https://wiki.oroboros.at/api.php?action=feedcontributions&user=Biljana&feedformat=atomBioblast - User contributions [en]2024-03-29T14:13:28ZUser contributionsMediaWiki 1.36.1https://wiki.oroboros.at/index.php?title=Nuskova_2010_J_Bioenerg_Biomembr&diff=7321Nuskova 2010 J Bioenerg Biomembr2010-11-02T13:52:54Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Nůsková H, Vrbacký M, Drahota Z, Houštěk J (2010) Cyanide inhibition and pyruvate-induced recovery of cytochrome c oxidase. J. Bioenerg. Biomembr. DOI: 10.1007/s10863-010-9307-6. In press.<br />
|authors=Nuskova H, Vrbacky M, Drahota Z, Houštek J<br />
|year=2010<br />
|journal=J. Bioenerg. Biomembr.<br />
|abstract=The mechanism of cyanide’s inhibitory effect on the mitochondrial cytochrome c oxidase (COX) as well as the conditions for its recovery have not yet been fully explained. We investigated three parameters of COX function, namely electron transport (oxygen consumption), proton transport (mitochondrial membrane potential ''Δψ'' m) and the enzyme affinity to oxygen (''p<sub>50</sub>'' value) with regard to the inhibition by KCN and its reversal by pyruvate. 250 μM KCN completely inhibited both the electron and proton transport function of COX. The inhibition was reversible as demonstrated by washing of mitochondria. The addition of 60 mM pyruvate induced the maximal recovery of both parameters to 60–80% of the original values. When using low KCN concentrations of up to 5 μM, we observed a profound, 30-fold decrease of COX affinity for oxygen. Again, this decrease was completely reversed by washing mitochondria while pyruvate induced only a partial, yet significant recovery of oxygen affinity. Our results demonstrate that the inhibition of COX by cyanide is reversible and that the potential of pyruvate as a cyanide poisoning antidote is limited. Importantly, we also showed that the COX affinity for oxygen is the most sensitive indicator of cyanide toxic effects.<br />
|keywords=Rat liver mitochondria, Cytochrome c oxidase, Cyanide toxicity, Pyruvate antidote, ''p<sub>50</sub>''<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|enzymes=Complex IV; Cytochrome c Oxidase<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Nuskova_2010_J_Bioenerg_Biomembr&diff=7320Nuskova 2010 J Bioenerg Biomembr2010-11-02T13:52:10Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Nůsková H, Vrbacký M, Drahota Z, Houštěk J (2010) Cyanide inhibition and pyruvate-induced recovery of cytochrome c oxidase. J. Bioenerg. Biomembr. DOI: 10.1007/s10863-010-9307-6. In press.<br />
<br />
|authors=Nůsková H, Vrbacký M, Drahota Z, Houštěk J<br />
|year=2010<br />
|journal=J. Bioenerg. Biomembr.<br />
|abstract=The mechanism of cyanide’s inhibitory effect on the mitochondrial cytochrome c oxidase (COX) as well as the conditions for its recovery have not yet been fully explained. We investigated three parameters of COX function, namely electron transport (oxygen consumption), proton transport (mitochondrial membrane potential ''Δψ'' m) and the enzyme affinity to oxygen (''p<sub>50</sub>'' value) with regard to the inhibition by KCN and its reversal by pyruvate. 250 μM KCN completely inhibited both the electron and proton transport function of COX. The inhibition was reversible as demonstrated by washing of mitochondria. The addition of 60 mM pyruvate induced the maximal recovery of both parameters to 60–80% of the original values. When using low KCN concentrations of up to 5 μM, we observed a profound, 30-fold decrease of COX affinity for oxygen. Again, this decrease was completely reversed by washing mitochondria while pyruvate induced only a partial, yet significant recovery of oxygen affinity. Our results demonstrate that the inhibition of COX by cyanide is reversible and that the potential of pyruvate as a cyanide poisoning antidote is limited. Importantly, we also showed that the COX affinity for oxygen is the most sensitive indicator of cyanide toxic effects. <br />
|keywords=Rat liver mitochondria, Cytochrome c oxidase, Cyanide toxicity, Pyruvate antidote, ''p<sub>50</sub>'' <br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|enzymes=Complex IV; Cytochrome c Oxidase<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Nuskova_2010_J_Bioenerg_Biomembr&diff=7319Nuskova 2010 J Bioenerg Biomembr2010-11-02T13:50:12Z<p>Biljana: Created page with "{{Publication |title=Nůsková H, Vrbacký M, Drahota Z, Houštěk J (2010) Cyanide inhibition and pyruvate-induced recovery of cytochrome c oxidase. J. Bioenerg. Biomembr. DOI: ..."</p>
<hr />
<div>{{Publication<br />
|title=Nůsková H, Vrbacký M, Drahota Z, Houštěk J (2010) Cyanide inhibition and pyruvate-induced recovery of cytochrome c oxidase. J. Bioenerg. Biomembr. DOI: 10.1007/s10863-010-9307-6. In press.<br />
<br />
|authors=Nůsková H, Vrbacký M, Drahota Z, Houštěk J<br />
|year=2010<br />
|journal=J. Bioenerg. Biomembr.<br />
|abstract=The mechanism of cyanide’s inhibitory effect on the mitochondrial cytochrome c oxidase (COX) as well as the conditions for its recovery have not yet been fully explained. We investigated three parameters of COX function, namely electron transport (oxygen consumption), proton transport (mitochondrial membrane potential Δψ m) and the enzyme affinity to oxygen (p 50 value) with regard to the inhibition by KCN and its reversal by pyruvate. 250 μM KCN completely inhibited both the electron and proton transport function of COX. The inhibition was reversible as demonstrated by washing of mitochondria. The addition of 60 mM pyruvate induced the maximal recovery of both parameters to 60–80% of the original values. When using low KCN concentrations of up to 5 μM, we observed a profound, 30-fold decrease of COX affinity for oxygen. Again, this decrease was completely reversed by washing mitochondria while pyruvate induced only a partial, yet significant recovery of oxygen affinity. Our results demonstrate that the inhibition of COX by cyanide is reversible and that the potential of pyruvate as a cyanide poisoning antidote is limited. Importantly, we also showed that the COX affinity for oxygen is the most sensitive indicator of cyanide toxic effects. <br />
|keywords=Rat liver mitochondria, Cytochrome c oxidase, Cyanide toxicity, Pyruvate antidote, p 50 <br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|enzymes=Complex IV; Cytochrome c Oxidase<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Havlickova_2010_Biochim_Biophys_Acta&diff=7318Havlickova 2010 Biochim Biophys Acta2010-11-02T12:56:09Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2009) Knockdown of F1 epsilon subunit decreases mitochondrial content of ATP synthase 2 and leads to accumulation of subunit c. Biochimica et Biophysica Acta. 1797: 1124-1129.<br />
|authors=Havličkova V, Kaplanova V, Nuskova H, Drahota Z, Houštek J<br />
|year=2009<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=The subunit ε of mitochondrial ATP synthase is the only F1 subunit without a homolog in bacteria and chloroplasts and represents the least characterized F1 subunit of the mammalian enzyme. Silencing of the ''ATP5E'' gene in HEK293 cells resulted in downregulation of the activity and content of the mitochondrial ATP synthase complex and of ADP-stimulated respiration to approximately 40% of the control. The decreased content of the ε subunit was paralleled by a decrease in the F1 subunits α and β and in the Fo subunits a and d while the content of the subunit c was not affected. The subunit c was present in the full-size ATP synthase complex and in subcomplexes of 200–400 kDa that neither contained the F1 subunits, nor the Fo subunits. The results indicate that the ε subunit is essential for the assembly of F1 and plays an important role in the incorporation of the hydrophobic subunit c into the F1-c oligomer rotor of the mitochondrial ATP synthase complex.<br />
|keywords=Mitochondria, ATP synthase, Epsilon subunit, C subunit, Biogenesis<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|enzymes=Complex V; ATP Synthase<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Havlickova_2010_Biochim_Biophys_Acta&diff=7317Havlickova 2010 Biochim Biophys Acta2010-11-02T12:53:32Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2009) Knockdown of F1 epsilon subunit decreases mitochondrial content of ATP synthase 2 and leads to accumulation of subunit c. Biochimica et Biophysica Acta. 1797: 1124-1129.<br />
|authors=Havličkova V, Kaplanova V, Nůskova H, Drahota Z, Houštek J<br />
|year=2009<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=The subunit ε of mitochondrial ATP synthase is the only F1 subunit without a homolog in bacteria and chloroplasts and represents the least characterized F1 subunit of the mammalian enzyme. Silencing of the ''ATP5E'' gene in HEK293 cells resulted in downregulation of the activity and content of the mitochondrial ATP synthase complex and of ADP-stimulated respiration to approximately 40% of the control. The decreased content of the ε subunit was paralleled by a decrease in the F1 subunits α and β and in the Fo subunits a and d while the content of the subunit c was not affected. The subunit c was present in the full-size ATP synthase complex and in subcomplexes of 200–400 kDa that neither contained the F1 subunits, nor the Fo subunits. The results indicate that the ε subunit is essential for the assembly of F1 and plays an important role in the incorporation of the hydrophobic subunit c into the F1-c oligomer rotor of the mitochondrial ATP synthase complex.<br />
|keywords=Mitochondria, ATP synthase, Epsilon subunit, C subunit, Biogenesis<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|enzymes=Complex V; ATP Synthase<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Havlickova_2010_Biochim_Biophys_Acta&diff=7316Havlickova 2010 Biochim Biophys Acta2010-11-02T12:51:44Z<p>Biljana: Created page with "{{Publication |title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2009) Knockdown of F1 epsilon subunit decreases mitochondrial content of ATP synthase 2 a..."</p>
<hr />
<div>{{Publication<br />
|title=Havlíčková V, Kaplanová V, Nůsková H, Drahota Z, Houštěk J (2009) Knockdown of F1 epsilon subunit decreases mitochondrial content of ATP synthase 2 and leads to accumulation of subunit c. Biochimica et Biophysica Acta. 1797: 1124-1129.<br />
|authors=Havličkova V, Kaplanova V, Nůskova H, Drahota Z, Houštek J<br />
|year=2009<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=The subunit ε of mitochondrial ATP synthase is the only F1 subunit without a homolog in bacteria and chloroplasts and represents the least characterized F1 subunit of the mammalian enzyme. Silencing of the ATP5E gene in HEK293 cells resulted in downregulation of the activity and content of the mitochondrial ATP synthase complex and of ADP-stimulated respiration to approximately 40% of the control. The decreased content of the ε subunit was paralleled by a decrease in the F1 subunits α and β and in the Fo subunits a and d while the content of the subunit c was not affected. The subunit c was present in the full-size ATP synthase complex and in subcomplexes of 200–400 kDa that neither contained the F1 subunits, nor the Fo subunits. The results indicate that the ε subunit is essential for the assembly of F1 and plays an important role in the incorporation of the hydrophobic subunit c into the F1-c oligomer rotor of the mitochondrial ATP synthase complex.<br />
|keywords=Mitochondria, ATP synthase, Epsilon subunit, c subunit, Biogenesis<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|enzymes=Complex V; ATP Synthase<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cizkova_2008_Nat_Genet&diff=7315Cizkova 2008 Nat Genet2010-11-02T12:38:59Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S (2008) TMEM70 mutations cause isolated ATP synthase deficiency and neonatal mitochondrial encephalocardiomyopathy. Nature Gen. 40(11): 1288-1290.<br />
<br />
|authors=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S<br />
|year=2008<br />
|journal=Nature Gen.<br />
|abstract=We carried out whole-genome homozygosity mapping, gene<br />
expression analysis and DNA sequencing in individuals with<br />
isolated mitochondrial ATP synthase deficiency and identified<br />
disease-causing mutations in ''TMEM70''. Complementation of the<br />
cell lines of these individuals with wild-type ''TMEM70'' restored<br />
biogenesis and metabolic function of the enzyme complex. Our<br />
results show that ''TMEM70'' is involved in mitochondrial ATP<br />
synthase biogenesis in higher eukaryotes.<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|preparations=Isolated Mitochondria<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cizkova_2008_Nat_Genet&diff=7314Cizkova 2008 Nat Genet2010-11-02T12:38:41Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S (2008) TMEM70 mutations cause isolated ATP synthase deficiency and neonatal mitochondrial encephalocardiomyopathy. Nature Gen. 40(11): 1288-1290.<br />
<br />
|authors=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S<br />
|year=2008<br />
|journal=Nature Gen.<br />
|abstract=We carried out whole-genome homozygosity mapping, gene<br />
expression analysis and DNA sequencing in individuals with<br />
isolated mitochondrial ATP synthase deficiency and identified<br />
disease-causing mutations in ''TMEM70''. Complementation of the<br />
cell lines of these individuals with wild-type ''TMEM70'' restored<br />
biogenesis and metabolic function of the enzyme complex. Our<br />
results show that TMEM70 is involved in mitochondrial ATP<br />
synthase biogenesis in higher eukaryotes.<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|preparations=Isolated Mitochondria<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cizkova_2008_Nat_Genet&diff=7313Cizkova 2008 Nat Genet2010-11-02T12:38:17Z<p>Biljana: Created page with "{{Publication |title=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honz..."</p>
<hr />
<div>{{Publication<br />
|title=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S (2008) TMEM70 mutations cause isolated ATP synthase deficiency and neonatal mitochondrial encephalocardiomyopathy. Nature Gen. 40(11): 1288-1290.<br />
<br />
|authors=Cızkova A, Stranecky V, Mayr JA, Tesarova M, Havlıckova V, Paul J, Ivanek R, Kuss AW, Hansıkova H, Kaplanova W, Vrbacky M, Hartmannova H, Noskova L, Honzık T, Drahota Z, Magner M, Hejzlarova K, Sperl W, Zeman J, Houstek J, Kmoch S<br />
|year=2008<br />
|journal=Nature Gen.<br />
|abstract=We carried out whole-genome homozygosity mapping, gene<br />
expression analysis and DNA sequencing in individuals with<br />
isolated mitochondrial ATP synthase deficiency and identified<br />
disease-causing mutations in TMEM70. Complementation of the<br />
cell lines of these individuals with wild-type TMEM70 restored<br />
biogenesis and metabolic function of the enzyme complex. Our<br />
results show that TMEM70 is involved in mitochondrial ATP<br />
synthase biogenesis in higher eukaryotes.<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|preparations=Isolated Mitochondria<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Nat_Genet&diff=7312Nat Genet2010-11-02T12:33:48Z<p>Biljana: Created page with "{{Journal |Title=Nature Gen. }}"</p>
<hr />
<div>{{Journal<br />
|Title=Nature Gen.<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Aragones_2008_Nat_Genet&diff=7311Aragones 2008 Nat Genet2010-11-02T12:33:21Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Aragonés J, Schneider M, Van Geyte K, Fraisl P, Dresselaers T, Mazzone M, Dirkx R, Zacchigna S, Lemieux H, Jeoung NH, Lambrechts D, Bishop T, Lafuste P, Diez-Juan A, K Harten S, Van Noten P, De Bock K, Willam C, Tjwa M, Grosfeld A, Navet R, Moons L, Vandendriessche T, Deroose C, Wijeyekoon B, Nuyts J, Jordan B, Silasi-Mansat R, Lupu F, Dewerchin M, Pugh C, Salmon P, Mortelmans L, Gallez B, Gorus F, Buyse J, Sluse F, Harris RA, Gnaiger E, Hespel P, Van Hecke P, Schuit F, Van Veldhoven P, Ratcliffe P, Baes M, Maxwell P, Carmeliet P (2008) Deficiency or inhibition of oxygen sensor Phd1 induces hypoxia tolerance by reprogramming basal metabolism. Nature Genetics 40: 170-180.<br />
|authors=Aragones J, Schneider M, Van Geyte K, Fraisl P, Dresselaers T, Mazzone M, Dirkx R, Zacchigna S, Lemieux H, Jeoung NH, Lambrechts D, Bishop T, Lafuste P, Diez-Juan A, K Harten S, Van Noten P, De Bock K, Willam C, Tjwa M, Grosfeld A, Navet R, Moons L, Vandendriessche T, Deroose C, Wijeyekoon B, Nuyts J, Jordan B, Silasi-Mansat R, Lupu F, Dewerchin M, Pugh C, Salmon P, Mortelmans L, Gallez B, Gorus F, Buyse J, Sluse F, Harris RA, Gnaiger E, Hespel P, Van Hecke P, Schuit F, Van Veldhoven P, Ratcliffe P, Baes M, Maxwell P, Carmeliet P<br />
|year=2008<br />
|journal=Nature Gen.<br />
|mipnetlab=AT_Innsbruck_GnaigerE<br />
|abstract=HIF prolyl hydroxylases (PHD1-3) are oxygen sensors that regulate the stability of the hypoxia-inducible factors (HIFs) in an oxygen-dependent manner. Here, we show that loss of Phd1 lowers oxygen consumption in skeletal muscle by reprogramming glucose metabolism from oxidative to more anaerobic ATP production through activation of a Pparα pathway. This metabolic adaptation to oxygen conservation impairs oxidative muscle performance in healthy conditions, but it provides acute protection of myofibers against lethal ischemia. Hypoxia tolerance is not due to HIF-dependent angiogenesis, erythropoiesis or vasodilation, but rather to reduced generation of oxidative stress, which allows Phd1-deficient myofibers to preserve mitochondrial respiration. Hypoxia tolerance relies primarily on Hif-2α and was not observed in heterozygous Phd2-deficient or homozygous Phd3-deficient mice. Of medical importance, conditional knockdown of Phd1 also rapidly induces hypoxia tolerance. These findings delineate a new role of Phd1 in hypoxia tolerance and offer new treatment perspectives for disorders characterized by oxidative stress.<br />
|keywords=Oxygen stress, Hypoxia tolerance<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18176562 PMID: 18176562]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology, Biomedicine<br />
|injuries=Hypoxia, Ischemia-Reperfusion; Preservation, RONS; Oxidative Stress<br />
|organism=Mouse<br />
|tissues=Skeletal Muscle<br />
|preparations=Permeabilized Cell or Tissue; Homogenate<br />
|topics=Respiration; OXPHOS; ETS Capacity, Flux Control; Additivity; Threshold; Excess Capacity, Coupling; Membrane Potential, Mitochondrial Biogenesis; Mitochondrial Density, Aerobic and Anaerobic Metabolism, Substrate; Glucose; TCA Cycle<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Samper_2009_Free_Radic_Biol_Med&diff=7305Samper 2009 Free Radic Biol Med2010-11-02T10:28:18Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S (2009) Increase in mitochondrial biogenesis, oxidative stress, and glycolysis in murine lymphomas. Free Radical Biology and Medicine 46 (3): 387-396.<br />
|authors=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S<br />
|year=2009<br />
|journal=Free Radical Biol. Med.<br />
|abstract=Lymphomas adapt to their environment by undergoing a complex series of biochemical changes that are<br />
currently not well understood. To better define these changes, we examined the gene expression and gene<br />
ontology profiles of thymic lymphomas from a commonly used model of carcinogenesis, the p53−/− mouse.<br />
These tumors show a highly significant upregulation of mitochondrial biogenesis, mitochondrial protein<br />
translation, mtDNA copy number, reactive oxygen species, antioxidant defenses, proton transport, ATP<br />
synthesis, hypoxia response, and glycolysis, indicating a fundamental change in the bioenergetic profile of<br />
the transformed T cell. Our results suggest that T cell tumorigenesis involves a simultaneous upregulation of<br />
mitochondrial biogenesis, mitochondrial respiration, and glycolytic activity. These processes would allow<br />
cells to adapt to the stressful tumor environment by facilitating energy production and thereby promote<br />
tumor growth. Understanding these adaptations is likely to result in improved therapeutic strategies for this<br />
tumor type.<br />
|keywords=Mitochondria, Reactive oxygen species, Glycolysis, Lymphoma, p53, c-myc, Free radicals<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19038329 PMID: 19038329]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=RONS; Oxidative Stress, Genetic Defect; Knockdown; Overexpression<br />
|topics=Respiration; OXPHOS; ETS Capacity, Mitochondrial Biogenesis; Mitochondrial Density<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Samper_2008_FRBM&diff=7304Samper 2008 FRBM2010-11-02T10:23:33Z<p>Biljana: moved Samper 2008 FRBM to Samper 2009 FRBM</p>
<hr />
<div>#REDIRECT [[Samper 2009 FRBM]]</div>Biljanahttps://wiki.oroboros.at/index.php?title=Samper_2009_Free_Radic_Biol_Med&diff=7303Samper 2009 Free Radic Biol Med2010-11-02T10:23:33Z<p>Biljana: moved Samper 2008 FRBM to Samper 2009 FRBM</p>
<hr />
<div>{{Publication<br />
|title=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S (2008) Increase in mitochondrial biogenesis, oxidative stress, and glycolysis in murine lymphomas. Free Radical Biology and Medicine 46 (3): 387-396.<br />
|authors=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S<br />
|year=2008<br />
|journal=Free Radical Biol. Med.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19038329 PMID: 19038329]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Kupsch_2009_FEBS_J&diff=7298Kupsch 2009 FEBS J2010-11-02T09:37:51Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Kupsch K, Hertel S, Kreutzmann P, Wolf G, Wallesch CW, Siemen D, Schönfeld P (2009) Impairment of mitochondrial function by minocycline. FEBS J. 276: 1729–1738.<br />
|authors=Kupsch K, Hertel S, Kreutzmann P, Wolf G, Wallesch CW, Siemen D, Schoenfeld P<br />
|year=2009<br />
|journal=FEBS J.<br />
|abstract=There is an ongoing debate on the presence of beneficial effects of minocycline<br />
(MC), a tetracycline-like antibiotic, on the preservation of mitochondrial<br />
functions under conditions promoting mitochondria-mediated<br />
apoptosis. Here, we present a multiparameter study on the effects of MC<br />
on isolated rat liver mitochondria (RLM) suspended either in a KCl-based<br />
or in a sucrose-based medium. We found that the incubation medium used<br />
strongly affects the response of RLM to MC. In KCl-based medium, but<br />
not in sucrose-based medium, MC triggered mitochondrial swelling and<br />
cytochrome c release. MC-dependent swelling was associated with mitochondrial<br />
depolarization and a decrease in state 3 as well as uncoupled<br />
respiration. Swelling of RLM in KCl-based medium indicates that MC permeabilizes<br />
the inner mitochondrial membrane (IMM) to K<sup>+</sup> and Cl). This<br />
view is supported by our findings that MC-induced swelling in the KClbased<br />
medium was partly suppressed by N,N¢-dicyclohexylcarbodiimide (an<br />
inhibitor of IMM-linked K<sup>+</sup>-transport) and tributyltin (an inhibitor of the<br />
inner membrane anion channel) and that swelling was less pronounced<br />
when RLM were suspended in choline chloride-based medium. In addition,<br />
we observed a rapid MC-induced depletion of endogenous Mg<sup>2+</sup> from<br />
RLM, an event that is known to activate ion-conducting pathways within<br />
the IMM. Moreover, MC abolished the Ca<sup>2+</sup> retention capacity of RLM<br />
irrespective of the incubation medium used, most likely by triggering permeability<br />
transition. In summary, we found that MC at low micromolar<br />
concentrations impairs several energy-dependent functions of mitochondria<br />
''in vitro''.<br />
|keywords=Magnesium, Minocycline, Mitochondria, Neuroprotection, Permeability transition<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|injuries=Cancer; Apoptosis; Cytochrome c<br />
|organism=Rat<br />
|tissues=Hepatocyte; Liver<br />
|preparations=Isolated Mitochondria<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Kupsch_2009_FEBS_J&diff=7297Kupsch 2009 FEBS J2010-11-02T09:32:05Z<p>Biljana: Created page with "{{Publication |title=Kupsch K, Hertel S, Kreutzmann P, Wolf G, Wallesch CW, Siemen D, Schönfeld P (2009) Impairment of mitochondrial function by minocycline. FEBS J. 276: 1729..."</p>
<hr />
<div>{{Publication<br />
|title=Kupsch K, Hertel S, Kreutzmann P, Wolf G, Wallesch CW, Siemen D, Schönfeld P (2009) Impairment of mitochondrial function by minocycline. FEBS J. 276: 1729–1738.<br />
|authors=Kupsch K, Hertel S, Kreutzmann P, Wolf G, Wallesch CW, Siemen D, Schoenfeld P<br />
|year=2009<br />
|journal=FEBS J.<br />
|abstract=There is an ongoing debate on the presence of beneficial effects of minocycline<br />
(MC), a tetracycline-like antibiotic, on the preservation of mitochondrial<br />
functions under conditions promoting mitochondria-mediated<br />
apoptosis. Here, we present a multiparameter study on the effects of MC<br />
on isolated rat liver mitochondria (RLM) suspended either in a KCl-based<br />
or in a sucrose-based medium. We found that the incubation medium used<br />
strongly affects the response of RLM to MC. In KCl-based medium, but<br />
not in sucrose-based medium, MC triggered mitochondrial swelling and<br />
cytochrome c release. MC-dependent swelling was associated with mitochondrial<br />
depolarization and a decrease in state 3 as well as uncoupled<br />
respiration. Swelling of RLM in KCl-based medium indicates that MC permeabilizes<br />
the inner mitochondrial membrane (IMM) to K+ and Cl). This<br />
view is supported by our findings that MC-induced swelling in the KClbased<br />
medium was partly suppressed by N,N¢-dicyclohexylcarbodiimide (an<br />
inhibitor of IMM-linked K+-transport) and tributyltin (an inhibitor of the<br />
inner membrane anion channel) and that swelling was less pronounced<br />
when RLM were suspended in choline chloride-based medium. In addition,<br />
we observed a rapid MC-induced depletion of endogenous Mg2+ from<br />
RLM, an event that is known to activate ion-conducting pathways within<br />
the IMM. Moreover, MC abolished the Ca2+ retention capacity of RLM<br />
irrespective of the incubation medium used, most likely by triggering permeability<br />
transition. In summary, we found that MC at low micromolar<br />
concentrations impairs several energy-dependent functions of mitochondria<br />
in vitro.<br />
|keywords=Magnesium, Minocycline, Mitochondria, Neuroprotection, Permeability transition<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|injuries=Cancer; Apoptosis; Cytochrome c<br />
|organism=Rat<br />
|tissues=Hepatocyte; Liver<br />
|preparations=Isolated Mitochondria<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cheng_2010_FEBS_Lett&diff=7256Cheng 2010 FEBS Lett2010-10-29T16:29:02Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Cheng Y, Debska-Vielhaber G, Siemen D (2010) Interaction of mitochondrial potassium channels with the permeability transition pore. FEBS Letters 584: 2005–2012.<br />
|authors=Cheng Y, Debska-Vielhaber G, Siemen D<br />
|year=2010<br />
|journal=FEBS Lett.<br />
|abstract=Three types of potassium channels cooperate with the permeability transition pore (PTP) in the<br />
inner mitochondrial membranes of various tissues, mtK(ATP), mtBK, and mtKv1.3. While the latter<br />
two share similarities with their plasma membrane counterparts, mtK(ATP) exhibits considerable differences<br />
with the plasma membrane K<sub>(ATP)</sub>-channel. One important function seems to be suppression<br />
of release of proapototic substances from mitochondria through the PTP. Open potassium<br />
channels tend to keep the PTP closed thus acting as antiapoptotic. Nevertheless, in their mode of<br />
action there are considerable differences among them. This review introduces three K<sup>+</sup>-channels<br />
and the PTP, and discusses known facts about their interaction.<br />
|keywords=Mitochondria Ion channel, Permeability transition pore, Apoptosis, Mitochondrial potassium channel<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Cancer; Apoptosis; Cytochrome c<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cheng_2010_FEBS_Lett&diff=7255Cheng 2010 FEBS Lett2010-10-29T16:27:40Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Cheng Y, Debska-Vielhaber G, Siemen D (2010) Interaction of mitochondrial potassium channels with the permeability transition pore. FEBS Letters 584: 2005–2012.<br />
|authors=Cheng Y, Debska-Vielhaber G, Siemen D<br />
|year=2010<br />
|journal=FEBS Lett.<br />
|abstract=Three types of potassium channels cooperate with the permeability transition pore (PTP) in the<br />
inner mitochondrial membranes of various tissues, mtK(ATP), mtBK, and mtKv1.3. While the latter<br />
two share similarities with their plasma membrane counterparts, mtK(ATP) exhibits considerable differences<br />
with the plasma membrane K<sub>ATP</sub>-channel. One important function seems to be suppression<br />
of release of proapototic substances from mitochondria through the PTP. Open potassium<br />
channels tend to keep the PTP closed thus acting as antiapoptotic. Nevertheless, in their mode of<br />
action there are considerable differences among them. This review introduces three K<sup>+</sup>-channels<br />
and the PTP, and discusses known facts about their interaction.<br />
|keywords=Mitochondria Ion channel, Permeability transition pore, Apoptosis, Mitochondrial potassium channel<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Cancer; Apoptosis; Cytochrome c<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Cheng_2010_FEBS_Lett&diff=7254Cheng 2010 FEBS Lett2010-10-29T16:25:59Z<p>Biljana: Created page with "{{Publication |title=Cheng Y, Debska-Vielhaber G, Siemen D (2010) Interaction of mitochondrial potassium channels with the permeability transition pore. FEBS Letters 584: 2005–..."</p>
<hr />
<div>{{Publication<br />
|title=Cheng Y, Debska-Vielhaber G, Siemen D (2010) Interaction of mitochondrial potassium channels with the permeability transition pore. FEBS Letters 584: 2005–2012.<br />
|authors=Cheng Y, Debska-Vielhaber G, Siemen D<br />
|year=2010<br />
|journal=FEBS Lett.<br />
|abstract=Three types of potassium channels cooperate with the permeability transition pore (PTP) in the<br />
inner mitochondrial membranes of various tissues, mtK(ATP), mtBK, and mtKv1.3. While the latter<br />
two share similarities with their plasma membrane counterparts, mtK(ATP) exhibits considerable differences<br />
with the plasma membrane K(ATP)-channel. One important function seems to be suppression<br />
of release of proapototic substances from mitochondria through the PTP. Open potassium<br />
channels tend to keep the PTP closed thus acting as antiapoptotic. Nevertheless, in their mode of<br />
action there are considerable differences among them. This review introduces three K+-channels<br />
and the PTP, and discusses known facts about their interaction.<br />
|keywords=Mitochondria Ion channel, Permeability transition pore, Apoptosis, Mitochondrial potassium channel<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Cancer; Apoptosis; Cytochrome c<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Rorbach_2008_Nucleic_Acids_Res&diff=6964Rorbach 2008 Nucleic Acids Res2010-10-20T15:10:00Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kühl I, Gaisne M, Bonnefoy N, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZM (2008) The human mitochondrial ribosome recycling factor is essential for cell viability. Nucleic Acids Res. 36: 5787-5799.<br />
|authors=Rorbach J, Richter R, Wessels HJ, Wydro M, Pekalski M, Farhoud M, Kuehl I, Gaisne M, Bonnefoy N, Smeitink JA, Lightowlers RN, Chrzanowska-Lightowlers ZM<br />
|year=2008<br />
|journal=Nucleic Acids Res.<br />
|abstract=The molecular mechanism of human mitochondrial<br />
translation has yet to be fully described. We are particularly<br />
interested in understanding the process of<br />
translational termination and ribosome recycling in<br />
the mitochondrion. Several candidates have been<br />
implicated, for which subcellular localization and<br />
characterization have not been reported. Here,<br />
we show that the putative mitochondrial recycling<br />
factor, mtRRF, is indeed a mitochondrial protein.<br />
Expression of human mtRRF in fission yeast<br />
devoid of endogenous mitochondrial recycling<br />
factor suppresses the respiratory phenotype. Further,<br />
human mtRRF is able to associate with ''Escherichia<br />
coli'' ribosomes ''in vitro'' and can associate with<br />
mitoribosomes ''in vivo''. Depletion of mtRRF in<br />
human cell lines is lethal, initially causing profound<br />
mitochondrial dysmorphism, aggregation of mitoribosomes,<br />
elevated mitochondrial superoxide production<br />
and eventual loss of OXPHOS complexes.<br />
Finally, mtRRF was shown to co-immunoprecipitate<br />
a large number of mitoribosomal proteins attached<br />
to other mitochondrial proteins, including<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18782833 PMID: 18782833]<br />
}}<br />
{{Labeling<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|organism=Human, Bacteria<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Rostovtseva_2008_Proc_Natl_Acad_Sci_U_S_A&diff=6897Rostovtseva 2008 Proc Natl Acad Sci U S A2010-10-20T13:34:20Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Rostovtseva TK, Sheldon KL, Hassanzadeh E, Monge C, Saks V, Bezrukov SM, Sackett DL (2008) Tubulin binding blocks mitochondrial voltage-dependent anion channel and regulates respiration. Proc. Natl. Acad. Sci. USA 105: 18746-18751.<br />
|authors=Rostovtseva TK, Sheldon KL, Hassanzadeh E, Monge C, Saks V, Bezrukov SM, Sackett DL<br />
|year=2008<br />
|journal=Proc. Natl. Acad. Sci.<br />
|abstract=Regulation of mitochondrial outer membrane (MOM) permeability<br />
has dual importance: in normal metabolite and energy exchange<br />
between mitochondria and cytoplasm and thus in control of respiration,<br />
and in apoptosis by release of apoptogenic factors into the<br />
cytosol. However, the mechanism of this regulation, dependent on<br />
the voltage-dependent anion channel (VDAC), the major channel of<br />
MOM, remains controversial. A long-standing puzzle is that in permeabilized<br />
cells, adenine nucleotide translocase (ANT) is less accessible<br />
to cytosolic ADP than in isolated mitochondria. We solve this<br />
puzzle by finding a missing player in the regulation of MOM permeability:<br />
the cytoskeletal protein tubulin. We show that nanomolar<br />
concentrations of dimeric tubulin induce voltage-sensitive reversible<br />
closure of VDAC reconstituted into planar phospholipid membranes.<br />
Tubulin strikingly increases VDAC voltage sensitivity and at physiological<br />
salt conditions could induce VDAC closure at <10 mV transmembrane<br />
potentials. Experiments with isolated mitochondria confirm these<br />
findings. Tubulin added to isolated mitochondria decreases<br />
ADP availability to ANT, partially restoring the low MOM permeability<br />
(high apparent Km for ADP) found in permeabilized cells. Our findings<br />
suggest a previously unknown mechanism of regulation of mitochondrial<br />
energetics, governed by VDAC and tubulin at the mitochondria–<br />
cytosol interface. This tubulin–VDAC interaction requires tubulin<br />
anionic C-terminal tail (CTT) peptides. The significance of this interaction<br />
may be reflected in the evolutionary conservation of length<br />
and anionic charge in CTT throughout eukaryotes, despite wide<br />
changes in the exact sequence. Additionally, tubulins that have lost<br />
significant length or anionic character are only found in cells that do<br />
not have mitochondria.<br />
|keywords=Evolution, Microtubules, Oxidative phosphorylation, VDAC, Tubulin C-terminal<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19033201 PMID: 19033201]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology, Biomedicine<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=J_Acquir_Immune_Defic_Syndr&diff=6896J Acquir Immune Defic Syndr2010-10-20T13:33:49Z<p>Biljana: Created page with "{{Journal |Title=J. Acquir. Immune Defic. Syndr. }}"</p>
<hr />
<div>{{Journal<br />
|Title=J. Acquir. Immune Defic. Syndr.<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Saillan-Barreau_2008_J_Acquir_Immune_Defic_Syndr&diff=6895Saillan-Barreau 2008 J Acquir Immune Defic Syndr2010-10-20T13:33:25Z<p>Biljana: Created page with "{{Publication |title=Saillan-Barreau C, Tabbakh O, Chavoin JP, Casteilla L, Pénicaud L (2008) Drug-specific effect of nelfinavir and stavudine on primary culture of human preadi..."</p>
<hr />
<div>{{Publication<br />
|title=Saillan-Barreau C, Tabbakh O, Chavoin JP, Casteilla L, Pénicaud L (2008) Drug-specific effect of nelfinavir and stavudine on primary culture of human preadipocytes. J. Acquir. Immune Defic. Syndr. 48: 20-25.<br />
|authors=Saillan-Barreau C, Tabbakh O, Chavoin JP, Casteilla L, Penicaud L <br />
|year=2008<br />
|journal=J. Acquir. Immune Defic. Syndr.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18344876 PMID: 18344876]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Samper_2009_Free_Radic_Biol_Med&diff=6891Samper 2009 Free Radic Biol Med2010-10-20T13:32:08Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S (2008) Increase in mitochondrial biogenesis, oxidative stress, and glycolysis in murine lymphomas. Free Radical Biology and Medicine 46 (3): 387-396.<br />
|authors=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S<br />
|year=2008<br />
|journal=Free Radical Biol. Med.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19038329 PMID: 19038329]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Skalska_2008_Biochim_Biophys_Acta&diff=6887Skalska 2008 Biochim Biophys Acta2010-10-20T13:31:10Z<p>Biljana: Created page with "{{Publication |title=Skalska J, Piwonska M, Wyroba E, Surmacz L, Wieczorek R, Koszela-Piotrowska I, Zielinska J, Bednarczyk P, Dolowy K, Wilczynski GM, Szewczyk A, Kunz WS (2008)..."</p>
<hr />
<div>{{Publication<br />
|title=Skalska J, Piwonska M, Wyroba E, Surmacz L, Wieczorek R, Koszela-Piotrowska I, Zielinska J, Bednarczyk P, Dolowy K, Wilczynski GM, Szewczyk A, Kunz WS (2008) A novel potassium channel in skeletal muscle mitochondria. Biochim. Biophys. Acta 1777: 651-659.<br />
|authors=Skalska J, Piwonska M, Wyroba E, Surmacz L, Wieczorek R, Koszela-Piotrowska I, Zielinska J, Bednarczyk P, Dolowy K, Wilczynski GM, Szewczyk A, Kunz WS <br />
|year=2008<br />
|journal=Biochim. Biophys. Acta <br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18515063 PMID: 18515063]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Samper_2009_Free_Radic_Biol_Med&diff=6885Samper 2009 Free Radic Biol Med2010-10-20T13:30:20Z<p>Biljana: Created page with "{{Publication |title=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S (2008) Increase in mitochondrial biogenesis, oxidative stress, and glycolysis in mur..."</p>
<hr />
<div>{{Publication<br />
|title=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S (2008) Increase in mitochondrial biogenesis, oxidative stress, and glycolysis in murine lymphomas. Free Radical Biology and Medicine 46 (3): 387-396.<br />
|authors=Samper E, Morgado L, Estrada JC, Bernad A, Hubbard A, Cadenas S, Melov S <br />
|year=2008<br />
|journal=Free Radical Biol. Med.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19038329 PMID: 19038329]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Unterluggauer_2008_Biotechnol_J&diff=6877Unterluggauer 2008 Biotechnol J2010-10-20T13:26:43Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Unterluggauer H, Hütter E, Viertler HP, Jansen-Dürr P (2008) Insulin-like growth factor-induced signals activate mitochondrial respiration. J. Biotechnol. 3: 813-816.<br />
|authors=Unterluggauer H, Huetter E, Viertler HP, Jansen-Duerr P<br />
|year=2008<br />
|journal=J. Biotechnol. <br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18383021 PMID: 18383021]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Unterluggauer_2008_Biotechnol_J&diff=6875Unterluggauer 2008 Biotechnol J2010-10-20T13:25:40Z<p>Biljana: Created page with "{{Publication |title=Unterluggauer H, Hütter E, Viertler HP, Jansen-Dürr P (2008) Insulin-like growth factor-induced signals activate mitochondrial respiration. Biotechnol. J. ..."</p>
<hr />
<div>{{Publication<br />
|title=Unterluggauer H, Hütter E, Viertler HP, Jansen-Dürr P (2008) Insulin-like growth factor-induced signals activate mitochondrial respiration. Biotechnol. J. 3: 813-816. <br />
|authors=Unterluggauer H, Huetter E, Viertler HP, Jansen-Duerr P <br />
|year=2008<br />
|journal=Biotechnol. J.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18383021 PMID: 18383021]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Vanasco_2008_Free_Radic_Res&diff=6872Vanasco 2008 Free Radic Res2010-10-20T13:24:06Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Vanasco V, Cimolai MC, Evelson P, Alvarez S (2008) The oxidative stress and the mitochondrial dysfunction caused by endotoxemia are prevented by -lipoic acid. Free Radic. Res. 42(9): 815-823<br />
|authors=Vanasco V, Cimolai MC, Evelson P, Alvarez S<br />
|year=2008<br />
|journal=Free Radical Res.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19051079 PMID: 19051079]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Vanasco_2008_Free_Radic_Res&diff=6869Vanasco 2008 Free Radic Res2010-10-20T13:23:48Z<p>Biljana: Created page with "{{Publication |title=Vanasco V, Cimolai MC, Evelson P, Alvarez S (2008) The oxidative stress and the mitochondrial dysfunction caused by endotoxemia are prevented by -lipoic acid..."</p>
<hr />
<div>{{Publication<br />
|title=Vanasco V, Cimolai MC, Evelson P, Alvarez S (2008) The oxidative stress and the mitochondrial dysfunction caused by endotoxemia are prevented by -lipoic acid. Free Radic. Res. 42(9): 815-823<br />
|authors=Vanasco V, Cimolai MC, Evelson P, Alvarez S <br />
|year=2008<br />
|journal=Free Radic. Res.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19051079 PMID: 19051079]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Wijers_2008_PLoS_One&diff=6866Wijers 2008 PLoS One2010-10-20T13:22:21Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Wijers SL, Schrauwen P, Saris WH, van Marken Lichtenbelt WD (2008) Human skeletal muscle mitochondrial uncoupling is associated with cold induced adaptive thermogenesis. PLoS ONE 12 3 (3): e1777.<br />
|authors=Wijers SL, Schrauwen P, Saris WH, van Marken Lichtenbelt WD<br />
|year=2008<br />
|journal=PLoS One<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18335051 PMID: 18335051 ]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Wijers_2008_PLoS_One&diff=6865Wijers 2008 PLoS One2010-10-20T13:21:58Z<p>Biljana: Created page with "{{Publication |title=Wijers SL, Schrauwen P, Saris WH, van Marken Lichtenbelt WD (2008) Human skeletal muscle mitochondrial uncoupling is associated with cold induced adaptive th..."</p>
<hr />
<div>{{Publication<br />
|title=Wijers SL, Schrauwen P, Saris WH, van Marken Lichtenbelt WD (2008) Human skeletal muscle mitochondrial uncoupling is associated with cold induced adaptive thermogenesis. PLoS ONE 12 3 (3): e1777.<br />
|authors=Wijers SL, Schrauwen P, Saris WH, van Marken Lichtenbelt WD <br />
|year=2008<br />
|journal= PLoS ONE<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/18335051 PMID: 18335051 ]<br />
}}<br />
{{Labeling<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Vrbacky_2007_Biochim_Biophys_Acta&diff=6864Vrbacky 2007 Biochim Biophys Acta2010-10-20T13:20:46Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Vrbacky M, Drahota Z, Mracek T, Vojtískova A, Jesina P, Stopka P, Houstek J (2007) Respiratory chain components involved in the glycerophosphate dehydrogenase-dependent ROS production by brown adipose tissue mitochondria. Biochim. Biophys. Acta. 1767 (7): 989-97.<br />
|authors=Vrbacky M, Drahota Z, Mracek T, Vojtiskova A, Jesina P, Stopka P, Houstek J<br />
|year=2007<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=Involvement of mammalian mitochondrial glycerophosphate dehydrogenase (mGPDH, EC 1.1.99.5) in reactive oxygen species (ROS) generation was studied in brown adipose tissue mitochondria by different spectroscopic techniques. Spectrofluorometry using ROS-sensitive probes CM-H<sub>2</sub> DCFDA and Amplex Red was used to determine the glycerophosphate- or succinate-dependent ROS production in mitochondria supplemented with respiratory chain inhibitors antimycin A and myxothiazol. In case of glycerophosphate oxidation, most of the ROS originated directly from mGPDH and coenzyme Q while complex III was a typical site of ROS production in succinate oxidation. Glycerophosphate-dependent ROS production monitored by KCN-insensitive oxygen consumption was highly activated by one-electron acceptor ferricyanide, whereas succinate-dependent ROS production was unaffected. In addition, superoxide anion radical was detected as a mGPDH-related primary ROS species by fluorescent probe dihydroethidium, as well as by electron paramagnetic resonance (EPR) spectroscopy with DMPO spin trap. Altogether, the data obtained demonstrate pronounced differences in the mechanism of ROS production originating from oxidation of glycerophosphate and succinate indicating that electron transfer from mGPDH to coenzyme Q is highly prone to electron leak and superoxide generation.<br />
|keywords=Brown adipose tissue mitochondria, Glycerophosphate dehydrogenase, Reactive oxygen species, Fluorescent probes, Oxygraphy, EPR<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17560536 PMID: 17560536]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology, Biomedicine<br />
|organism=Other Mammal<br />
|enzymes=Complex III<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential, Ion Homeostasis<br />
|instruments=Oxygraph-2k, Spectrophotometry; Spectrofluorimetry<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Tokarska-Schlattner_2007_Biochim_Biophys_Acta&diff=6860Tokarska-Schlattner 2007 Biochim Biophys Acta2010-10-20T13:18:45Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Tokarska-Schlattner M, Dolder M, Gerber I, Speer O, Wallimann T, Schlattner U (2007) Reduced creatine-stimulated respiration in doxorubicin challenged mitochondria: particular sensitivity of the heart. Biochim. Biophys. Acta 1767: 1276-1284.<br />
|authors=Tokarska-Schlattner M, Dolder M, Gerber I, Speer O, Wallimann T, Schlattner U<br />
|year=2007<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=Doxorubicin (DXR) belongs to the most efficient anticancer drugs. However, its use is limited by a risk of cardiotoxicity, which is not completely understood. Recently, we have shown that DXR impairs essential properties of purified mitochondrial creatine kinase (MtCK), with cardiac isoenzyme (sMtCK) being particularly sensitive. In this study we assessed the effects of DXR on respiration of isolated structurally and functionally intact heart mitochondria, containing sMtCK, in the presence and absence of externally added creatine (Cr), and compared these effects with the response of brain mitochondria expressing uMtCK, the ubiquitous, non-muscle MtCK isoenzyme. DXR impaired respiration of isolated heart mitochondria already after short-term exposure (minutes), affecting both ADP- and Cr-stimulated respiration. During a first short time span (minutes to 1 h), detachment of MtCK from membranes occurred, while a decrease of MtCK activity related to oxidative damage was only observed after longer exposure (several hours). The early inhibition of Cr-stimulated respiration, in addition to impairment of components of the respiratory chain involves a partial disturbance of functional coupling between MtCK and ANT, likely due to interaction of DXR with cardiolipin leading to competitive inhibition of MtCK/membrane binding. The relevance of these findings for the regulation of mitochondrial energy production in the heart, as well as the obvious differences of DXR action in the heart as compared to brain tissue, is discussed.<br />
|keywords=Anthracycline, Creatine kinase, Cardiotoxicity, Isolated mitochondria, Creatine-simulated respiration<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17935690 PMID: 17935690]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine, Pharmacology; Biotechnology<br />
|injuries=Mitochondrial Disease; Degenerative Disease and Defect<br />
|organism=Human<br />
|tissues=Cardiac Muscle, Neurons; Brain<br />
|preparations=Isolated Mitochondria, Enzyme<br />
|kinetics=ADP; Pi, Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Severina_2007_Biochim_Biophys_Acta&diff=6846Severina 2007 Biochim Biophys Acta2010-10-20T13:13:54Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Severina II, Vyssokikh MY, Pustovidko AV, Simonyan RA, Rokitskaya TI, Skulachev VP (2007) Effects of lipophilic dications on planar bilayer phospholipid membrane and mitochondria. Biochim Biophys Acta. 1767: 1164-1168.<br />
|authors=Severina II, Vyssokikh MY, Pustovidko AV, Simonyan RA, Rokitskaya TI, Skulachev VP<br />
|year=2007<br />
|journal=Biochim. Biophys. Acta<br />
|abstract=In this paper, we studied effects of phosphonium dications P2C5 and P2C10 on bilayer planar phospholipid membrane (BLM) and rat liver mitochondria. In line with our previous observations [M.F. Ross, T. Da Ros, F.H. Blaikie, T.A. Prime, C.M. Porteous, I.I. Severina, V.P. Skulachev, H.G. Kjaergaard, R.A. Smith, M.P. Murphy, Accumulation of lipophilic dications by mitochondria and cells, Biochem. J. 400 (2006) 199–208], we showed both P2C5 and P2C10 are cationic penetrants for BLM. They generated transmembrane diffusion potential (ΔΨ), the compartment with a lower dication concentration positive. However, the ΔΨ values measured proved to be lower that the Nernstian. This fact could be explained by rather low BLM conductance for the cations at their small concentrations and by induction of some BLM damage at their large concentrations. The damage in question consisted in appearance of non-Ohmic current/voltage relationships which increased in time. Such a non-Ohmicity was especially strong at ΔΨ > 100 mV. Addition of penetrating lipophilic anion TPB, which increases the BLM conductance for lipophilic cations, yielded the Nernstian ΔΨ, i.e. 30 mV per ten-fold dication gradient. In the State 4 mitochondria, dications stimulated respiration and lowered ΔΨ. Moreover, they inhibited the State 3 respiration with succinate or glutamate and malate (but not with TMPD and ascorbate) in an uncoupler-sensitive fashion. Effect on the in State 4 mitochondria, similarly to that on BLM, was accounted for by a time-dependent membrane damage. On the other hand, the State 3 effect was most probably due to inhibition of the respiratory chain Complex I and/or Complex III. The damaging and inhibitory activities of lipophilic dications should be taken into account when one considers a possibility to use them as a vehicle to target antioxidants or other compounds to mitochondria.<br />
|keywords=Dication, Lipophilic cation, Planar phospholipids membrane, Mitochondria, Membrane potential, Damaging effect<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17692814 PMID: 17692814]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|injuries=RONS; Oxidative Stress<br />
|organism=Rat<br />
|tissues=Hepatocyte; Liver<br />
|preparations=Isolated Mitochondria<br />
|enzymes=Complex I, Complex III<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential, Ion Homeostasis<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Schneider_2007_Cell_Biol_Int&diff=6836Schneider 2007 Cell Biol Int2010-10-20T13:04:34Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Schneider N, Mouithys-Mickalad A, Lejeune JP, Duyckaerts C, Sluse F, Deby-Dupont G, Serteyn D (2007) Oxygen consumption of equine articular chondrocytes: Influence of applied oxygen tension and glucose concentration during culture. Cell. Biol. Int. 31: 878-886.<br />
|authors=Schneider N, Mouithys-Mickalad A, Lejeune JP, Duyckaerts C, Sluse F, Deby-Dupont G, Serteyn D<br />
|year=2007<br />
|journal=Cell. Biol. Int.<br />
|abstract=We investigated the oxygen (O<sub>2</sub>) uptake of equine articular chondrocytes to assess their reactions to anoxia/re-oxygenation. They were cultured under 5% or 21% gas phase O<sub>2</sub> and at glucose concentrations of 0, 1.0 or 4.5g/L in the culture medium (n=3). Afterwards, the O<sub>2</sub> consumption rate of the chondrocytes was monitored (oxymetry) before and after an anoxia period of 25min. The glucose consumption and lactate release were measured at the end of the re-oxygenation period. The chondrocytes showed a minimal O<sub>2</sub> consumption rate, which was hardly changed by anoxia. Independently from the O<sub>2</sub> tension, glucose uptake by the cells was about 30% of the available culture medium glucose, thus higher for cells at 4.5g/L glucose (n=3). Lactate release was also independent from O<sub>2</sub> tension, but lower for cells at 4.5g/L glucose (n=3). Our observations indicated that O<sub>2</sub> consumption by equine chondrocytes was very low despite a functional mitochondrial respiratory chain, and nearly insensitive to anoxia/re-oxygenation. But the chondrocytes metabolism was modified by an excess of O<sub>2</sub> and glucose.<br />
|keywords=Chondrocytes, Anoxia, Lactate, Glucose<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17442596 PMID: 17442596]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|injuries=Hypoxia, RONS; Oxidative Stress<br />
|organism=Other Mammal<br />
|kinetics=Oxygen<br />
|topics=Respiration; OXPHOS; ETS Capacity, Substrate; Glucose; TCA Cycle<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Rodriguez-Juarez_2007_Biochem_J&diff=6834Rodriguez-Juarez 2007 Biochem J2010-10-20T13:03:29Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Rodriguez-Juarez F, Aguirre E, Cadenas S (2007) Relative sensitivity of soluble guanylate cyclase and mitochondrial respiration to endogenous nitric oxide at physiological oxygen concentration. Biochem. J. 405: 223-231.<br />
|authors=Rodriguez-Juarez F, Aguirre E, Cadenas S <br />
|year=2007<br />
|journal=Biochem. J.<br />
|abstract=Disposition of the second messenger nitric oxide (NO) in mammalian tissues occurs through multiple pathways including dioxygenation by erythrocyte hemoglobin and red muscle myoglobin. Metabolism by a putative NO dioxygenase activity in non-striated tissues has also been postulated, but the exact nature of this activity is unknown. In the present study, we tested the hypothesis that cytoglobin, a newly discovered hexacoordinated globin, participates in cell-mediated NO consumption. Stable expression of small hairpin RNA targeting cytoglobin in fibroblasts resulted in decreased NO consumption and intracellular nitrate production. These cells were more sensitive to NO-induced inhibition of cell respiration and proliferation, which could be restored by re-expression of human cytoglobin. We also demonstrated cytoglobin expression in adventitial fibroblasts as well as vascular smooth muscle cells from various species including human and found that cytoglobin was expressed in the adventitia and media of intact rat aorta. These results indicate that cytoglobin contributes to cell-mediated NO dioxygenation and represents an important NO sink in the vascular wall.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17441787 PMID: 17441787]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Rat<br />
|tissues=Skeletal Muscle, Blood Cell; Suspension Culture<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Pasdois_2007_Am_J_Physiol_Heart_Circ_Physiol&diff=6825Pasdois 2007 Am J Physiol Heart Circ Physiol2010-10-20T13:01:07Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Pasdois P, Quinlan CL, Rissa A, Tariosse L, Vinassa B, Costa AD, Pierre SV, Dos Santos P, Garlid KD (2007) Ouabain protects rat hearts against ischemia-reperfusion injury via pathway involving src kinase, mitoKATP, and ROS. Am. J. Physiol. Heart Circ. Physiol. 292: H1470- H1478.<br />
|authors=Pasdois P, Quinlan CL, Rissa A, Tariosse L, Vinassa B, Costa AD, Pierre SV, Dos Santos P, Garlid KD<br />
|year=2007<br />
|journal=Am. J. Physiol. Heart Circ. Physiol.<br />
|abstract=We showed recently that mitochondrial ATP-dependent K<sup>+</sup> channel (mitoK<sub>ATP</sub>) opening is required for the inotropic response to ouabain. Because mitoK<sub>ATP</sub> opening is also required for most forms of cardioprotection, we investigated whether exposure to ouabain was cardioprotective. We also began to map the signaling pathways linking ouabain binding to Na<sup>+</sup>-K<sup>+</sup>-ATPase with the opening of mitoK<sub>ATP</sub>. In Langendorff-perfused rat hearts, 10-80 µM ouabain given before the onset of ischemia resulted in cardioprotection against ischemia-reperfusion injury, as documented by an improved recovery of contractile function and a reduction of infarct size. In skinned cardiac fibers, a ouabain-induced protection of mitochondrial outer membrane integrity, adenine nucleotide compartmentation, and energy transfer efficiency was evidenced by a decreased release of cytochrome ''c'' and preserved half-saturation constant of respiration for ADP and adenine nucleotide translocase-mitochondrial creatine kinase coupling, respectively. Ouabain-induced positive inotropy was dose dependent over the range studied, whereas ouabain-induced cardioprotection was maximal at the lowest dose tested. Compared with bradykinin (BK)-induced preconditioning, ouabain was equally efficient. However, the two ligands clearly diverge in the intracellular steps leading to mitoK<sub>ATP</sub> opening from their respective receptors. Thus BK-induced cardioprotection was blocked by inhibitors of cGMP-dependent protein kinase (PKG) or guanylyl cyclase (GC), whereas ouabain-induced protection was not blocked by either agent. Interestingly, however, ouabain-induced inotropy appears to require PKG and GC. Thus 5-hydroxydecanoate (a selective mitoK<sub>ATP</sub> inhibitor), N-(2-mercaptopropionyl)glycine (MPG; a reactive oxygen species scavenger), ODQ (a GC inhibitor), PP2 (a src kinase inhibitor), and KT-5823 (a PKG inhibitor) abolished preconditioning by BK and blocked the inotropic response to ouabain. However, only PP2, 5-HD, and MPG blocked ouabain-induced cardioprotection.<br />
|keywords=Na<sup>+</sup>-K<sup>+</sup>-ATPase, Inotropy, Bradykinin, Signaling pathway, Reactive oxygen species<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17098831 PMID: 17098831]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine, Pharmacology; Biotechnology<br />
|injuries=Ischemia-Reperfusion; Preservation<br />
|organism=Rat<br />
|tissues=Cardiac Muscle<br />
|preparations=Intact Organ<br />
|enzymes=Complex IV; Cytochrome c Oxidase, Inner mtMembrane Transporter<br />
|kinetics=Reduced Substrate; Cytochrome c<br />
|topics=Respiration; OXPHOS; ETS Capacity, Aerobic and Anaerobic Metabolism<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Paillard_2009_J_Mol_Cell_Cardiol&diff=6819Paillard 2009 J Mol Cell Cardiol2010-10-20T12:59:15Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Paillard M, Gomez L, Augeul L, Loufouat J, Lesnefsky EJ, Ovize M (2009) Postconditioning inhibits mPTP opening independent of oxidative phosphorylation and membrane potential. J. Mol. Cell Cardiol. 46: 902-909.<br />
|authors=Paillard M, Gomez L, Augeul L, Loufouat J, Lesnefsky EJ, Ovize M<br />
|year=2009<br />
|journal=J. Mol. Cell. Cardiol.<br />
|abstract=Mitochondrial permeability transition pore (mPTP) inhibition plays a relevant role in postconditioning (PostC). Ischemia damages the electron transport chain, and the potential contribution of additional modifications in mitochondrial function caused by PostC remains unknown. We sought to determine which mitochondrial functions are involved in the inhibition of mPTP opening during the first minutes of reperfusion. Anesthetized New Zealand White rabbits underwent 30-min ischemia followed by 10-min reperfusion. At reperfusion, they received either no intervention (Control, C), PostC with 4 cycles of 1-min ischemia followed by 1-min reperfusion, or an IV injection of 5 mg/kg cyclosporine A (CsA: a powerful inhibitor of mPTP opening). Sham rabbits underwent no ischemia throughout the 40-min experiment. At the end of the 10-min reperfusion, mitochondria were isolated from the area at risk by differential centrifugations. Calcium retention capacity (CRC) and mitochondrial membrane potential (ΔΨm) were assessed by fluorimetry in subsarcolemmal (SSM) and interfibrillar (IFM) mitochondria. Oxidative phosphorylation was assessed using a Clark-type electrode, and oxidative stress via protein carbonylation by Western blotting. PostC and CsA treatments improved CRC when compared to the C group. Control, PostC and CsA mitochondria exhibited a comparable significant dissipation of ΔΨm, together with a comparable significant decrease in state 3 and an increase in state 4 respiration, in both SSM and IFM. However, PostC but not CsA treatment reduced total heart oxidative stress. These data suggest that during the early minutes of reperfusion, PostC reduces oxidative stress and inhibits mPTP opening, independent of alteration of oxidative phosphorylation or of ΔΨm.<br />
|keywords=Oxidative phosphorylation, Mitochondria, Postconditioning, Ischemia, Reperfusion, Cardioprotection<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/19254723 PMID: 19254723]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology, Biomedicine<br />
|injuries=Ischemia-Reperfusion; Preservation, RONS; Oxidative Stress<br />
|organism=Other Mammal<br />
|enzymes=Inner mtMembrane Transporter<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential, Ion Homeostasis<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Pasdois_2007_J_Mol_Cell_Cardiol&diff=6817Pasdois 2007 J Mol Cell Cardiol2010-10-20T12:57:14Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Pasdois P, Beauvoit B, Costa AD, Vinassa B, Tariosse L, Bonoron-Adèle S, Garlid KD, Dos Santos P (2007) Sarcoplasmic ATP-sensitive potassium channel blocker HMR1098 protects the ischemic heart: implication of calcium, complex I, reactive oxygen species and mitochondrial ATP-sensitive potassium channel. J. Mol. Cell. Cardiol. 42: 631-642.<br />
|authors=Pasdois P, Beauvoit B, Costa AD, Vinassa B, Tariosse L, Bonoron-Adele S, Garlid KD, Dos Santos P<br />
|year=2007<br />
|journal=J. Mol. Cell. Cardiol.<br />
|abstract=The aim of this study was to investigate the effects of HMR1098, a selective blocker of sarcolemmal ATP-sensitive potassium channel (sarcKATP), in Langendorff-perfused rat hearts submitted to ischemia and reperfusion. The recovery of heart hemodynamic and mitochondrial function, studied on skinned fibers, was analyzed after 30-min global ischemia followed by 20-min reperfusion. Infarct size was quantified on a regional ischemia model after 2-h reperfusion. We report that the perfusion of 10 μM HMR1098 before ischemia, delays the onset of ischemic contracture, improves recovery of cardiac function upon reperfusion, preserves the mitochondrial architecture, and finally decreases infarct size. This HMR1098-induced cardioprotection is prevented by 1 mM 2-mercaptopropionylglycine, an antioxidant, and by 100 nM nifedipine, an L-type calcium channel blocker. Concomitantly, it is shown that HMR1098 perfusion induces (i) a transient and specific inhibition of the respiratory chain complex I and, (ii) an increase in the averaged intracellular calcium concentration probed by the in situ measurement of indo-1 fluorescence. Finally, all the beneficial effects of HMR1098 were strongly inhibited by 5-hydroxydecanoate and abolished by glibenclamide, two mitoKATP blockers. This study demonstrates that the HMR1098-induced cardioprotection occurs indirectly through extracellular calcium influx, respiratory chain complex inhibition, reactive oxygen species production and mitoKATP opening. Taken together, these data suggest that a functional interaction between sarcKATP and mitoKATP exists in isolated rat heart ischemia model, which is mediated by extracellular calcium influx.<br />
|keywords=Heart, schemia, Cardioprotection, Skinned fibers, Potassium channels<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17306295 PMID: 17306295]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Ischemia-Reperfusion; Preservation, RONS; Oxidative Stress, Cancer; Apoptosis; Cytochrome c<br />
|organism=Human<br />
|tissues=Cardiac Muscle<br />
|enzymes=Complex I<br />
|topics=Respiration; OXPHOS; ETS Capacity, Ion Homeostasis<br />
|instruments=Oxygraph-2k, Method<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=IEEE&diff=6816IEEE2010-10-20T12:55:46Z<p>Biljana: Created page with "{{Journal |Title=IEEE }}"</p>
<hr />
<div>{{Journal<br />
|Title=IEEE<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Kuhnt_2007_Neurochem_Res&diff=6814Kuhnt 2007 Neurochem Res2010-10-20T12:52:53Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Kuhnt T, Pelz T, Qu X, Haensgen G, Dunst J, Gellerich F (2007) Mitochondrial OXPHOS functions in R1H rhabdomyosarcoma and skeletal muscles of the rat. Neurochem Res 32:973–980.<br />
|authors=Kuhnt T, Pelz T, Qu X, Haensgen G, Dunst J, Gellerich F<br />
|year=2007<br />
|journal=Neurochem. Res.<br />
|abstract=The aim of the study was to determinate mitochondrial oxidative phosphorylation (OXPHOS) functions in rat rhabdomyosarcoma R1H (R1H) and rat skeletal muscles. For that purpose skinned fiber technique and multiple substrate inhibitor titration were adapted to tumor samples. In our animal tumor model (R1H) functional abnormalities of OXPHOS were found compared to skeletal muscles. In R1H the state 3 respiration of pyruvate + malate was decreased: 0.56 ± 0.28 nmol O<sub>2</sub>/mg/min versus 2.32 ± 1.19 nmol O<sub>2</sub>/mg/min, P < 0.001, whereas the state 3 respiration of succinate + rotenone was increased: 36 ± 14% versus 19 ± 11%, P < 0.001. In R1H the rotenone-insensitive respiration reached higher levels than the antimycin A-insensitive respiration, whereas in normal muscles the converse was observed. Additionally, the obvious difference between the CAT- and the antimycin A-independent respiration indicates an increased part of leak respiration in R1H. By now, the high feasibility of these techniques is appreciated for the investigation of muscles and prospectively for tumors, too.<br />
|keywords=Mitochondria, OXPHOS functions, Skinned fiber technique, High-resolution respirometry, Multiple substrate inhibitor titration, Rat rhabdomyosarcoma R1H<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17273927 PMID: 17273927 ]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Cancer; Apoptosis; Cytochrome c, Genetic Defect; Knockdown; Overexpression<br />
|organism=Rat<br />
|tissues=Skeletal Muscle<br />
|preparations=Permeabilized Cell or Tissue; Homogenate<br />
|topics=Respiration; OXPHOS; ETS Capacity, Substrate; Glucose; TCA Cycle<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Kuhnt_2007_Neurochem_Res&diff=6813Kuhnt 2007 Neurochem Res2010-10-20T12:51:28Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Kuhnt T, Pelz T, Qu X, Haensgen G, Dunst J, Gellerich F (2007) Mitochondrial OXPHOS functions in R1H rhabdomyosarcoma and skeletal muscles of the rat. Neurochem Res 32:973–980.<br />
|authors=Kuhnt T, Pelz T, Qu X, Haensgen G, Dunst J, Gellerich F<br />
|year=2007<br />
|journal=Neurochem. Res.<br />
|abstract=The aim of the study was to determinate mitochondrial oxidative phosphorylation (OXPHOS) functions in rat rhabdomyosarcoma R1H (R1H) and rat skeletal muscles. For that purpose skinned fiber technique and multiple substrate inhibitor titration were adapted to tumor samples. In our animal tumor model (R1H) functional abnormalities of OXPHOS were found compared to skeletal muscles. In R1H the state 3 respiration of pyruvate + malate was decreased: 0.56 ± 0.28 nmol O2/mg/min versus 2.32 ± 1.19 nmol O2/mg/min, P < 0.001, whereas the state 3 respiration of succinate + rotenone was increased: 36 ± 14% versus 19 ± 11%, P < 0.001. In R1H the rotenone-insensitive respiration reached higher levels than the antimycin A-insensitive respiration, whereas in normal muscles the converse was observed. Additionally, the obvious difference between the CAT- and the antimycin A-independent respiration indicates an increased part of leak respiration in R1H. By now, the high feasibility of these techniques is appreciated for the investigation of muscles and prospectively for tumors, too.<br />
|keywords=Mitochondria, OXPHOS functions, Skinned fiber technique, High-resolution respirometry, Multiple substrate inhibitor titration, Rat rhabdomyosarcoma R1H<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17273927 PMID: 17273927 ]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=Cancer; Apoptosis; Cytochrome c, Genetic Defect; Knockdown; Overexpression<br />
|organism=Rat<br />
|tissues=Skeletal Muscle<br />
|preparations=Permeabilized Cell or Tissue; Homogenate<br />
|topics=Respiration; OXPHOS; ETS Capacity, Substrate; Glucose; TCA Cycle<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Krivakova_2007_Physiol_Res&diff=6802Krivakova 2007 Physiol Res2010-10-20T12:23:48Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Krivakova P, Labajova A, Cervinkova Z, Drahota Z (2007) Inhibitory effect of t-butyl hydroperoxide on mitochondrial oxidative phosphorylation in isolated rat hepatocytes. Physiol Res. 56: 137-140.<br />
|authors=Krivakova P, Labajova A, Cervinkova Z, Drahota Z<br />
|year=2007<br />
|journal=Physiol. Res.<br />
|abstract=Using high-resolution oxygraphy, we tested the changes of various parameters characterizing the mitochondrial energy provision system that were induced by peroxidative damage. In the presence of succinate as respiratory substrate, 3 mM<br />
t-butyl hydroperoxide increased respiration in the absence of ADP, which indicated partial uncoupling of oxidative phosphorylation. Low activity of coupled respiration was still maintained as indicated by the ADP-activated and<br />
oligomycin-inhibited respiration. However, during the incubation the phosphorylative capacity decreased as indicated by the continuous decrease of the mitochondrial membrane potential. Under these experimental conditions the<br />
maximum capacity of the succinate oxidase system was inhibited by 50 % in comparison with values obtained in the absence of t-butyl hydroperoxide. Our data thus indicate that the oxygraphic evaluation of mitochondrial function<br />
represents a useful tool for evaluation of changes participating in peroxidative damage of cell energy metabolism.<br />
|keywords=Hepatocytes, Oxidative phosphorylation, t-Butyl hydroperoxide<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17381246 PMID: 17381246]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Rat<br />
|enzymes=Complex I, Complex II; Succinate Dehydrogenase, Uncoupler Protein<br />
|kinetics=ADP; Pi, Oxygen, Reduced Substrate; Cytochrome c<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential, Ion Homeostasis<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=Koenitzer_2007_Am_J_Physiol_Heart_Circ_Physiol&diff=6801Koenitzer 2007 Am J Physiol Heart Circ Physiol2010-10-20T12:23:08Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Koenitzer JR, Isbell TS, Patel HD, Benavides GA, Dickinson DA, Patel RP, Darley-Usmar VM, Lancaster JR Jr, Doeller JE, Kraus DW (2007) Hydrogen sulfide mediates vasoactivity in an O2-dependent manner. Am. J. Physiol. Heart Circ. Physiol. 292: H1953-1960.<br />
|authors=Koenitzer JR, Isbell TS, Patel HD, Benavides GA, Dickinson DA, Patel RP, Darley-Usmar VM, Lancaster JR Jr, Doeller JE, Kraus DW<br />
|year=2007<br />
|journal=Am. J. Physiol. Heart Circ. Physiol.<br />
|abstract=Hydrogen sulfide (H<sub>2</sub>S) has recently been shown to have a signaling role in vascular cells. Similar to nitric oxide (NO), H<sub>2</sub>S is enzymatically produced by amino acid metabolism and can cause posttranslational modification of proteins, particularly at thiol residues. Molecular targets for H<sub>2</sub>S include ATP-sensitive K+ channels, and H<sub>2</sub>S may interact with NO and heme proteins such as cyclooxygenase. It is well known that the reactions of NO in the vasculature are O<sub>2</sub> dependent, but this has not been addressed in most studies designed to elucidate the role of H<sub>2</sub>S in vascular function. This is important, since H<sub>2</sub>S reactions can be dramatically altered by the high concentrations of O2 used in cell culture and organ bath experiments. To test the hypothesis that the effects of H2S on the vasculature are O<sub>2</sub> dependent, we have measured real-time levels of H<sub>2</sub>S and O<sub>2</sub> in respirometry and vessel tension experiments, as well as the associated vascular responses. A novel polarographic H<sub>2</sub>S sensor developed in our laboratory was used to measure H<sub>2</sub>S levels. Here we report that, in rat aorta, H<sub>2</sub>S concentrations that mediate rapid contraction at high O<sub>2</sub> levels cause rapid relaxation at lower physiological O<sub>2</sub> levels. At high O<sub>2</sub>, the vasoconstrictive effect of H2S suggests that it may not be H<sub>2</sub>S per se but, rather, a putative vasoactive oxidation product that mediates constriction. These data are interpreted in terms of the potential for H<sub>2</sub>S to modulate vascular tone ''in vivo.''<br />
|keywords=Aorta, Sulfide sensor, Oxygen consumption, Vasorelaxation, Mitochondria<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17237242 PMID: 17237242]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology, Biomedicine<br />
|injuries=Genetic Defect; Knockdown; Overexpression<br />
|organism=Rat<br />
|tissues=Blood Cell; Suspension Culture<br />
|preparations=Permeabilized Cell or Tissue; Homogenate<br />
|enzymes=Inner mtMembrane Transporter, Marker Enzyme<br />
|topics=Respiration; OXPHOS; ETS Capacity<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljanahttps://wiki.oroboros.at/index.php?title=MiPNet10.04_CellRespiration&diff=6800MiPNet10.04 CellRespiration2010-10-20T12:20:30Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Garedew A, Haffner B, Huetter E, Gnaiger E. An experiment with high-resolution respirometry: Phosphorylation control in cell respiration. Mitochondr. Physiol. Network 10.04.<br />
|authors=Garedew A, Haffner B, Huetter E, Gnaiger E<br />
|year=*<br />
|mipnetlab=AT_Innsbruck_OROBOROS<br />
|abstract=Methodological and conceptual features of highresolution respirometry are illustrated in an experiment with cultured, suspended cells in the OROBOROS<br />
Oxygraph-2k (O2k). The experiment demonstrates manual titrations of inhibitors, and automatic titrations of an uncoupler using the electronic Titration-Injection microPump TIP2k. Application of the DatLab 4.3 (upgraded) software is shown for instrumental control (O2k and TIP2k), and on-line data analysis. The following guideline describes the experiment in the form of a laboratory protocol, complementary to the relevant sections of the Oxygraph-2k Manual. The experiments were carried out by participants of an O2k-Course on high-resolution respirometry in April 2005 (IOC30; Schröcken, Austria).<br />
|info=[http://www.oroboros.at/index.php?id=protocols_cell_hrr_pc MiPNet10.04]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Mouse<br />
|tissues=Blood Cell; Suspension Culture<br />
|preparations=Intact Cell; Cultured; Primary<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k, TIP2k, DatLab Software; Separate Application, Method<br />
|articletype=Protocol; Manual, MiPNet-online Publication<br />
}}<br />
[[Category:OroboroPedia]]</div>Biljanahttps://wiki.oroboros.at/index.php?title=MiPNet10.04_CellRespiration&diff=6799MiPNet10.04 CellRespiration2010-10-20T12:19:15Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Garedew A, Haffner B, Huetter E, Gnaiger E. An experiment with high-resolution respirometry: Phosphorylation control in cell respiration. Mitochondr. Physiol. Network 10.04.<br />
|authors=Garedew A, Haffner B, Huetter E, Gnaiger E<br />
|year=*<br />
|journal=Mitochondr. Physiol. Network 10.04.<br />
|mipnetlab=AT_Innsbruck_OROBOROS<br />
|abstract=Methodological and conceptual features of highresolution respirometry are illustrated in an experiment with cultured, suspended cells in the OROBOROS<br />
Oxygraph-2k (O2k). The experiment demonstrates manual titrations of inhibitors, and automatic titrations of an uncoupler using the electronic Titration-Injection microPump TIP2k. Application of the DatLab 4.3 (upgraded) software is shown for instrumental control (O2k and TIP2k), and on-line data analysis. The following guideline describes the experiment in the form of a laboratory protocol, complementary to the relevant sections of the Oxygraph-2k Manual. The experiments were carried out by participants of an O2k-Course on high-resolution respirometry in April 2005 (IOC30; Schröcken, Austria).<br />
|info=[http://www.oroboros.at/index.php?id=protocols_cell_hrr_pc MiPNet10.04]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Mouse<br />
|tissues=Blood Cell; Suspension Culture<br />
|preparations=Intact Cell; Cultured; Primary<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k, TIP2k, DatLab Software; Separate Application, Method<br />
|articletype=Protocol; Manual, MiPNet-online Publication<br />
}}<br />
[[Category:OroboroPedia]]</div>Biljanahttps://wiki.oroboros.at/index.php?title=MiPNet10.04_CellRespiration&diff=6798MiPNet10.04 CellRespiration2010-10-20T12:18:45Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Garedew A, Haffner B, Huetter E, Gnaiger E. An experiment with high-resolution respirometry: Phosphorylation control in cell respiration. Mitochondr. Physiol. Network 10.04.<br />
|authors=Garedew A, Haffner B, Huetter E, Gnaiger E<br />
|year=*<br />
|mipnetlab=AT_Innsbruck_OROBOROS<br />
|abstract=Methodological and conceptual features of highresolution respirometry are illustrated in an experiment with cultured, suspended cells in the OROBOROS<br />
Oxygraph-2k (O2k). The experiment demonstrates manual titrations of inhibitors, and automatic titrations of an uncoupler using the electronic Titration-Injection microPump TIP2k. Application of the DatLab 4.3 (upgraded) software is shown for instrumental control (O2k and TIP2k), and on-line data analysis. The following guideline describes the experiment in the form of a laboratory protocol, complementary to the relevant sections of the Oxygraph-2k Manual. The experiments were carried out by participants of an O2k-Course on high-resolution respirometry in April 2005 (IOC30; Schröcken, Austria).<br />
|info=[http://www.oroboros.at/index.php?id=protocols_cell_hrr_pc MiPNet10.04]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Mouse<br />
|tissues=Blood Cell; Suspension Culture<br />
|preparations=Intact Cell; Cultured; Primary<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k, TIP2k, DatLab Software; Separate Application, Method<br />
|articletype=Protocol; Manual, MiPNet-online Publication<br />
}}<br />
[[Category:OroboroPedia]]</div>Biljanahttps://wiki.oroboros.at/index.php?title=MiPNet10.04_CellRespiration&diff=6797MiPNet10.04 CellRespiration2010-10-20T12:16:37Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Garedew A, Haffner B, Hütter E, Gnaiger E. An experiment with high-resolution respirometry: Phosphorylation control in cell respiration. Mitochondr. Physiol. Network 10.04.<br />
|authors=Garedew A, Haffner B, Huetter E, Gnaiger E<br />
|year=*<br />
|mipnetlab=AT_Innsbruck_OROBOROS<br />
|abstract=Methodological and conceptual features of highresolution respirometry are illustrated in an experiment with cultured, suspended cells in the OROBOROS<br />
Oxygraph-2k (O2k). The experiment demonstrates manual titrations of inhibitors, and automatic titrations of an uncoupler using the electronic Titration-Injection microPump TIP2k. Application of the DatLab 4.3 (upgraded) software is shown for instrumental control (O2k and TIP2k), and on-line data analysis. The following guideline describes the experiment in the form of a laboratory protocol, complementary to the relevant sections of the Oxygraph-2k Manual. The experiments were carried out by participants of an O2k-Course on high-resolution respirometry in April 2005 (IOC30; Schröcken, Austria).<br />
|info=[http://www.oroboros.at/index.php?id=protocols_cell_hrr_pc MiPNet10.04]<br />
}}<br />
{{Labeling<br />
|discipline=Mitochondrial Physiology<br />
|organism=Mouse<br />
|tissues=Blood Cell; Suspension Culture<br />
|preparations=Intact Cell; Cultured; Primary<br />
|kinetics=Inhibitor; Uncoupler<br />
|topics=Respiration; OXPHOS; ETS Capacity, Coupling; Membrane Potential<br />
|instruments=Oxygraph-2k, TIP2k, DatLab Software; Separate Application, Method<br />
|articletype=Protocol; Manual, MiPNet-online Publication<br />
}}<br />
[[Category:OroboroPedia]]</div>Biljanahttps://wiki.oroboros.at/index.php?title=Huetter_2007_Aging_Cell&diff=6796Huetter 2007 Aging Cell2010-10-20T12:13:37Z<p>Biljana: </p>
<hr />
<div>{{Publication<br />
|title=Hütter E, Skovbro M, Lener B, Prats C, Rabol R, Dela F, Jansen-Durr P (2007) Oxidative stress and mitochondrial impairment can be separated from lipofuscin accumulation in aged human skeletal muscle. Aging Cell 6: 245-256.<br />
|authors=Huetter E, Skovbro M, Lener B, Prats C, Rabol R, Dela F, Jansen-Durr P<br />
|year=2007<br />
|journal=Aging Cell<br />
|abstract=According to the free radical theory of aging, reactive oxygen species (ROS) act as a driving force of the aging process, and it is generally believed that mitochondrial dysfunction is a major source of increased oxidative stress in tissues with high content of mitochondria, such as muscle or brain. However, recent experiments in mouse models of premature aging have questioned the role of mitochondrial ROS production in premature aging. To address the role of mitochondrial impairment and ROS production for aging in human muscles, we have analyzed mitochondrial properties in muscle fibres isolated from the vastus lateralis of young and elderly donors. Mitochondrial respiratory functions were addressed by high-resolution respirometry, and ROS production was analyzed by in situ staining with the redox-sensitive dye dihydroethidium. We found that aged human skeletal muscles contain fully functional mitochondria and that the level of ROS production is higher in young compared to aged muscle. Accordingly, we could not find any increase in oxidative modification of proteins in muscle from elderly donors. However, the accumulation of lipofuscin was identified as a robust marker of human muscle aging. The data support a model, where ROS-induced molecular damage is continuously removed, preventing the accumulation of dysfunctional mitochondria despite ongoing ROS production.<br />
|info=[http://www.ncbi.nlm.nih.gov/pubmed/17376148 PMID: 17376148]<br />
}}<br />
{{Labeling<br />
|discipline=Biomedicine<br />
|injuries=RONS; Oxidative Stress, Mitochondrial Disease; Degenerative Disease and Defect, Aging; Senescence<br />
|organism=Mouse<br />
|tissues=Skeletal Muscle, Neurons; Brain<br />
|preparations=Intact Cell; Cultured; Primary, Permeabilized Cell or Tissue; Homogenate<br />
|kinetics=ADP; Pi, Oxygen<br />
|topics=Respiration; OXPHOS; ETS Capacity, Ion Homeostasis<br />
|instruments=Oxygraph-2k<br />
}}</div>Biljana