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Am J Physiol Renal Physiol 280: F325-F332, 2001;
0363-6127/01 $5.00
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Vol. 280, Issue 2, F325-F332, February 2001

UT-A3: localization and characterization of an additional urea transporter isoform in the IMCD

James M. Terris1,2, Mark A. Knepper1, and James B. Wade3

1 Laboratory of Kidney and Electrolyte Metabolism, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda; 2 Department of Physiology, Uniformed Services University of the Health Sciences, Bethesda; and 3 Department of Physiology, University of Maryland School of Medicine, Baltimore, Maryland 21201

UT-A3 has recently been identified as a splicing variant transcript of the UT-A gene present in the kidney. To study the cellular and subcellular localization of UT-A3, we raised a new polyclonal antibody to its COOH-terminal end. Immunoblots identified bands at 44 and 67 kDa predominately in the inner medulla and showed that the antibody does not recognize UT-A1. Deglycosylation with PNGase decreased the molecular mass of both forms to 40 kDa. UT-A3 is most abundant in the inner third of the inner medulla and is present in membrane fractions. Cell fractionation studies showed that UT-A3 is only detectable in inner medullary collecting duct (IMCD) cells. These observations were confirmed with immunolocalization studies demonstrating an exclusive labeling of IMCD cells. Double-labeling studies with anti-Na-K-ATPase demonstrated UT-A3 in intracellular membranes and in the apical region but were incompatible with a basolateral site for UT-A3. Although the function of this isoform in the inner medulla is unknown, the large abundance suggests that it may be important in the renal handling of urea.

urinary concentrating mechanism; inner medullary collecting duct


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