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Activity of cytoplasmic acetyl-CoA hydrolase in sheep liver and its potential role in heat production

Published online by Cambridge University Press:  27 March 2009

N. S. Jessop ,
N. D. Scollan ,
M. J. Souter  and
B. Crabtree
N. S. Jessop
Affiliation:
Department of Agriculture, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh EH9 3JGUK
N. D. Scollan
Affiliation:
Department of Agriculture, University of Edinburgh, King's Buildings, West Mains Road, Edinburgh EH9 3JGUK
M. J. Souter
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SBUK
B. Crabtree
Affiliation:
The Rowett Research Institute, Bucksburn, Aberdeen AB2 9SBUK
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Summary

Acetyl-CoA hydrolase which is stimulated by adenosine-5′-triphosphate is present in the cytoplasm of ovine liver and, unlike in certain others species, is not inactivated by cold. It is suggested that this enzyme is involved in a substrate cycle between acetate and acetyl-CoA. The heat produced as a result of such cycling may be as much as 2·5% of basal heat production and may be partly responsible for the increased heat increment that often follows the ingestion of diets that provide large quantities of acetate.

Type
Animals
Information
The Journal of Agricultural Science , Volume 115 , Issue 2 , October 1990 , pp. 265 - 267
Copyright
Copyright © Cambridge University Press 1990

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References

REFERENCES

Crabtree, B., Marr, S. A., Anderson, S. E. & MacRae, J. C. (1987). Measurement of the rate of substrate cycling between acetate and acetyl-CoA in sheep muscle in vivo. Biochemical Journal 243, 821–827.CrossRefGoogle ScholarPubMed
Gill, M., Thornley, J. H. M., Black, J. L., Oldham, J. D. & Beever, D. E. (1984). Simulation of the metabolism of absorbed energy-yielding nutrients in young sheep. British Journal of Nutrition 52, 621–649.CrossRefGoogle Scholar
Jessop, N. S., Smith, G. H. & Crabtree, B. (1986). Measurement of a substrate cycle between acetate and acetyl-CoA in rat hepatocytes. Biochemical Society Transactions 14, 146–147.CrossRefGoogle Scholar
Knowles, S. E., Jarrett, I. G., Filsell, O. H. & Ballard, F. J. (1974). Production and utilisation of acetate in mammals. Biochemical Journal 142, 401–411.CrossRefGoogle ScholarPubMed
Lienhard, G. E. & Secemski, I. I. (1973). P1, P5-Di-(adenosine-5′)pentaphosphate, a potent multisubstrate inhibitor of adenylate kinase. Journal of Biological Chemistry 248, 1121–1123.CrossRefGoogle Scholar
MacRae, J. C. & Lobley, G. E. (1982). Some factors influencing thermal energy losses during the metabolism of ruminants. Livestock Production Science 9, 447–456.CrossRefGoogle Scholar
Matsunaga, T., Isohashi, F., Nakanishi, Y. & Sakamoto, H. (1985). Physiological changes in the activities of extramitochondrial acetyl-CoA hydrolase in the liver of rats under various metabolic conditions. European Journal of Biochemistry 152, 331–335.CrossRefGoogle ScholarPubMed
Pethick, D. W., Lindsay, D. B., Barker, P. J. & Northrop, A. J. (1981). Acetate supply and utilisation by the tissues of sheep in vivo. British Journal of Nutrition 46, 97–110.CrossRefGoogle ScholarPubMed
Prass, R. L., Isohashi, F. & Utter, M. F. (1980). Purification and characterisation of an extramitochondrial acetyl coenzyme A hydrolase from rat liver. Journal of Biological Chemistry 255, 5215–5223.CrossRefGoogle ScholarPubMed
Rabkin, M. & Blum, J. J. (1985). Quantitative analysis of intermediary metabolism in hepatocytes incubated in the presence and absence of glucagon with a substrate mixture containing glucose, ribose, fructose, alanine and acetate. Biochemical Journal 225, 761–786.CrossRefGoogle ScholarPubMed
Soling, H. D. & Rescher, C. (1985). On the regulation of cold-labile cytosolic and of mitochondrial acetyl-CoA hydrolase in rat liver. European Journal of Biochemistry 147, 111–117.CrossRefGoogle ScholarPubMed