Ter Veld 2005 FEBS J
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