Puchowicz 2004 Mitochondrion: Difference between revisions
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|enzymes=Inner mt-membrane transporter, TCA cycle and matrix dehydrogenases | |enzymes=Inner mt-membrane transporter, TCA cycle and matrix dehydrogenases | ||
|topics=Substrate | |topics=Substrate | ||
|couplingstates=OXPHOS | |couplingstates=OXPHOS | ||
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Revision as of 15:38, 15 June 2015
Puchowicz MA, Varnes ME, Cohen BH, Friedman NR, Kerr DS, Hoppel CL (2004) Oxidative phosphorylation analysis: assessing the integrated functional activity of human skeletal muscle mitochondria-case studies. Mitochondrion 4:377-85. |
Puchowicz MA, Varnes ME, Cohen BH, Friedman NR, Kerr DS, Hoppel CL (2004) Mitochondrion
Abstract: Oxidative phosphorylation analysis, performed on freshly-isolated mitochondria, assesses the integrated function of the electron transport chain (ETC) coupled to ATP synthesis, membrane transport, dehydrogenase activities, and the structural integrity of the mitochondria. In this review, a case study approach is employed to highlight detection of defects in the adenine nucleotide translocator, the pyruvate dehydrogenase complex, fumarase, coenzyme Q function, fatty acid metabolism, and mitochondrial membrane integrity. Our approach uses the substrates glutamate, pyruvate, 2-ketoglutarate (coupled with malonate), malate, and fatty acid substrates (palmitoylcarnitine, octanoylcarnitine, palmitoyl-CoA (with carnitine), octanoyl-CoA (with carnitine), octanoate and acetylcarnitine) in addition to succinate, durohydroquinone and TMPD/ascorbate to uncover metabolic defects that would not be apparent from ETC assays performed on detergent-solubilized mitochondria. โข Keywords: Oxidative phosphorylation; Skeletal muscle mitochondria; Adenine nucleotide translocator; Pyruvate dehydrogenase complex; Uncoupling; Carnitine palmitoyltransferase
โข O2k-Network Lab: US OH Cleveland Hoppel CL
Labels:
Organism: Human
Tissue;cell: Skeletal muscle
Preparation: Isolated mitochondria
Enzyme: Inner mt-membrane transporter, TCA cycle and matrix dehydrogenases
Regulation: Substrate
Coupling state: OXPHOS