ANT2 Isoform Required for Cancer Cell Glycolysis |
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Authors: | Arnaud?Chevrollier Dominique?Loiseau Béatrice?Chabi Gilles?Renier Olivier?Douay Yves?Malthièry Email author" target="_blank">Georges?StepienEmail author |
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Institution: | (1) Inserm, U694, Angers, F-49033, France;(2) Univ Angers, Angers, F-49035, France;(3) CHRU Angers, Service d' Immunologie, Angers, F-49033, France;(4) INRA, U1019, Clermont-Ferrand, F-63009, France;(5) Univ Auvergne, Clermont-Ferrand, F-63001, France;(6) Inserm, U484, Clermont-Ferrand, F-63005, France |
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Abstract: | The three adenine nucleotide translocator ({ANT1} to {ANT3}) isoforms, differentially expressed in human cells, play a crucial
role in cell bioenergetics by catalyzing ADP and ATP exchange across the mitochondrial inner membrane. In contrast to differentiated
tissue cells, transformed cells, and their ρ0 derivatives, i.e. cells deprived of mitochondrial DNA, sustain a high rate of glycolysis. We compared the expression pattern
of {ANT} isoforms in several transformed human cell lines at different stages of the cell cycle. The level of {ANT2} expression
and glycolytic ATP production in these cell lines were in keeping with their metabolic background and their state of differentiation.
The sensitivity of the mitochondrial inner membrane potential (Δψ) to several inhibitors of glycolysis and oxidative phosphorylation
confirmed this relationship. We propose a new model for ATP uptake in cancer cells implicating the {ANT2} isoform, in conjunction
with hexokinase II and the β subunit of mitochondrial ATP synthase, in the Δψ maintenance and in the aggressiveness of cancer
cells. |
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Keywords: | Carcinogenesis mitochondria glycolysis adenine nucleotide translocator |
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