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Cited by 685

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Role of long-chain fatty acyl-CoA esters in the regulation of metabolism and in cell signalling

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FÆRGEMAN, Nils Joakim, KNUDSEN, Jens·1997·Biochemical Journal
DOI 10.1042/bj3230001
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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 Δ9-desaturase in yeast deficient in acyl-CoA synthetase.

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Metadata

Authors
FÆRGEMAN, N. J., & KNUDSEN, J.
Venue
Biochemical Journal
Publisher
Portland Press Ltd.
Published
1997-04-01
Volume
323
Issue
1
Pages
1-12
ISSN
  • 0264-6021 (ISSN-L)
  • 1470-8728
DOI
10.1042/bj3230001
OpenAlex
W1763805809
Cited by
685
References
2
FWCI
14.77
Type
journal article
Language
en
Open access
green

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