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Journal of Cell Science, Vol 111, Issue 8 1095-1104, Copyright © 1998 by Company of Biologists
JOURNAL ARTICLES |
GR Phillips, LA Krushel and KL Crossin
Department of Neurobiology, Scripps Research Institute, La Jolla, CA 92037, USA.
Tenascin (TN) is an extracellular matrix protein found in areas of cell migration during development and expressed at high levels in migratory tumor cells. TN was previously shown to support the attachment and migration of glioma cells in culture. To determine the domains responsible for glioma migration and attachment, we produced recombinant fusion proteins that collectively span the majority of the molecule including its epidermal growth factor-like repeats, fibronectin type III repeats and fibrinogen domain. These domains were tested for their ability to support migration of C6 glioma cells in an aggregate migration assay. A recombinant fusion protein including fibronectin type III (FNIII) repeats 2-6 (TNfn2-6) was the only fragment found to promote migration of C6 glioma cells at levels similar to that promoted by intact TN. Evaluation of smaller segments and individual FNIII repeats revealed that TNfn3 promoted migration and attachment of glioma cells and TNfn6 promoted migration but not attachment. While TNfn3 and TNfn6 promoted migration individually, the presence of both TNfn3 and TNfn6 was required for migration on segments of the FNIII region that included TNfn5. TNfn5 inhibited migration in a dose dependent manner when mixed with TNfn3 and also promoted strong attachment and spreading of C6 glioma cells. TNfn3 and TNfn6 promote cell migration and may function cooperatively to overcome the inhibitory activity of TNfn5. Additional cell attachment studies suggested that both beta1 integrins and heparin may differentially influence the attachment of glioma cells to TN fragments. Together, these findings show that C6 glioma cells integrate their response upon binding to at least three domains within TN.
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 M. D. Puente Navazo, D. Valmori, and C. Ruegg The Alternatively Spliced Domain TnFnIII A1A2 of the Extracellular Matrix Protein Tenascin-C Suppresses Activation-Induced T Lymphocyte Proliferation and Cytokine Production J. Immunol., December 1, 2001; 167(11): 6431 - 6440. [Abstract] [Full Text] [PDF]
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 L. Häkkinen, H. C. Hildebrand, A. Berndt, H. Kosmehl, and H. Larjava Immunolocalization of Tenascin-C, {alpha}9 Integrin Subunit, and {alpha}v{beta}6 Integrin During Wound Healing in Human Oral Mucosa J. Histochem. Cytochem., July 1, 2000; 48(7): 985 - 998. [Abstract] [Full Text]
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