Acclimation to low temperature is associated with an increase in long-chain acyl-CoA synthetase in rainbow trout (Oncorhynchus mykiss) heart

Rainbow trout (Oncorhynchus mykiss) were acclimated to 5 and 15 °C. Uptake of radiolabelled palmitate by isolated cardiomyocytes was linear for at least 65 min. Myocytes from fish acclimated to 5 °C and tested at 5 °C showed higher rates of uptake than those from fish acclimated to 15 °C and tested at 5 °C. There was no significant difference in fatty acid uptake between myocytes from fish acclimated to 5 and 15 °C and tested at their respective acclimation temperature. Acclimation temperature had no effect on levels of intracellular fatty acid binding protein or carnitine palmitoyltransferase. However, acclimation to low temperature resulted in a twofold enhancement in fatty acyl-CoA synthetase activity, which increased in a linear fashion over a 28-day period. An increase in fatty acyl-CoA synthetase, which occurs on the outer mitochondrial membrane and the endoplasmic reticulum, is possibly related to low temperature-induced changes in fatty acid oxidation and synthesis of complex lipids.

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The Expression of Brain-Type Fatty Acid Binding Protein (FABP7) in Rainbow Trout (Oncorhynchus Mykiss)

Proceedings of the 2018 10th International Conference on Bioinformatics and Biomedical Technology - ICBBT '18 ◽

10.1145/3232059.3232062 ◽

2018 ◽

Author(s):

Xiaofei Yang ◽

Shaogang Xu ◽

Wentong Li ◽

Ding Yuan ◽

Jiangqi Qu

Keyword(s):

Fatty Acid ◽

Rainbow Trout ◽

Oncorhynchus Mykiss ◽

Fatty Acid Binding Protein ◽

Binding Protein ◽

Fatty Acid Binding ◽

Acid Binding Protein ◽

Rainbow Trout Oncorhynchus Mykiss

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Cold acclimation increases activities of mitochondrial long-chain acyl-CoA synthetase and carnitine acyl-CoA transferase I in heart of rainbow trout (Oncorhynchus mykiss)

Canadian Journal of Zoology ◽

10.1139/z97-041 ◽

1997 ◽

Vol 75 (2) ◽

pp. 324-331 ◽

Cited By ~ 13

Author(s):

Christopher P. Patey ◽

William R. Driedzic

Keyword(s):

Fatty Acid ◽

Rainbow Trout ◽

Low Temperature ◽

Oncorhynchus Mykiss ◽

Fatty Acid Oxidation ◽

Acid Oxidation ◽

Rainbow Trout Oncorhynchus Mykiss ◽

Coa Transferase ◽

Chain Acyl ◽

Long Chain

Rainbow trout (Oncorhynchus mykiss) were acclimated to 5 or 15 °C. Hearts were excised and assayed for the activity of enzymes essential for fatty acid metabolism. The activity of long-chain acyl-CoA synthetase, the first enzyme required in either fatty acid oxidation or complex fatty acid synthesis, was increased following acclimation to low temperature. Total crude homogenates exhibited an increase in activity with either palmitate (0.037–0.047 μmol/(min∙g)), stearate (0.037–0.055 μmol/(min∙g)), or oleate (0.041–0.064 μmol/(min∙g)) as substrate. Mitochondrial preparations showed the greatest increase in activity with palmitate (0.486–0.962 nmol/(min∙g)) as substrate, whereas microsomal preparations exhibited the greatest increase in activity with oleate (0.976–1.933 nmol/(min∙g)) as substrate. The activity of carnitine acyl-CoA transferase I, which is located on the outer mitochondrial membrane and is required for fatty acid oxidation, increased following acclimation to low temperature with palmitoyl CoA (0.137–0.352 μmol/(min∙g)), stearoyl CoA (0.066–0.152 μmol/(min∙g)), or oleoyl CoA (0.137–0.224 μmol/(min∙g)) as substrate. The parallel increase in mitochondrial long-chain acyl-CoA synthetase and carnitine acyl-CoA transferase I is consistent with previous observations of an elevated capacity of heart to oxidize fatty acids as exogenous fuels following acclimation to low temperature. The increase in microsome-based long-chain acyl-CoA synthetase may contribute to heart growth at low temperature.

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