Pecina 2004 Am J Physiol Cell Physiol: Difference between revisions
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{{Publication | {{Publication | ||
|title=Pecina P, Gnaiger E, Zeman J, Pronicka E, Houstek J (2004) Decreased affinity to oxygen of cytochrome c oxidase in Leigh syndrome caused by SURF1 mutations. Am J Physiol Cell Physiol 287: C1384- | |title=Pecina P, Gnaiger E, Zeman J, Pronicka E, Houstek J (2004) Decreased affinity to oxygen of cytochrome c oxidase in Leigh syndrome caused by SURF1 mutations. Am J Physiol Cell Physiol 287:C1384-8. | ||
|info=[http://www.ncbi.nlm.nih.gov/pubmed/15269007 PMID: 15269007] | |info=[http://www.ncbi.nlm.nih.gov/pubmed/15269007 PMID: 15269007 Open-Access] | ||
|authors=Pecina P, Gnaiger | |authors=Pecina P, Gnaiger Erich, Zeman J, Pronicka E, Houstek J | ||
|year=2004 | |year=2004 | ||
|journal=Am J Physiol Cell Physiol | |journal=Am J Physiol Cell Physiol | ||
|abstract=Mutations in the gene ''SURF1'' prevent synthesis of cytochrome-c oxidase (COX)-specific assembly protein and result in a fatal neurological disorder, Leigh syndrome. Because this severe COX deficiency presents with barely detectable changes of cellular respiratory rates under normoxic conditions, we analyzed the respiratory response to low oxygen in cultured fibroblasts harboring ''SURF1'' mutations with high-resolution respirometry. The oxygen kinetics was quantified by the partial pressure of oxygen (P<sub>O2</sub>) at half-maximal respiration rate (P<sub>50</sub>) in intact coupled cells and in digitonin-permeabilized uncoupled cells. In both cases, the P<sub>50</sub> in patients was elevated 2.1- and 3.3-fold, respectively, indicating decreased affinity of COX for oxygen. These results suggest that at physiologically low intracellular P<sub>O2</sub>, the depressed oxygen affinity may lead in vivo to limitations of respiration, resulting in impaired energy provision in Leigh syndrome patients. | |abstract=Mutations in the gene ''SURF1'' prevent synthesis of cytochrome-c oxidase (COX)-specific assembly protein and result in a fatal neurological disorder, Leigh syndrome. Because this severe COX deficiency presents with barely detectable changes of cellular respiratory rates under normoxic conditions, we analyzed the respiratory response to low oxygen in cultured fibroblasts harboring ''SURF1'' mutations with high-resolution respirometry. The oxygen kinetics was quantified by the partial pressure of oxygen (P<sub>O2</sub>) at half-maximal respiration rate (P<sub>50</sub>) in intact coupled cells and in digitonin-permeabilized uncoupled cells. In both cases, the P<sub>50</sub> in patients was elevated 2.1- and 3.3-fold, respectively, indicating decreased affinity of COX for oxygen. These results suggest that at physiologically low intracellular P<sub>O2</sub>, the depressed oxygen affinity may lead ''in vivo'' to limitations of respiration, resulting in impaired energy provision in Leigh syndrome patients. | ||
|keywords=Oxygen kinetics, Mitochondrial disease | |keywords=Oxygen kinetics, Mitochondrial disease | ||
|mipnetlab= | |mipnetlab=AT Innsbruck Gnaiger E, CZ Prague Zeman J, CZ Prague Houstek J | ||
}} | }} | ||
== Cited by == | |||
::* 10 articles in PubMed (2021-12-27) https://pubmed.ncbi.nlm.nih.gov/15269007/ | |||
{{Labeling | {{Labeling | ||
|area=Respiration, nDNA;cell genetics, mt-Medicine, Patients | |area=Respiration, nDNA;cell genetics, mt-Medicine, Patients | ||
|diseases=Inherited | |||
|organism=Human | |organism=Human | ||
| | |tissues=Fibroblast | ||
|preparations=Intact cells | |preparations=Intact cells | ||
|enzymes=Complex IV; | |enzymes=Complex IV;cytochrome c oxidase | ||
|topics=Oxygen kinetics | |||
|topics= | |||
|couplingstates=ROUTINE | |couplingstates=ROUTINE | ||
|instruments=Oxygraph-2k | |instruments=Oxygraph-2k | ||
}} | }} |
Latest revision as of 14:00, 27 December 2021
Pecina P, Gnaiger E, Zeman J, Pronicka E, Houstek J (2004) Decreased affinity to oxygen of cytochrome c oxidase in Leigh syndrome caused by SURF1 mutations. Am J Physiol Cell Physiol 287:C1384-8. |
Pecina P, Gnaiger Erich, Zeman J, Pronicka E, Houstek J (2004) Am J Physiol Cell Physiol
Abstract: Mutations in the gene SURF1 prevent synthesis of cytochrome-c oxidase (COX)-specific assembly protein and result in a fatal neurological disorder, Leigh syndrome. Because this severe COX deficiency presents with barely detectable changes of cellular respiratory rates under normoxic conditions, we analyzed the respiratory response to low oxygen in cultured fibroblasts harboring SURF1 mutations with high-resolution respirometry. The oxygen kinetics was quantified by the partial pressure of oxygen (PO2) at half-maximal respiration rate (P50) in intact coupled cells and in digitonin-permeabilized uncoupled cells. In both cases, the P50 in patients was elevated 2.1- and 3.3-fold, respectively, indicating decreased affinity of COX for oxygen. These results suggest that at physiologically low intracellular PO2, the depressed oxygen affinity may lead in vivo to limitations of respiration, resulting in impaired energy provision in Leigh syndrome patients. โข Keywords: Oxygen kinetics, Mitochondrial disease
โข O2k-Network Lab: AT Innsbruck Gnaiger E, CZ Prague Zeman J, CZ Prague Houstek J
Cited by
- 10 articles in PubMed (2021-12-27) https://pubmed.ncbi.nlm.nih.gov/15269007/
Labels: MiParea: Respiration, nDNA;cell genetics, mt-Medicine, Patients
Pathology: Inherited
Organism: Human Tissue;cell: Fibroblast Preparation: Intact cells Enzyme: Complex IV;cytochrome c oxidase Regulation: Oxygen kinetics Coupling state: ROUTINE
HRR: Oxygraph-2k