PMID:9173866
| Citation |
Faergeman, NJ and Knudsen, J (1997) Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling. Biochem. J. 323 ( Pt 1):1-12 |
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| Abstract |
The intracellular concentration of free unbound acyl-CoA esters is tightly controlled by feedback inhibition of the acyl-CoA synthetase and is buffered by specific acyl-CoA binding proteins. Excessive increases in the concentration are expected to be prevented by conversion into acylcarnitines or by hydrolysis by acyl-CoA hydrolases. Under normal physiological conditions the free cytosolic concentration of acyl-CoA esters will be in the low nanomolar range, and it is unlikely to exceed 200 nM under the most extreme conditions. The fact that acetyl-CoA carboxylase is active during fatty acid synthesis (Ki for acyl-CoA is 5 nM) indicates strongly that the free cytosolic acyl-CoA concentration is below 5 nM under these conditions. Only a limited number of the reported experiments on the effects of acyl-CoA on cellular functions and enzymes have been carried out at low physiological concentrations in the presence of the appropriate acyl-CoA-buffering binding proteins. Re-evaluation of many of the reported effects is therefore urgently required. However, the observations that the ryanodine-senstitive Ca2+-release channel is regulated by long-chain acyl-CoA esters in the presence of a molar excess of acyl-CoA binding protein and that acetyl-CoA carboxylase, the AMP kinase kinase and the Escherichia coli transcription factor FadR are affected by low nanomolar concentrations of acyl-CoA indicate that long-chain acyl-CoA esters can act as regulatory molecules in vivo. This view is further supported by the observation that fatty acids do not repress expression of acetyl-CoA carboxylase or Delta9-desaturase in yeast deficient in acyl-CoA synthetase. |
| Links | |
| Keywords |
Acyl Coenzyme A/physiology; Amino Acid Sequence; Animals; Carrier Proteins/physiology; Cell Communication/physiology; Coenzyme A Ligases/metabolism; Diazepam Binding Inhibitor; Energy Metabolism; Fatty Acid-Binding Proteins; Fatty Acids/physiology; Humans; Lipids/biosynthesis; Models, Biological; Molecular Sequence Data; Myelin P2 Protein/physiology; Neoplasm Proteins; Protein Kinase C/metabolism; Signal Transduction; Tumor Suppressor Proteins |
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