期刊
JOURNAL OF EXPERIMENTAL BIOLOGY
卷 211, 期 8, 页码 1262-1269出版社
COMPANY BIOLOGISTS LTD
DOI: 10.1242/jeb.013474
关键词
hepatocytes; primary culture; adenosine; temperature acclimation; cytochrome c oxidase; citrate synthase; RNase protection assay
类别
Exposure of ectothermic organisms to variations in temperatures causes a transient mismatch between energy supply and demand, which needs to be compensated for during acclimation. Adenosine accumulation from ATP breakdown indicates such an imbalance and its reversal reflects a restoration of energy status. We monitored adenosine levels in blood serum and liver of common eelpout (Zoarces viviparus) during cold exposure in vivo. Furthermore, we tested its effect on the pattern of thermal acclimation in hepatocytes isolated from cold- (4 degrees C) versus warm-(11 degrees C) exposed fish. Adenosine levels increased during cold exposure in vivo and reached a transient maximum after 24 h in serum, but remained permanently elevated in liver. Whole animal cold acclimation induced a rise of liver citrate synthase activity by 44 +/- 15%, but left cytochrome c oxidase activity ( COX) and RNA expression of the respective genes unchanged. Cold incubation of hepatocytes from warm-acclimated fish failed to cause an increase of mitochondrial enzyme activities despite increased COX4 mRNA levels. Conversely, warm acclimation of hepatocytes from cold- acclimated fish reduced both enzyme activities and COX2 and COX4 mRNA levels by 26 - 37%. Adenosine treatment of both warm- and cold- acclimated hepatocytes suppressed COX activities but activated COX mRNA expression. These effects were not receptor mediated. The present findings indicate that adenosine has the potential to regulate mitochondrial functioning in vivo, albeit the pathways resulting in the contrasting effects on expression and activity need to be identified.
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