The Schwann cell basal lamina acts as an organizer of peripheral nerve tissue and influences many aspects of cell behavior during development and regeneration. A principal component of the Schwann cell basal lamina is laminin-2. This study was undertaken to identify Schwann cell receptors for laminin-2. We found that among several Schwann cell integrins that can potentially interact with laminin-2, only alpha7beta1 bound to laminin-2-Sepharose. Dystroglycan, a non-integrin Schwann cell receptor for laminin-2 identified previously, was also found to bind to laminin-2-Sepharose. Antibody to the alpha7 integrin subunit partially inhibited Schwann cell adhesion to laminin-2. Small interfering RNA-mediated suppression of either alpha7 integrin or dystroglycan expression decreased adhesion and spreading of Schwann cells on laminin-2, whereas knocking down both proteins together inhibited adhesion and spreading on laminin-2 almost completely. alpha7 integrin and dystroglycan both colocalized with laminin-2 containing basal lamina tubes in differentiating neuron-Schwann cell cocultures. The alpha7beta1 integrin also coprecipitates with focal adhesion kinase in differentiating cocultures. These findings strongly suggest that alpha7beta1 integrin is a Schwann cell receptor for laminin-2 that provides transmembrane linkage between the Schwann cell basal lamina and cytoskeleton.
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