期刊
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS
卷 1807, 期 12, 页码 1549-1561出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbabio.2011.08.005
关键词
Permeabilized cardiac cells; Respiration; Heart; Mitochondria; Creatine kinase; Metabolic Control Analysis
资金
- INSERM
- CNRS, France
- Estonian Science Foundation [7823]
- Estonia Ministry of Education and Science [SF0180114Bs08]
- Austrian Science Fund (FWF) [P 22080-B20]
- Doctoral Studies and Internationalization Programme DoRa
- Austrian Science Fund (FWF) [P 22080] Funding Source: researchfish
The aim of our study was to analyze a distribution of metabolic flux controls of all mitochondrial complexes of ATP-Synthasome and mitochondrial creatine kinase (MtCK) in situ in permeabilized cardiac cells. For this we used their specific inhibitors to measure flux control coefficients (C-vi(JATP)) in two different systems: A) direct stimulation of respiration by ADP and B) activation of respiration by coupled MtCK reaction in the presence of MgATP and creatine. In isolated mitochondria the C-vi(JATP) were for system A: Complex I - 0.19, Complex III - 0.06, Complex IV 0.18, adenine nucleotide translocase (ANT) - 0.11, ATP synthase - 0.01, Pi carrier - 0.20, and the sum of C-vi(JATP) was 0.75. In the presence of 10 mM creatine (system B) the C-vi(JATP) were 0.38 for ANT and 0.80 for MtCK. In the permeabilized cardiomyocytes inhibitors had to be added in much higher final concentration, and the following values of C-vi(JATP) were determined for condition A and B, respectively: Complex I 0.20 and 0.64, Complex III - 0.41 and 0.40, Complex IV - 0.40 and 0.49, ANT - 0.20 and 0.92, ATP synthase - 0.065 and 0.38, Pi carrier - 0.06 and 0.06, MtCK 0.95. The sum of C-vi(JATP) was 1.33 and 3.84, respectively. Thus, C-vi(JATP) were specifically increased under conditions B only for steps involved in ADP turnover and for Complex I in permeabilized cardiomyocytes within Mitochondrial Interactosome, a supercomplex consisting of MtCK, ATP-Synthasome, voltage dependent anion channel associated with tubulin beta II which restricts permeability of the mitochondrial outer membrane. (C) 2011 Elsevier B.V. All rights reserved.
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