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(Received for publication, September 19, 1996, and in revised form, October 24, 1996)
From the Division of Nephrology, Department of Medicine, Mount
Sinai School of Medicine, New York, New York 10029
Maintenance of urate homeostasis requires urate
efflux from urate-producing cells with subsequent renal and
gastrointestinal excretion. The molecular basis for urate transport,
however, has not been identified. A novel full-length cDNA encoding
a 322-amino acid protein, designated UAT (urate transporter), has been
cloned from a rat renal cDNA library by antibody screening. UAT
mRNA transcripts that approximate 1.55 kilobases are present, but
differentially expressed in various rat tissues. Recombinant UAT
protein that was expressed from the cloned cDNA in
Escherichia coli and purified via immobilized metal
affinity chromatography has been functionally reconstituted as a highly
selective urate transporter/channel in planar lipid bilayers. The IgG
fraction of the polyclonal antibody that was used to select the UAT
clone from the cDNA library, but not nonimmune IgG, blocked urate
channel activity. Based on the wide tissue distribution of the mRNA
for UAT we propose that UAT provides the molecular basis for urate flux
across cell membranes, allowing urate that is formed during purine
metabolism to efflux from cells and serving as an electrogenic
transporter that plays an important role in renal and gastrointestinal
urate excretion.
Volume 272, Number 1,
Issue of January 3, 1997
pp. 617-625
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
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