Fingerprints of hSGLT5 sugar and cation selectivity

Sodium glucose cotransporters (SGLTs) mediate the translocation of carbohydrates across the brush border membrane of different organs such as intestine, kidney, and brain. The human SGLT5 (hSGLT5), in particular, is localized in the kidney were it is responsible for mannose and fructose reabsorption...

Full description

Saved in:
Bibliographic Details
Published in:American Journal of Physiology: Cell Physiology 2014-05, Vol.306 (9), p.C864-C870
Main Authors: Ghezzi, Chiara, Gorraitz, Edurne, Hirayama, Bruce A, Loo, Donald D F, Grempler, Rolf, Mayoux, Eric, Wright, Ernest M
Format: Article
Language:English
Subjects:
Animals
Biochemistry
Brain
Cations
Cells
Glucose
HEK293 Cells
Humans
Hydrogen-Ion Concentration
Ions
Kidney - drug effects
Kidney - metabolism
Kidneys
Kinetics
Lithium - metabolism
Mannose - metabolism
Membrane Potentials
Molecular Structure
Phlorhizin - pharmacology
Rats
Rats, Sprague-Dawley
Rodents
Sodium - metabolism
Sodium-Glucose Transport Proteins - antagonists & inhibitors
Sodium-Glucose Transport Proteins - genetics
Sodium-Glucose Transport Proteins - metabolism
Transfection
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Sodium glucose cotransporters (SGLTs) mediate the translocation of carbohydrates across the brush border membrane of different organs such as intestine, kidney, and brain. The human SGLT5 (hSGLT5), in particular, is localized in the kidney were it is responsible for mannose and fructose reabsorption from the glomerular filtrate as confirmed by more recent studies on hSGLT5 knockout mice. Here we characterize the functional properties of hSGLT5 expressed in a stable T-Rex-HEK-293 cell line using biochemical and electrophysiological assays. We confirmed that hSGLT5 is a sodium/mannose transporter that is blocked by phlorizin. Li(+) and H(+) ions were also able to drive mannose transport, and transport was electrogenic. Our results moreover indicate that substrates require a pyranose ring with an axial hydroxyl group (-OH) on carbon 2 (C-2). Compared with Na(+)/glucose cotransport, the level of function of Na(+)/mannose cotransport in rat kidney slices was low.
ISSN:0363-6143
1522-1563
DOI:10.1152/ajpcell.00027.2014