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(Received for publication, July 8, 1996, and in revised form, April 1, 1997)
From the Twenty-six different hepatoma cell lines
established from cancer-prone transgenic mice exhibited a close
correlation between expression of the GLUT 2 glucose transporter and
activation of the L-type pyruvate kinase (L-PK) gene by glucose,
as judged by Northern blot analyses and transient transfection assays.
The L-PK gene and a transfected L-PK construct were silent in GLUT 2(+)
cells and active in GLUT 2( The expression of the L-PK gene in GLUT 2(
Volume 272, Number 29,
Issue of July 18, 1997
pp. 17937-17943
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
,
,
,
Institut National de la Santé et de la
Recherche Médicale U.129, Institut Cochin de
Génétique Moléculaire, Université René
Descartes, 75014 Paris, France, the 
Centre de Recherche sur
l'Endocrinologie Moléculaire et le Développement, CNRS, 9 rue Jules Hetzel, 92190 Meudon, France, and the ** Institut National de
la Santé et de la Recherche Médicale U.246, Institut
Fédératif de Recherche, Faculté de Médecine
Xavier Bichat, B.P.416, 75018 Paris, France
) cells cultured in glucose-free medium.
Transfection of GLUT 2() cells with a GLUT 2 expression vector
restored the inducibility of the L-PK promoter by glucose, mainly by
suppressing the glucose-independent activity of this promoter. Culture
of GLUT 2() cells, in which the L-PK gene is constitutively
expressed, in a culture medium using fructose as fuel selected GLUT
2(+) clones in which the L-PK gene responded to glucose.
) cells cultured in the
absence of glucose was correlated with a high intracellular glucose
6-phosphate (Glu-6-P) concentration while under similar culture
conditions Glu-6-P concentration was very low in GLUT 2(+) cells.
Consequently, a role of GLUT 2 in the glucose responsiveness of
glucose-sensitive genes in cultured hepatoma cells could be to allow
for Glu-6-P depletion under gluconeogenic culture conditions. In the
absence of GLUT 2, glucose endogeneously produced might be unable to be
exported from the cells and would be phosphorylated again to Glu-6-P by
constitutively expressed hexokinase isoforms, continuously generating
the glycolytic intermediates active on the L-PK gene transcription.
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