Neuronal cell adhesion molecule contactin/F11 binds to tenascin via its immunoglobulin-like domains.

• DOI: 10.1083/jcb.119.1.203
• Publication Date: 2004-05-15T00:22:22Z
• Authors: A H Zisch; L D'Alessandri; B Ranscht; R Falchetto; K H Winterhalter; L Vaughan
• Keywords: Tenascin; Tenascin C; Immunoglobulin superfamily; Immunoglobulin domain

Adhesive interactions between neurons and extracellular matrix (ECM) play a key role in neuronal pattern formation. The prominent played by the protein tenascin/cytotactin development of nervous system, tied to its abundance, led us speculate that brain may contain yet unidentified tenascin receptors. Here we show cell adhesion molecule contactin/F11, member immunoglobulin(Ig)-superfamily, is surface ligand for system. Through affinity chromatography membrane glycoproteins from chick on tenascin-Sepharose, isolated major 135 kD which identified as contactin/F11 NH2-terminal sequencing. binding specificity was demonstrated solid-phase assays. Binding immunopurified 125I-labeled immobilized completely inhibited addition soluble or but not fibronectin. When fractionated isoforms were used substrates, bound preferentially 190-kD isoform. This isoform differs having no alternatively spliced fibronectin type III domains. Our results imply introduction these additional domains some way disrupts site tenascin. To localize proteolytic fragments generated characterized smallest fragment binds 45 also begins with sequence. implies through within first three Ig-domains.