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Ter Veld 2005 FEBS J

From Bioblast
Publications in the MiPMap
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.

Β» PMID: 15691329 Open Access

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-CK–/–), mitochondrial (mt-CK–/–) and double knock-out (mtM-CK–/–), respectively). Maximal ADP-stimulated oxygen consumption flux (State3 Vmax; nmol O2Β·mg mitochondrial protein–1Β·min–1) and ADP affinity (inline image; Β΅m) were determined by respirometry. State 3 Vmax and inline image of M-CK–/– and mtIM-CK–/– gastrocnemius mitochondria were twofold higher than those of WT, but were unchanged for mt-CK–/–. For mutant cardiac mitochondria, only the inline image of mitochondria isolated from the mtM-CK–/– 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–/– 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


Organism: Rat  Tissue;cell: Heart  Preparation: Isolated mitochondria 

Coupling state: OXPHOS 

HRR: Oxygraph-2k