Abstract
A CONSIDERABLE amount of evidence indicates that phosphofructokinase (PFK) is of importance in regulating the rate of glycolysis in a number of tissues1–5. In turn, glucose-6-phosphate, which accumulates when PFK is in hibited, has an inhibitory effect on the phosphorylation of glucose6. Thus, alterations of PFK activity may have a significant influence on carbohydrate utilization. In vitro, the activity of PFK may be altered by a multiplicity of factors7,8, some inhibitory and others stimulatory. One of the inhibitory substances is citrate9–11, and some evidence that citrate may be an inhibitor in vivo derives from the observation that citrate is elevated and PFK activity is depressed in hearts of diabetic rats and in normal hearts perfused with fatty acids9,11. Likewise, in hearts exposed to fluoroacetate, in which citrate rises to high levels, there is an inhibition of PFK12.
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BOWMAN, R., PARMEGGIANI, A. Hormonal Regulation of Cardiac Muscle Citrate. Nature 207, 988–989 (1965). https://doi.org/10.1038/207988a0
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DOI: https://doi.org/10.1038/207988a0
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