Intestinal Glucose-dependent Expression of Glucose-6-phosphatase
Abstract
Glucose-6-phosphatase (G6Pase) catalyzes the release of glucose from glucose 6-phosphate. This enzyme was mainly studied in the liver, but while detected in the small intestine little is known about the regulation of its intestinal expression. This study describes the mechanisms of the glucose-dependent regulation of G6Pase expression in intestinal cells. Results obtained in vivo and in Caco-2/TC7 enterocytes showed that glucose increases the G6Pase mRNA level. In Caco-2/TC7 cells, glucose stabilized G6Pase mRNA and activated the transcription of the gene, meaning that glucose-dependent G6Pase expression involved both transcriptional and post-transcriptional mechanisms. Reporter-gene studies showed that, although the -299/+57 region of the human G6Pase promoter was sufficient to trigger the glucose response in the hepatoma cell line HepG2, the -1157/-1133 fragment was required for maximal activation of glucose-6-phosphatase gene transcription in Caco-2/TC7 cells. This fragment binds the aryl receptor nuclear translocator (ARNT), cAMP-responsive element-binding protein, and upstream stimulatory factor transcription factors. The DNA binding activity of these transcription factors was increased in nuclear extracts of differentiated cells from the intestinal villus of mice fed sugar-rich diets as compared with mice fed a no-sugar diet. A direct implication of ARNT in the activation of G6Pase gene transcription by glucose has been observed in Caco-2/TC7 cells using RNA interference experiments. These results support a physiological role for G6Pase in the control of nutrient absorption in the small intestine.
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BibTeX
@article{carriere2026intestinal,
title = {{Intestinal Glucose-dependent Expression of Glucose-6-phosphatase}},
author = {Véronique Carrière and Maude Le Gall and Florence Gouyon-Saumande and Dieter Schmoll and Edith Brot-Laroche and Valérie Chauffeton and Jean Chambaz and Monique Rousset},
journal = {Journal of Biological Chemistry},
year = {2026},
month = sep,
doi = {10.1074/jbc.m502192200},
url = {https://hal.science/hal-05754772v1},
note = {CC BY},
}
RIS
TY - JOUR
TI - Intestinal Glucose-dependent Expression of Glucose-6-phosphatase
AU - Véronique Carrière
AU - Maude Le Gall
AU - Florence Gouyon-Saumande
AU - Dieter Schmoll
AU - Edith Brot-Laroche
AU - Valérie Chauffeton
AU - Jean Chambaz
AU - Monique Rousset
PY - 2026
DA - 2026/09/18
JO - Journal of Biological Chemistry
DO - 10.1074/jbc.m502192200
UR - https://hal.science/hal-05754772v1
AB - Glucose-6-phosphatase (G6Pase) catalyzes the release of glucose from glucose 6-phosphate. This enzyme was mainly studied in the liver, but while detected in the small intestine little is known about the regulation of its intestinal expression. This study describes the mechanisms of the glucose-dependent regulation of G6Pase expression in intestinal cells. Results obtained in vivo and in Caco-2/TC7 enterocytes showed that glucose increases the G6Pase mRNA level. In Caco-2/TC7 cells, glucose stabilized G6Pase mRNA and activated the transcription of the gene, meaning that glucose-dependent G6Pase expression involved both transcriptional and post-transcriptional mechanisms. Reporter-gene studies showed that, although the -299/+57 region of the human G6Pase promoter was sufficient to trigger the glucose response in the hepatoma cell line HepG2, the -1157/-1133 fragment was required for maximal activation of glucose-6-phosphatase gene transcription in Caco-2/TC7 cells. This fragment binds the aryl receptor nuclear translocator (ARNT), cAMP-responsive element-binding protein, and upstream stimulatory factor transcription factors. The DNA binding activity of these transcription factors was increased in nuclear extracts of differentiated cells from the intestinal villus of mice fed sugar-rich diets as compared with mice fed a no-sugar diet. A direct implication of ARNT in the activation of G6Pase gene transcription by glucose has been observed in Caco-2/TC7 cells using RNA interference experiments. These results support a physiological role for G6Pase in the control of nutrient absorption in the small intestine.
SN - 0021-9258
SN - 1083-351X
ER -