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1 Department of Pathology, 3 Division of Nephrology, Department of Medicine, Emory University School of Medicine, Atlanta, Georgia 30322; and 2 Marine Biomedicine and Environmental Sciences, Medical University of South Carolina, Charleston, South Carolina 29425
We have isolated and characterized the human homolog of the rat largest urea transporter of the UT-A family (hUT-A1). The 4.2-kb hUT-A1 cDNA encodes a 920-amino acid peptide, which is 89% identical to the rat UT-A1 protein. By Northern hybridization, hUT-A1 expression is detected in the human inner medulla as a ~4.4-kb mRNA transcript. By Western analysis, hUT-A1 is identified as a ~100-kDa protein in the human inner medulla. By immunohistochemistry, hUT-A1 expression is localized to the inner medullary collecting duct (IMCD). When transfected into HEK-293 cells hUT-A1 cDNA is translated into a ~98-kDa protein. Expression of hUT-A1 in Xenopus oocytes results in phloretin-inhibitable uptake of 14C-urea, which shows only modest stimulation by cAMP, suggesting that in the human IMCD vasopressin may have a limited role in the short-term regulation of hUT-A1-mediated urea transport. We determined the organization of the human Slc14a2 gene and identified 20 exons distributed over ~67.5 kb on chromosome 18, from which hUT-A1 and the other human urea transporter, hUT-A2, are transcribed.
urea transport; urine transporter; vasopressin; kidney
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