Effect of warm or cold exposure on GDP binding and uncoupling protein in rat brown fat

P. Trayhurn, M. Ashwell, G. Jennings, D. Richard and D. M. Stirling The effects of acute and chronic exposure to different environmental temperatures on the total tissue cytochrome oxidase activity, level of mitochondrial GDP binding, and specific mitochondrial concentration of uncoupling protein ha...

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Veröffentlicht in:American journal of physiology: endocrinology and metabolism 1987-02, Vol.252 (2), p.E237-E243
Hauptverfasser: Trayhurn, P, Ashwell, M, Jennings, G, Richard, D, Stirling, D. M
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Sprache:eng
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Zusammenfassung:P. Trayhurn, M. Ashwell, G. Jennings, D. Richard and D. M. Stirling The effects of acute and chronic exposure to different environmental temperatures on the total tissue cytochrome oxidase activity, level of mitochondrial GDP binding, and specific mitochondrial concentration of uncoupling protein have been investigated in rat brown adipose tissue, a radioimmunoassay being used to measure uncoupling protein. Acclimation at different temperatures for 3 wk produced parallel changes in GDP binding, the concentration of uncoupling protein, and the activity of cytochrome oxidase, each parameter rising with decreasing temperature between thermoneutrality (29 degrees C) and 4 degrees C. Acute exposure of warm-acclimated (29 degrees C) rats to the cold (4 degrees C) led to a rapid increase in GDP binding without any alteration in the amount of uncoupling protein. The increase in binding was accompanied by an increase in the rate of acetate-induced swelling of the mitochondria. The concentration of uncoupling protein in warm-acclimated rats was significantly raised only after 48 h exposure to cold. When cold-acclimated rats were exposed acutely to the warm, there was a rapid decrease in GDP binding without any alteration in the amount of uncoupling protein. It is concluded that after alterations in environmental temperature the concentration of uncoupling protein in brown adipose tissue mitochondria changes much more slowly than GDP binding and that binding can therefore be dissociated from the amount of the protein.
ISSN:0193-1849
0002-9513
1522-1555
DOI:10.1152/ajpendo.1987.252.2.e237