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AJP - Renal Physiology, Vol 263, Issue 3 459-F465, Copyright © 1992 by American Physiological Society
ARTICLES |
R. G. Wells, A. M. Pajor, Y. Kanai, E. Turk, E. M. Wright and M. A. Hediger
Department of Medicine, Brigham and Women's Hospital, Boston, Massachusetts 02115.
We have used low-stringency screening with the human intestinal Na(+)-glucose cotransporter SGLT1 to isolate a 2,271-nucleotide cDNA (Hu14) from human kidney. This clone, which encodes a 672-residue protein, is 59% identical at the amino acid level to SGLT1 and has a similar number and arrangement of predicted membrane-spanning regions. It also shares significant sequence identity with other Na(+)-coupled transporters. Northern blot analysis suggests strong expression of Hu14 in kidney, but, unlike SGLT1, no significant expression in intestine. We have been unable to demonstrate definitive transport of any of a number of substrates (including amino acids, sugars, nucleosides, and vitamins) into Hu14 cRNA-injected Xenopus oocytes, although sequence conservation makes it likely that Hu14 represents another member of the Na+ cotransporter family, possibly a second Na(+)-glucose cotransporter.
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