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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Mouse Na+/K+-ATPase beta1-subunit has a K+-dependent cell adhesion activity for beta-GlcNAc-terminating glycans.

A 48-kDa beta-N-acetylglucosamine (GlcNAc)-binding protein was isolated from mouse brain by GlcNAc-agarose column chromatography. The N-terminal amino acid residues showed the protein to be a mouse Na(+)/K(+)-ATPase beta1-subunit. When the recombinant FLAG-beta1-subunit expressed in Sf-9 cells was applied to a GlcNAc-agarose column, only the glycosylated 38- and 40-kDa proteins bound to the column. In the absence of KCl, little of the proteins bound to a GlcNAc-agarose column, but the 38- and 40-kDa proteins bound in the presence of KCl at concentrations above 1 mM. Immunohistochemical study showed that the beta1-subunit and GlcNAc-terminating oligosaccharides are at the cell contact sites. Inclusion of anti-beta1-subunit antibody or chitobiose in cell aggregation assays using mouse neural cells resulted in inhibition of cell aggregation. These results indicate that the Na(+)/K(+)-ATPase beta1-subunit is a potassium-dependent lectin that binds to GlcNAc-terminating oligosaccharides: it may be involved in neural cell interactions.[1]

References

  1. Mouse Na+/K+-ATPase beta1-subunit has a K+-dependent cell adhesion activity for beta-GlcNAc-terminating glycans. Kitamura, N., Ikekita, M., Sato, T., Akimoto, Y., Hatanaka, Y., Kawakami, H., Inomata, M., Furukawa, K. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
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