Meeting details menu

Meeting Authors
Meeting Abstracts
Keynote lectures
Oral communications
Poster presentations
Special symposia
Other

Acta Physiologica Congress

Back

Acta Physiologica 2009; Volume 195, Supplement 669
The 88th Annual Meeting of The German Physiological Society
3/22/2009-3/25/2009
Giessen, Germany


STIMULATION OF THE NA+-GLUCOSE COTRANSPORTER SGLT1 BY AMP-ACTIVATED PROTEIN KINASE
Abstract number: O306

Sopjani1 M., Foller1 M., Fraser2 S. A., Lang1 F.

1Department of Physiology, Eberhard-Karls-University, Tbingen
2The Burnet Research Institute, Austin Health,, Victoria, Australia

The cellular energy status is sensed by the AMP-activated protein kinase (AMPK) which is activated upon increase in cytosolic AMP/ATP concentration ratio. Effects of AMPK include stimulation of cellular glucose uptake, glycolysis, stimulation of fatty acid oxidation and expression of enzymes required for ATP production. The Na+/glucose cotransporter SGLT1 mediates the Na+-coupled cellular uptake of glucose. As it is driven by the steep electrochemical gradient for Na+, it allows the glucose uptake even at low extracellular glucose concentrations. Thus, we hypothesized that AMPK may stimulate SGLT1. To test this hypothesis, SGLT1 was expressed in Xenopus oocytes either without or with AMPK and SGLT1 activity estimated from glucose-induced current (Iglu) in dual voltage clamp experiments. In oocytes expressing SGLT1 alone Iglu approached a maximal current of 0.0980.001 mA. Half maximal current was observed at 0.650.03 mM glucose concentration. In Xenopus oocytes coexpressing SGLT1 and AMPK, the maximal current (0.1630.002 mA) was significantly higher, whereas the glucose concentration needed (0.580.03 mM) for half maximal current was similar to the respective values in the absence of AMPK. The present observations disclose a novel function of AMPK serving cellular nutrient supply during energy depletion.

To cite this abstract, please use the following information:
Acta Physiologica 2009; Volume 195, Supplement 669 :O306

Our site uses cookies to improve your experience.You can find out more about our use of cookies in our standard cookie policy, including instructions on how to reject and delete cookies if you wish to do so.

By continuing to browse this site you agree to us using cookies as described in our standard cookie policy .

CLOSE