Band 3 protein-cholesterol interactions in erythrocyte membranes. Possible role in anion transport and dependency on membrane phospholipid.
Band 3 protein of the human erythrocyte membrane, the anion transport protein, possesses a high affinity steroid binding site. In mixed phospholipid-cholesterol monolayers, the state of occupancy of this site is positively correlated with their cholesterol and sphingomyelin content and negatively with their glycerophospholipid content. We suggest that, in the erythrocyte membrane, the binding site is an inhibitory site of anion transport and that the modulation of its state of occupancy by the membrane lipid is responsible for the negative correlation of anion transport with the membrane's content of cholesterol and sphingomyelin and the positive correlation with the phosphatidylcholine content.
D001457:Anion Exchange Protein 1, Erythrocyte; D001665:Binding Sites; D001693:Biological Transport, Active; D001798:Blood Proteins; D002784:Cholesterol / Q000097:blood*; D004910:Erythrocyte Membrane / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism*; D010743:Phospholipids / Q000097:blood*
D001457:Anion Exchange Protein 1, Erythrocyte; D001798:Blood Proteins; D008563:Membrane Lipids; D010743:Phospholipids; D002784:Cholesterol