XB-ART-3612Blood Cells Mol Dis May 1, 2004; 32 (3): 379-83.
The disruption of the third extracellular loop of the red cell anion exchanger AE1 does not affect electroneutral Cl-/HCO3- exchange activity.
The red cell anion exchanger (band 3; AE1) is a multispanning membrane protein that traverses the bilayer up to 14 times and mediates the stilbene-disulfonate-sensitive, electroneutral exchange of chloride and bicarbonate. Previous studies showed that the integrity of the third extracellular loop (EC3) of the protein was not essential for stilbene-disulfonate-sensitive chloride uptake. Here we demonstrate that the chloride uptake mediated by assemblies separated at EC3 represents the physiological electroneutral Cl(-)/HCO(3)(-) activity associated with intact AE1 protein. This provides further evidence that the 1:5 and 6:14 regions of the protein form discrete folding domains and confirms that the third extracellular loop does not play a pivotal role in AE1 transport function.
PubMed ID: 15121095
Article link: Blood Cells Mol Dis
Species referenced: Xenopus laevis
Genes referenced: slc4a1