Difference between revisions of "Kudin 2002 Mol Biol Rep"
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{{Publication | {{Publication | ||
|title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol. Biol. Rep. 29: 89-92. | |title=Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol. Biol. Rep. 29: 89-92. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/12241082 PMID: 12241082] | |||
|authors=Kudin A, Vielhaber S, Elger CE, Kunz WS | |authors=Kudin A, Vielhaber S, Elger CE, Kunz WS | ||
|year=2002 | |year=2002 | ||
|journal=Molec. Biol. Rep. | |journal=Molec. Biol. Rep. | ||
|abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue. | |abstract=To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue. | ||
| | |discipline=Mitochondrial Physiology | ||
}} | }} | ||
{{Labeling | {{Labeling | ||
| | |instruments=Oxygraph-2k | ||
|organism=Human | |organism=Human | ||
|tissues=Skeletal Muscle, Neurons; Brain | |tissues=Skeletal Muscle, Neurons; Brain | ||
|preparations=Permeabilized Cell or Tissue; Homogenate | |preparations=Permeabilized Cell or Tissue; Homogenate | ||
|enzymes= | |enzymes=Complex IV; Cytochrome c Oxidase | ||
| | |discipline=Mitochondrial Physiology | ||
}} | }} |
Revision as of 11:09, 9 September 2011
Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Differences in flux control and reserve capacity of cytochrome c oxidase (COX) in human skeletal muscle and brain suggest different metabolic effects of mild COX deficiencies. Mol. Biol. Rep. 29: 89-92. |
Kudin A, Vielhaber S, Elger CE, Kunz WS (2002) Molec. Biol. Rep.
Abstract: To evaluate tissue specific control of oxidative phosphorylation by cytochrome c oxidase (COX) we determined the flux control coefficient and the metabolic reserve capacity of this enzyme in human saponin-permeabilised muscle fibers and digitonin-treated parahippocampal homogenates. In these tissue preparations it is possible to investigate mitochondrial function under conditions which are close to the in vivo situation. In the presence of NAD-dependent substrates we observed, under active state conditions, a flux control coefficient of COX over oxidative phosphorylation of 0.24±0.07 and a 1.9±0.2-fold excess capacity in human skeletal muscle fibers. In human parahippocampal gyrus we determined, under similar conditions, a flux control coefficient of COX of 0.12±0.05 and a 3.9±0.6-fold excess capacity of the enzyme. The observed difference in metabolic control can be attributed to activity differences of COX in human brain and muscle mitochondria. Our results predict stronger metabolic effects of mild COX activity deficits in human skeletal muscle than in brain tissue.
Labels:
Organism: Human
Tissue;cell: Skeletal Muscle"Skeletal Muscle" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property., Neurons; Brain"Neurons; Brain" is not in the list (Heart, Skeletal muscle, Nervous system, Liver, Kidney, Lung;gill, Islet cell;pancreas;thymus, Endothelial;epithelial;mesothelial cell, Blood cells, Fat, ...) of allowed values for the "Tissue and cell" property.
Preparation: Permeabilized Cell or Tissue; Homogenate"Permeabilized Cell or Tissue; Homogenate" is not in the list (Intact organism, Intact organ, Permeabilized cells, Permeabilized tissue, Homogenate, Isolated mitochondria, SMP, Chloroplasts, Enzyme, Oxidase;biochemical oxidation, ...) of allowed values for the "Preparation" property.
Enzyme: Complex IV; Cytochrome c Oxidase"Complex IV; Cytochrome c Oxidase" is not in the list (Adenine nucleotide translocase, Complex I, Complex II;succinate dehydrogenase, Complex III, Complex IV;cytochrome c oxidase, Complex V;ATP synthase, Inner mt-membrane transporter, Marker enzyme, Supercomplex, TCA cycle and matrix dehydrogenases, ...) of allowed values for the "Enzyme" property.
HRR: Oxygraph-2k