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Blood, 1 January 2002, Vol. 99, No. 1, pp. 342-347
RED CELLS
Band 3 Walton, a C-terminal deletion associated with distal renal
tubular acidosis, is expressed in the red cell membrane but retained
internally in kidney cells
Ashley M. Toye,
Lesley J. Bruce,
Robert J. Unwin,
Oliver Wrong, and
Michael J. A. Tanner
From the Department of Biochemistry, School of Medical
Sciences, University of Bristol; and Centre for Nephrology, University
College London Medical School, United Kingdom.
Human band 3 Walton is an AE1 mutation that results in the deletion
of the 11 COOH-terminal amino acids of the protein and is associated
with dominant distal renal tubular acidosis. The properties of
band 3 Walton expressed with normal band 3 in the heterozygous mutant
erythrocytes and the kidney isoform expressed in Xenopus
oocytes and in the Madin-Darby canine kidney cell line were examined.
The mutant erythrocytes have normal hematology but have reduced band 3 Walton content. Transport studies showed that erythrocyte band 3 Walton
has normal sulfate transport activity, and kidney band 3 Walton has
normal chloride transport activity when expressed in
Xenopus oocytes. The mutant protein is clearly able to
reach the cell surface of erythrocytes and oocytes. In contrast, while
normal kidney band 3 was expressed at the cell surface in the kidney
cell line, the Walton mutant protein was retained intracellularly
within the kidney cells. The results demonstrate that band 3 Walton is
targeted differently in erythrocytes and kidney cells and indicate that
the COOH-terminal tail of band 3 is required to allow movement to the
cell surface in kidney cells. It is proposed here that the
mutant band 3 gives rise to dominant distal renal tubular acidosis by
inhibiting the movement of normal band 3 to the cell surface. It is
suggested that this results from the association of the normal
and mutant proteins in band 3 hetero-oligomers, which causes the
intracellular retention of normal band 3 with the mutant protein.
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