Abstract
The neural cell adhesion molecule (N-CAM) has been implicated in morphogenetic events during formation of the nervous system1,2. Three forms of N-CAM exist, all glycoprotein chains, of relative molecular masses 180,000 (180K), 140K and 120K (N-CAM180, N-CAM140 and N-CAM120) which are differentially expressed on neural cell types and during development3–5. The three chains are thought to carry similar if not identical amino-acid sequences on their extracellular amino-terminal domains, but differ in the length of their carboxy-terminal cytoplasmic region6–8. They occur in highly sialylated embryonic and less sialylated adult forms9,10. N-CAM180 is selectively expressed in more differentiated neural cells and may play a role in the stabilization of cell contacts5. To investigate this, we have studied in the surface membrane of a mouse neuroblastoma cell line N2A the lateral mobility of the two predominant forms of N-CAM, N-CAM180 and N-CAM140, as a function of differentiation. Here we report that as judged by fringe pattern photobleaching, the surface mobility of N-CAM140 is higher than that of N-CAM180, suggesting an association of N-CAM180 with the cytoskeleton or other stabilizing factors. We also show that brain spectrin, a membrane-cytoskeleton linker protein11, binds only to N-CAM180. The immobilization of N-CAM in differentiated N2A cells is achieved by a shift in expression from N-CAM140 to N-CAM180.
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Pollerberg, G., Schachner, M. & Davoust, J. Differentiation state-dependent surface mobilities of two forms of the neural cell adhesion molecule. Nature 324, 462–465 (1986). https://doi.org/10.1038/324462a0
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DOI: https://doi.org/10.1038/324462a0
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