Regulation of fructose 2,6-bisphosphate metabolism in human fibroblasts |
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| Affiliation: | 1. Department of Applied Chemistry, South China Agricultural University, Guangzhou 510642, China;2. School of Chemical Engineering and Energy Technology, Dongguan University of Technology, Dongguan 523808, China;3. CSIRO Agriculture & Food Flagship, 671 Sneydes Road, Werribee, Vic 3030, Australia;4. College of Food Sciences, South China University of Technology, Guangzhou 510640, China;5. Department of Applied Mathematics, South China Agricultural University, Guangzhou 510642, China;1. Graduate Faculty of Environment, University of Tehran, P.O. Box 14155-6135, Tehran, Iran;2. Environmental Research Laboratory, Department of Water and Environmental Engineering, School of Civil Engineering, Iran University of Science and Technology, P.O. Box 16765-163, Narmak, Tehran, Iran;1. The Cardiac Registry, Departments of Cardiology, Pathology, and Cardiac Surgery, Boston Children''s Hospital, Boston, MA, USA;2. Department of Thoracic and Cardiovascular Surgery, Mie University Graduate School of Medicine, Mie, Japan;3. Department of Pediatrics, Harvard Medical School, Boston, MA, USA;4. Department of Pathology, Boston Children''s Hospital and Harvard Medical School, Boston, MA, USA |
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| Abstract: | In the present work, the mechanism involved in the regulation of fructose 2,6-bisphosphate (fructose-2,6-P2) metabolism in human fibroblasts has been studied. Various agents like serum, insulin and adrenaline known to affect glycolysis have been investigated for their ability to influence fructose 2,6-P2 metabolism in confluent human fibroblasts. Serum appears to be the most potent activator of fructose-2,6-P2 levels and capable of inducing a marked increase in 6-phosphofructo-2-kinase (ATP: d-fructose-6-phosphate-2-phosphotransferase), EC 2.7.1. 105). To a lesser extent insulin has the same effects. The increase in enzyme activity elicited by serum and insulin does not require de novo protein synthesis since the process is insensitive to cycloheximide. Incubation of fibroblasts in the presence of adrenaline is responsible for a significant rise in fructose-2,6-P2 levels without affecting 6-phosphofructo-2-kinase. Similar experiments performed on glucose-starved or cytochalasin B-treated cells show that the effects elicited by all the agents are strictly dependent on glucose availability. |
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