Cloning of a human kidney cDNA with similarity to the sodium-glucose cotransporter.

  title={Cloning of a human kidney cDNA with similarity to the sodium-glucose cotransporter.},
  author={Rebecca G. Wells and Ana M. Pajor and Yoshikatsu Kanai and Eric Turk and Ernest M. Wright and Matthias A. Hediger},
  journal={The American journal of physiology},
  volume={263 3 Pt 2},
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… 
The human gene of a protein that modifies Na(+)-D-glucose co-transport.
The cloning of the intronless human gene hRS1 is reported, which encodes a 617-amino-acid protein with 74% amino acid identity to pRS1, which inhibits Na(+)-D-glucose co-transport expressed by human SGLT1 by decreasing both the Vmax and the apparent Km value of the transporter.
Cloning and expression of bovine sodium/glucose cotransporters.
The sequence and expression data reported in this paper lay the groundwork for future studies aimed at unraveling the functional roles of SGLT in supporting milk production and maintaining glucose homeostasis during lactation.
Cloning and expression of bovine sodium/glucose cotransporter SGLT2.
The second member of the Na(+)/glucose cotransporter family, SGLT2, is a low-affinity active glucose transporter. In humans, it is predominantly located on the apical membrane of the S1 and S2
Function and presumed molecular structure of Na+-D-glucose cotransport systems
The experiments support the hypothesis that functional Na+-d-glucose cotransport systems in mammals are composed of two SGLT1- type subunits and may contain one or two RS1-type proteins.
Differential regulation of mouse kidney sodium-dependent transporters mRNA by cadmium.
The results imply that individual sodium-glucose cotransporter mRNA species are not regulated in a similar fashion, and suggests that, in addition to SGLT1 and S GLT2, glucose reabsorption by renal epithelial cells might involve additional glucose transporters such as SglT3.
MAP17 Is a Necessary Activator of Renal Na+/Glucose Cotransporter SGLT2.
Using expression cloning, an accessory protein, 17 kDa membrane-associated protein (MAP17), was identified that increased SGLT2 activity in RNA-injected Xenopus oocytes by two orders of magnitude and occurred in opossum kidney cells cotransfected with S GLT2 and MAP17.
Molecular cloning and characterization of the vasopressin-regulated urea transporter of rat kidney collecting ducts.
The data show that UT1 corresponds to the previously characterized vasopressin-regulated urea transporter in the apical membrane of the terminal IMCD which plays a critical role in renal water conservation.
Cloning and regulation of expression of the rat kidney urea transporter (rUT2).
Analysis of rat kidney mRNA revealed that the expression levels of the two rUT2 transcripts are modulated by different pathways to allow fluid and nitrogen balance to be regulated independently, providing important insights into the regulation of the renal urea transporter UT2.
The human kidney low affinity Na+/glucose cotransporter SGLT2. Delineation of the major renal reabsorptive mechanism for D-glucose.
The major reabsorptive mechanism for D-glucose in the kidney is known to involve a low affinity high capacity Na+/glucose cotransporter, which is located in the early proximal convoluted tubule