Apoptosis induced by growth factor withdrawal in fibroblasts overproducing fructose 2,6‐bisphosphate
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TL;DR
Production of 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, suggests that 5′‐AMP‐activated protein kinase interferes with this phenomenon.
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.
