The adhesion molecule on glia (AMOG) is a homologue of the β subunit of the Na,K-ATPase

S. Gloor, H. Antonicek, K. J. Sweadner, S. Pagliusi, R. Frank, M. Moos, M. Schachner

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AMOG (adhesion molecule on glia) is a Ca2+-independent adhesion molecule which mediates selective neuron-astrocyte interaction in vitro (Antonicek, H., E. Persohn, and M. Schachner. 1987. J. Cell Biol. 104:1587-1595). Here we report the structure of AMOG and its association with the Na,K-ATPase. The complete cDNA sequence of mouse AMOG revealed 40% amino acid identity with the previously cloned β subunit of rat brain Na,K-ATPase. Immunoaffinity-purified AMOG and the β subunit of detergent-purified brain Na,K-ATPase had identical apparent molecular weights, and were immunologically cross-reactive. Immunoaffinity-purified AMOG was associated with a protein of 100,000 M(r). Monoclonal antibodies revealed that this associated protein comprised the α2 (and possibly α3) isoforms of the Na,K-ATPase catalytic subunit, but not α1. The monoclonal AMOG antibody that blocks adhesion was shown to interact with Na,K-ATPase in intact cultured astrocytes by its ability to increase ouabain-inhibited 86Rb+ uptake. AMOG-mediated adhesion occurred, however, both at 4°C and in the presence of ouabain, an inhibitor of the Na,K-ATPase. Both AMOG and the β subunit are predicted to be extracellularly exposed glycoproteins with single transmembrane segments, quite different in structure from the Na,K-ATPase α subunit or any other ion pump. We hypothesize that AMOG or variants of the β subunit of the Na,K-ATPase, tightly associated with an α subunit, are recognition elements for adhesion that subsequently link cell adhesion with ion transport.

Original languageEnglish (US)
Pages (from-to)165-174
Number of pages10
JournalJournal of Cell Biology
Issue number1
StatePublished - 1990
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Cell Biology


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