Regulation of Carnitine Palmitoyltransferase (CPT) I during Fasting in Rainbow Trout (Oncorhynchus mykiss) Promotes Increased Mitochondrial Fatty Acid Oxidation

2011 ◽  
Vol 84 (6) ◽  
pp. 625-633 ◽  
Author(s):  
Andrea J. Morash ◽  
Grant B. McClelland
Keyword(s):  
Fatty Acid ◽  
Rainbow Trout ◽  
Oncorhynchus Mykiss ◽  
Fatty Acid Oxidation ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Rainbow Trout Oncorhynchus Mykiss ◽  
Mitochondrial Fatty Acid ◽  
Cpt I

scholarly journals Specific inhibition of mitochondrial fatty acid oxidation by 2-bromopalmitate and its co-enzyme A and carnitine esters

1972 ◽  
Vol 129 (1) ◽  
pp. 55-65 ◽  
Author(s):  
J. F. A. Chase ◽  
P. K. Tubbs
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Liver Mitochondria ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Dependent Manner ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Succinate Oxidation ◽  
Mitochondrial Fatty Acid ◽  
Long Chain

1. The CoA and carnitine esters of 2-bromopalmitate are extremely powerful and specific inhibitors of mitochondrial fatty acid oxidation. 2. 2-Bromopalmitoyl-CoA, added as such or formed from 2-bromopalmitate, inhibits the carnitine-dependent oxidation of palmitate or palmitoyl-CoA, but not the oxidation of palmitoylcarnitine, by intact liver mitochondria. 3. 2-Bromopalmitoylcarnitine inhibits the oxidation of palmitoylcarnitine as well as that of palmitate or palmitoyl-CoA. It has no effect on succinate oxidation, but inhibits that of pyruvate, 2-oxoglutarate or hexanoate; however, the oxidation of these substrates (but not of palmitate, palmitoyl-CoA or palmitoyl-carnitine) is restored by carnitine. 4. In damaged mitochondria, added 2-bromopalmitoyl-CoA does inhibit palmitoylcarnitine oxidation; pyruvate oxidation is unaffected by the inhibitor alone, but is impaired if palmitoylcarnitine is subsequently added. 5. The findings have been interpreted as follows. 2-Bromopalmitoyl-CoA inactivates (in a carnitine-dependent manner) a pool of carnitine palmitoyltransferase which is accessible to external acyl-CoA. This results in inhibition of palmitate or palmitoyl-CoA oxidation. A second pool of carnitine palmitoyltransferase, inaccessible to added acyl-CoA in intact mitochondria, can generate bromopalmitoyl-CoA within the matrix from external 2-bromopalmitoylcarnitine; this reaction is reversible. Such internal 2-bromopalmitoyl-CoA inactivates long-chain β-oxidation (as does added 2-bromopalmitoyl-CoA if the mitochondria are damaged) and its formation also sequesters intramitochondrial CoA. Since this CoA is shared by pyruvate and 2-oxoglutarate dehydrogenases, the oxidation of their substrates is depressed by 2-bromopalmitoylcarnitine, unless free carnitine is available to act as a ‘sink’ for long-chain acyl groups. 6. These effects are compared with those reported for other inhibitors of fatty acid oxidation.

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

1997 ◽  
Vol 75 (2) ◽  
pp. 324-331 ◽  
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.

scholarly journals Resveratrol-Dependent Stimulation of Mitochondrial Fatty Acid Oxidation in Deficient Cells. Implication of miRNAs

Proceedings ◽  
2019 ◽  
Vol 11 (1) ◽  
pp. 5
Author(s):  
Aires ◽  
Delmas ◽  
Djouadi ◽  
Bastin ◽  
Cherkaoui ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Mitochondrial Fatty Acid ◽  
Stimulation Of

The mitochondrial-located enzyme Carnitine palmitoyltransferase [...]

Glucocorticoids promote mitochondrial fatty acid oxidation in the fetal heart

2019 ◽  
Author(s):  
Helena Urquijo ◽  
Emma N Panting ◽  
Roderick N Carter ◽  
Emma J Agnew ◽  
Caitlin S Wyrwoll ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Fetal Heart ◽  
Acid Oxidation ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Mitochondrial Fatty Acid

scholarly journals Quantitation of acyl-CoA and acylcarnitine esters accumulated during abnormal mitochondrial fatty acid oxidation.

1991 ◽  
Vol 266 (34) ◽  
pp. 22932-22938
Author(s):  
R.S. Kler ◽  
S. Jackson ◽  
K. Bartlett ◽  
L.A. Bindoff ◽  
S. Eaton ◽  
...  
Keyword(s):  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
Acid Oxidation ◽  
Mitochondrial Fatty Acid Oxidation ◽  
Mitochondrial Fatty Acid
Sign in / Sign up

Export Citation Format

Share Document