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J. Biol. Chem., Vol. 268, Issue 3, 1509-1512, Jan, 1993
CT Kong, SF Yet and JE Lever
We describe the full-length sequence and functional expression of a cDNA
cloned from LLC-PK1 cells, which appears to encode a mammalian
Na(+)-dependent neutral amino acid transporter with properties
characteristic of system A. This sequence, designated SAAT1, is 76%
identical and 89% similar in amino acid sequence to the Na(+)-dependent
glucose transporter SGLT1 of the same species. A leucine zipper region was
detected in both SAAT1 and SGLT1. The message for SAAT1 was a single
2.4-kilobase species in kidney, but mRNA species of 2.4 and 3.7 kilobases
were observed in LLC-PK1 cells as well as in intestine. Transcripts were
also found in spleen, liver, and muscle. Expression of SAAT1 in COS-7 cells
resulted in increased levels of Na(+)-dependent uptake of
2-(methylamino)isobutyric acid, a specific substrate for the system A amino
acid transporter. Uptake due to cDNA expression was inhibited by a range of
amino acids that are transported by system A and exhibited a km of 0.8 +/-
0.2 mM. These results suggest that the system A amino acid transporter is
closely related to the Na+/glucose transporter SGLT1.
Cloning and expression of a mammalian Na+/amino acid cotransporter with sequence similarity to Na+/glucose cotransporters
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225.
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