Tenascin-C Suppresses Activation-Induced T A1A2 of the Extracellular Matrix Protein The Alternatively Spliced Domain TnFnIII

Lymphocyte Proliferation and Cytokine Tenascin-C Suppresses Activation-Induced T A1A2 of the Extracellular Matrix Protein The Alternatively Spliced Domain TnFnIII

Quantitative in situ localization of tenascin-C alternatively spliced transcripts in the avian optic tectum.

PURPOSE Tenascin-C is an extracellular matrix glycoprotein found at sites of embryonic cell motility, including the developing visual system. Numerous alternatively spliced variants of tenascin-C have been identified, and these variants have distinctive properties in vitro. The purpose of this study was to use quantitative in situ hybridization to determine the relative abundance of transcripts...

Analysis of Alternatively Spliced Domains in Multimodular Gene Products - The Extracellular Matrix Glycoprotein Tenascin C

The glia-derived extracellular matrix glycoprotein tenascin-C promotes embryonic and postnatal retina axon outgrowth via the alternatively spliced fibronectin type III domain TNfnD.

Tenascin-C (Tnc) is an astrocytic multifunctional extracellular matrix (ECM) glycoprotein that potentially promotes or inhibits neurite outgrowth. To investigate its possible functions for retinal development, explants from embryonic day 18 (E18) rat retinas were cultivated on culture substrates composed of poly-d-lysine (PDL), or PDL additionally coated with Tnc or laminin (LN)-1, which signif...

Cell surface annexin II is a high affinity receptor for the alternatively spliced segment of tenascin-C

We have investigated the binding of soluble tenascin-C (TN-C) to several cell lines using a radioligand binding assay. Specific binding was demonstrated to U-251MG human glioma cells and to a line of bovine aortic endothelial cells, but hamster fibroblasts showed no specific binding. Recombinant proteins corresponding to specific domains of TN-C were used to map the binding site(s) in TN-C. The...