Difference between revisions of "Ter Veld 2005 FEBS J"
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|year=2005 | |year=2005 | ||
|journal=FEBS J | |journal=FEBS J | ||
|abstract=Adaptations of the kinetic properties of mitochondria in striated muscle lacking cytosolic (M) and/or mitochondrial ( | |abstract=Adaptations of the kinetic properties of mitochondria in striated muscle lacking cytosolic (M) and/or mitochondrial (mt) creatine kinase (CK) isoforms in comparison to wild-type (WT) were investigated ''in vitro''. Intact mitochondria were isolated from heart and gastrocnemius muscle of WT and single- and double CK-knock-out mice strains (cytosolic (M-CK<sup>β/β</sup>), mitochondrial (mt-CK<sup>β/β</sup>) and double knock-out (mtM-CK<sup>β/β</sup>), respectively). Maximal ADP-stimulated oxygen consumption flux (State3 Vmax; nmol O2Β·mg mitochondrial protein<sup>β1</sup>Β·min<sup>β1</sup>) and ADP affinity (inline image; Β΅m) were determined by respirometry. State 3 Vmax and inline image of M-CK<sup>β/β</sup> and mtIM-CK<sup>β/β</sup> gastrocnemius mitochondria were twofold higher than those of WT, but were unchanged for mt-CK<sup>β/β</sup>. For mutant cardiac mitochondria, only the inline image of mitochondria isolated from the mtM-CK<sup>β/β</sup>Β phenotype was different (i.e. twofold higher) than that of WT. The implications of these adaptations for striated muscle function were explored by constructing force-flow relations of skeletal muscle respiration. It was found that the identified shift in affinity towards higher ADP concentrations in mtM-CK<sup>β/β</sup> muscle genotypes may contribute to linear mitochondrial control of the reduced cytosolic ATP free energy potentials in these phenotypes. | ||
|keywords=Heart, Metabolic control, Mitochondrial respiration, Skeletal muscle, Transgenic mice | |keywords=Heart, Metabolic control, Mitochondrial respiration, Skeletal muscle, Transgenic mice | ||
|mipnetlab=NL Eindhoven Nicolay K | |mipnetlab=NL Eindhoven Nicolay K |
Latest revision as of 20:13, 4 January 2018
ter Veld F, Jeneson JA, Nicolay K (2005) Mitochondrial affinity for ADP is twofold lower in creatine kinase knock-out muscles. Possible role in rescuing cellular energy homeostasis. FEBS J 272:956-65. |
ter Veld F, Jeneson JA, Nicolay K (2005) FEBS J
Abstract: Adaptations of the kinetic properties of mitochondria in striated muscle lacking cytosolic (M) and/or mitochondrial (mt) creatine kinase (CK) isoforms in comparison to wild-type (WT) were investigated in vitro. Intact mitochondria were isolated from heart and gastrocnemius muscle of WT and single- and double CK-knock-out mice strains (cytosolic (M-CKβ/β), mitochondrial (mt-CKβ/β) and double knock-out (mtM-CKβ/β), respectively). Maximal ADP-stimulated oxygen consumption flux (State3 Vmax; nmol O2Β·mg mitochondrial proteinβ1Β·minβ1) and ADP affinity (inline image; Β΅m) were determined by respirometry. State 3 Vmax and inline image of M-CKβ/β and mtIM-CKβ/β gastrocnemius mitochondria were twofold higher than those of WT, but were unchanged for mt-CKβ/β. For mutant cardiac mitochondria, only the inline image of mitochondria isolated from the mtM-CKβ/β phenotype was different (i.e. twofold higher) than that of WT. The implications of these adaptations for striated muscle function were explored by constructing force-flow relations of skeletal muscle respiration. It was found that the identified shift in affinity towards higher ADP concentrations in mtM-CKβ/β muscle genotypes may contribute to linear mitochondrial control of the reduced cytosolic ATP free energy potentials in these phenotypes. β’ Keywords: Heart, Metabolic control, Mitochondrial respiration, Skeletal muscle, Transgenic mice
β’ O2k-Network Lab: NL Eindhoven Nicolay K
Labels:
Organism: Rat
Tissue;cell: Heart
Preparation: Isolated mitochondria
Coupling state: OXPHOS
HRR: Oxygraph-2k