Abstract
Fructose 2,6-bisphosphate is a potent endogenous stimulator of glycolysis. A high aerobic glycolytic rate often correlates with increased cell proliferation. To investigate this relationship, we have produced clonal cell lines of Rat-1 fibroblasts that stably express transgenes coding for 6-phosphofructo-2-kinase, which catalyzes the synthesis of fructose 2,6-bisphosphate, or for fructose 2,6-bisphosphatase, which catalyzes its degradation. While serum deprivation in culture reduced the growth rate of control cells, it caused apoptosis in cells overproducing fructose 2,6-bisphosphate. Apoptosis was inhibited by 5-amino-4-imidazolecarboxamide riboside, suggesting that 5'-AMP-activated protein kinase interferes with this phenomenon.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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AMP-Activated Protein Kinases
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Aminoimidazole Carboxamide / analogs & derivatives
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Animals
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Apoptosis*
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Bromodeoxyuridine / metabolism
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Dose-Response Relationship, Drug
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Fibroblasts / physiology*
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Fructosediphosphates / biosynthesis*
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Glycolysis
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Growth Substances / physiology*
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Multienzyme Complexes / metabolism
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Mutagenesis, Site-Directed
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Phosphofructokinase-2
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Phosphotransferases (Alcohol Group Acceptor) / metabolism
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Protein Serine-Threonine Kinases / metabolism
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Rats
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Ribonucleotides
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Time Factors
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Transfection
Substances
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Fructosediphosphates
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Growth Substances
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Multienzyme Complexes
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Ribonucleotides
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Aminoimidazole Carboxamide
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fructose 2,6-diphosphate
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Phosphotransferases (Alcohol Group Acceptor)
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Phosphofructokinase-2
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Protein Serine-Threonine Kinases
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AMP-Activated Protein Kinases
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AICA ribonucleotide
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Bromodeoxyuridine