title: The adhesion molecule on glia (AMOG/beta 2) and alpha 1 subunits assemble to functional sodium pumps in Xenopus oocytes.
abstract: The adhesion molecule on glia, AMOG, an integral cell surface glycoprotein highly expressed by cerebellar astrocytes and involved in neuron to astrocyte adhesion and granule neuron migration (Antonicek, H., Persohn, E., and Schachner, M. (1987) J. Cell Biol. 104, 1587-1595) has been identified as a beta 2 subunit isoform of the mouse sodium pump (Gloor, S., Antonicek, H., Sweadner, K.J., Pagliusi, S., Frank, R., Moos, M., and Schachner, M. (1990) J. Cell Biol. 110, 165-174). Here we demonstrate that AMOG/beta 2 expressed by cRNA injection in Xenopus oocytes is capable of combining with endogenous Xenopus alpha 1 subunits or coexpressed Torpedo alpha 1 subunits to yield a functional alpha 1/AMOG sodium pump isozyme. Determinations of the number of ouabain binding sites and ouabain-sensitive 86Rb+ uptake suggest that the alpha 1/AMOG isozyme has slightly lower maximum transport rate and apparent affinity for external K+ than the alpha 1/beta 1 isozyme. Immunoprecipitation of alpha 1/AMOG complexes from digitonin extracts of [35S]methionine-labeled oocytes with a monoclonal anti-AMOG antibody provides direct evidence for a stable association between AMOG and the alpha 1 subunits of Xenopus and Torpedo.
authors.affiliation: Max-Planck-Institute of Biophysics, Frankfurt, Germany.
authors.forename: G
authors.initials: G
authors.lastname: Schmalzing
authors.forename: S
authors.initials: S
authors.lastname: Kröner
authors.forename: M
authors.initials: M
authors.lastname: Schachner
authors.forename: S
authors.initials: S
authors.lastname: Gloor
mesh_terms: D000251:Adenosine Triphosphatases; D000818:Animals; D027682:Cation Transport Proteins; D015816:Cell Adhesion Molecules, Neuronal / Q000235:genetics / Q000378:metabolism*; D002478:Cells, Cultured; D004072:Digitonin; D004591:Electrophoresis, Polyacrylamide Gel; D016326:Extracellular Matrix Proteins / Q000235:genetics / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism; D051379:Mice; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D009457:Neuroglia / Q000378:metabolism*; D009865:Oocytes; D010042:Ouabain / Q000378:metabolism; D010957:Plasmids; D011233:Precipitin Tests; D012313:RNA / Q000235:genetics; D018075:RNA, Complementary; D012413:Rubidium / Q000378:metabolism; D000254:Sodium-Potassium-Exchanging ATPase; D014101:Torpedo; D014981:Xenopus
chemical_list: C504191:Atp1b2 protein, mouse; D027682:Cation Transport Proteins; D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D007527:Isoenzymes; D009419:Nerve Tissue Proteins; D018075:RNA, Complementary; D010042:Ouabain; D012313:RNA; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase; D004072:Digitonin; D012413:Rubidium