dorsal root ganglion neurons (strongly expressing α5β1 integrin and the disialoganglioside GD3) by a ganglioside‐sensitive signaling mechanism; and (2) migration of primary myoblasts and other non‐neuronal cells in a ganglioside‐independent manner. Our findings suggest the functional role of TN‐R in PNS pattern formation during distinct stages of axon pathfinding and skeletal muscle innervation. J. Neurosci. Res. 64:70–78, 2001.Keywords
This publication has 21 references indexed in Scilit:
- Involvement of chondroitin sulfates on brain-derived tenascin-R in carbohydrate-dependent interactions with fibronectin and tenascin-CBrain Research, 2000
- The yin and yang of tenascin-R in CNS development and pathologyProgress in Neurobiology, 2000
- Tenascin-C inhibits 1 integrin-dependent cell adhesion and neurite outgrowth on fibronectin by a disialoganglioside-mediated signaling mechanismGlycobiology, 1999
- Expression of the immunoglobulin superfamily cell adhesion molecule F3 by oligodendrocyte-lineage cellsGlia, 1997
- The extracellular matrix molecule tenascin-C: Expression in vivo and functional characterization in vitroProgress in Neurobiology, 1996
- The axonal recognition molecule F11 is a multifunctional protein: Specific domains mediate interactions with Ng-CAM and restrictinNeuron, 1993
- The F3/11 cell adhesion molecule mediates the repulsion of neurons by the extracellular matrix glycoprotein J1-160/180Neuron, 1993
- Proliferation and differentiation of O4+ oligodendrocytes in postnatal rat cerebellum: Analysis in unfixed tissue slices using anti‐glycolipid antibodiesJournal of Neuroscience Research, 1992
- Divalent Cations Modulate the Inhibitory Substrate Properties of Murine Glia‐derived J1‐160 and J1‐180 Extracellular Matrix Glycoproteins for Neuronal AdhesionEuropean Journal of Neuroscience, 1991
- J1-160 and J1-180 are oligodendrocyte-secreted nonpermissive substrates for cell adhesion.The Journal of cell biology, 1989