Single cell suspensions of early postnatal mouse cerebellum adhere to substrate-bound culture supernatants of the teratocarcinoma cell line PF-HR9 and can be inhibited to adhere by antibodies to the neural cell adhesion molecules L1 and N-CAM. Adhesion can also be inhibited by the glycosaminoglycans heparin and heparan sulfate, and less by chondroitin sulfate or hyaluronic acid. Heparinase treatment of cells, but not of HR9 substrate, reduces adhesion. Adhesion does not appear to be mediated by laminin, a constituent of HR9 extracellular matrix, since L1 and N-CAM antibodies do not interfere with cell adhesion on EHS sarcoma laminin as substrate and since antibodies to EHS sarcoma laminin partially inhibit adhesion to HR9 extracellular matrix which contains laminin. Of the other extracellular matrix constituents analysed in HR9 culture supernatants (collagen type IV, a heparan sulfate proteoglycan and fibronectin) none could be shown to promote adhesion, when coated as substrate, suggesting that yet unidentified compounds are responsible for L1- or N-CAM-mediated cell adhesion. These experiments show for the first time that extracellular matrix constituents can act as binding partners for the neural cell adhesion molecules L1 and N-CAM.
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