Document Detail


Glucose transport by human renal Na+/D-glucose cotransporters SGLT1 and SGLT2.
MedLine Citation:
PMID:  20980548     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The human Na(+)/D-glucose cotransporter 2 (hSGLT2) is believed to be responsible for the bulk of glucose reabsorption in the kidney proximal convoluted tubule. Since blocking reabsorption increases urinary glucose excretion, hSGLT2 has become a novel drug target for Type 2 diabetes treatment. Glucose transport by hSGLT2 was studied at 37°C in human embryonic kidney 293T cells using whole cell patch-clamp electrophysiology. We compared hSGLT2 with hSGLT1, the transporter in the straight proximal tubule (S3 segment). hSGLT2 transports with surprisingly similar glucose affinity and lower concentrative power than hSGLT1: Na(+)/D-glucose cotransport by hSGLT2 was electrogenic with apparent glucose and Na(+) affinities of 5 and 25 mM, and a Na(+):glucose coupling ratio of 1; hSGLT1 affinities were 2 and 70 mM and coupling ratio of 2. Both proteins showed voltage-dependent steady-state transport; however, unlike hSGLT1, hSGLT2 did not exhibit detectable pre-steady-state currents in response to rapid jumps in membrane voltage. D-Galactose was transported by both proteins, but with very low affinity by hSGLT2 (≥100 vs. 6 mM). β-D-Glucopyranosides were either substrates or blockers. Phlorizin exhibited higher affinity with hSGLT2 (K(i) 11 vs. 140 nM) and a lower Off-rate (0.03 vs. 0.2 s⁻¹) compared with hSGLT1. These studies indicate that, in the early proximal tubule, hSGLT2 works at 50% capacity and becomes saturated only when glucose is ≥35 mM. Furthermore, results on hSGLT1 suggest it may play a significant role in the reabsorption of filtered glucose in the late proximal tubule. Our electrophysiological study provides groundwork for a molecular understanding of how hSGLT inhibitors affect renal glucose reabsorption.
Authors:
Charles S Hummel; Chuan Lu; Donald D F Loo; Bruce A Hirayama; Andrew A Voss; Ernest M Wright
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural     Date:  2010-10-27
Journal Detail:
Title:  American journal of physiology. Cell physiology     Volume:  300     ISSN:  1522-1563     ISO Abbreviation:  Am. J. Physiol., Cell Physiol.     Publication Date:  2011 Jan 
Date Detail:
Created Date:  2010-12-29     Completed Date:  2011-02-04     Revised Date:  2012-01-02    
Medline Journal Info:
Nlm Unique ID:  100901225     Medline TA:  Am J Physiol Cell Physiol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  C14-21     Citation Subset:  IM    
Affiliation:
Department of Physiology, David Geffen School of Medicine at UCLA, Los Angeles, CA 90095-1751, USA.
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MeSH Terms
Descriptor/Qualifier:
Action Potentials
Biological Transport, Active
Carbon Isotopes / metabolism
Gene Expression Regulation / physiology
Glucose / metabolism*
HEK293 Cells
Humans
Kidney / physiology*
Methylglucosides / metabolism
Phlorhizin / pharmacology
Sodium-Glucose Transporter 1 / genetics,  metabolism*
Sodium-Glucose Transporter 2 / genetics,  metabolism*
Thermodynamics
Grant Support
ID/Acronym/Agency:
DK-019567/DK/NIDDK NIH HHS; DK-082153/DK/NIDDK NIH HHS
Chemical
Reg. No./Substance:
0/Carbon Isotopes; 0/Methylglucosides; 0/SLC5A1 protein, human; 0/SLC5A2 protein, human; 0/Sodium-Glucose Transporter 1; 0/Sodium-Glucose Transporter 2; 25360-07-0/methylglucoside; 50-99-7/Glucose; 60-81-1/Phlorhizin
Comments/Corrections
Comment In:
Am J Physiol Cell Physiol. 2011 Jan;300(1):C6-8   [PMID:  21048164 ]
Erratum In:
Am J Physiol Cell Physiol. 2011 Mar;300(3):C721

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