Anion exchanger 2. (AE2) binds to erythrocyte ankyrin and is colocalized with ankyrin along the basolateral plasma membrane of human gastric parietal cells

• Published in: European journal of cell biology 1998-03, Vol.75 (3), p.232-236
• Main Authors: Jöns, Thomas, Drenckhahn, Detlev
• Format: Article
• Language: English
• Subjects: anion exchanger 2; Anion Transport Proteins; ankyrin; Ankyrins - metabolism; Antiporters; Cell Membrane - metabolism; cytoskeleton; Erythrocytes - metabolism; Fluorescent Antibody Technique, Indirect; Humans; Immunoblotting; Membrane Proteins - genetics; Membrane Proteins - metabolism; Parietal cells; Parietal Cells, Gastric - metabolism; polarity; Recombinant Fusion Proteins - genetics; Recombinant Fusion Proteins - metabolism; SLC4A Proteins
• ISSN: 0171-9335; 1618-1298
• DOI: 10.1016/S0171-9335(98)80117-9

The hydrochloric acid secreting parietal cells of the human stomach mucosa have been shown to express anion exchanger 2. (AE2). AE2 is restricted to the basolateral membrane domain and is responsible for the basolateral uptake of Cl- and release of HCO 3. It is unknown which mechanism is responsible for the basolateral positioning of AE2 in parietal cells. We raised the question whether AE2 might be immobilized at the cell surface by linkage via ankyrin to the spectrin/actinbased membrane cytoskeleton. In the present study we communicate two observations that support this hypothesis, namely that in parietal cells ankyrin is localized with AE2 along the basolateral cell surface and, secondly, that purified erythrocyte ankyrin binds to the in vitrotranslated cytoplasmic domain of AE2. We conclude from these observations that AE2 in parietal cells might be linked via ankyrin to the basolateral membrane cytoskeleton and that this type of linkage might play a role in immobilizing AE2 in a non-random fashion along the basolateral membrane domain.