Familial distal renal tubular acidosis is associated with mutations in the red cell anion exchanger (Band 3, AE1) gene.

LJ Bruce, DL Cope, GK Jones… - The Journal of …, 1997 - Am Soc Clin Investig
LJ Bruce, DL Cope, GK Jones, AE Schofield, M Burley, S Povey, RJ Unwin, O Wrong…
The Journal of clinical investigation, 1997Am Soc Clin Investig
All affected patients in four families with autosomal dominant familial renal tubular acidosis
(dRTA) were heterozygous for mutations in their red cell HCO3-/Cl-exchanger, band 3 (AE1,
SLC4A1) genes, and these mutations were not found in any of the nine normal family
members studied. The mutation Arg589--> His was present in two families, while Arg589-->
Cys and Ser613--> Phe changes were found in the other families. Linkage studies confirmed
the co-segregation of the disease with a genetic marker close to AE1. The affected …
All affected patients in four families with autosomal dominant familial renal tubular acidosis (dRTA) were heterozygous for mutations in their red cell HCO3-/Cl- exchanger, band 3 (AE1, SLC4A1) genes, and these mutations were not found in any of the nine normal family members studied. The mutation Arg589--> His was present in two families, while Arg589--> Cys and Ser613--> Phe changes were found in the other families. Linkage studies confirmed the co-segregation of the disease with a genetic marker close to AE1. The affected individuals with the Arg589 mutations had reduced red cell sulfate transport and altered glycosylation of the red cell band 3 N-glycan chain. The red cells of individuals with the Ser613--> Phe mutation had markedly increased red cell sulfate transport but almost normal red cell iodide transport. The erythroid and kidney isoforms of the mutant band 3 proteins were expressed in Xenopus oocytes and all showed significant chloride transport activity. We conclude that dominantly inherited dRTA is associated with mutations in band 3; but both the disease and its autosomal dominant inheritance are not related simply to the anion transport activity of the mutant proteins.
The Journal of Clinical Investigation