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Difference between revisions of "Appaix 2002 Biochim Biophys Acta"

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{{Publication
{{Publication
|title=Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA (2002) Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition. Biochim Biophys Acta 1556: 155-167.
|title=Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA (2002) Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition. Biochim Biophys Acta 1556:155-67.
|info=[http://www.ncbi.nlm.nih.gov/pubmed/12460673 PMID: 12460673 Open Access]
|authors=Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA
|authors=Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA
|year=2002
|year=2002
|journal=Biochim. Biophys. Acta
|journal=Biochim Biophys Acta
|abstract=The effects of Bax (full-length, FL, and C-terminal truncated, ΔC) on respiration rate, membrane potential, MgATPase activity and kinetics of regulation of respiration were studied in isolated rat heart mitochondria and permeabilized cardiomyocytes. The results showed that while both Bax-FL and Bax-ΔC permeabilized the outer mitochondrial membrane, released cytochrome c and reduced the respiration rate, the latter could be fully restored by exogenous cytochrome c  only in the case of Bax-ΔC, but not in presence of Bax-FL. In addition, Bax-FL but not Bax-ΔC increased the MgATPase activity, and their effects on the mitochondrial membrane potential were quantitatively different. None of these effects was sensitive to cyclosporin A (CsA).
|abstract=The effects of Bax (full-length, FL, and C-terminal truncated, ΔC) on respiration rate, membrane potential, MgATPase activity and kinetics of regulation of respiration were studied in isolated rat heart mitochondria and permeabilized cardiomyocytes. The results showed that while both Bax-FL and Bax-ΔC permeabilized the outer mitochondrial membrane, released cytochrome c and reduced the respiration rate, the latter could be fully restored by exogenous cytochrome c  only in the case of Bax-ΔC, but not in presence of Bax-FL. In addition, Bax-FL but not Bax-ΔC increased the MgATPase activity, and their effects on the mitochondrial membrane potential were quantitatively different. None of these effects was sensitive to cyclosporin A (CsA).


It is concluded that Bax-FL affects both the outer and the inner mitochondrial membranes by: (1) opening large pores in the outer membrane; (2) inhibiting some segments of the respiratory chain in the inner membrane; and (3) uncoupling the inner mitochondrial membrane by increasing proton leak without opening the permeability transition pore (PTP).
It is concluded that Bax-FL affects both the outer and the inner mitochondrial membranes by: (1) opening large pores in the outer membrane; (2) inhibiting some segments of the respiratory chain in the inner membrane; and (3) uncoupling the inner mitochondrial membrane by increasing proton leak without opening the permeability transition pore (PTP).
|keywords=Mitochondrion, Apoptosis, Heart, Oxidative phosphorylation, Bax
|keywords=Mitochondrion, Apoptosis, Heart, Oxidative phosphorylation, Bax
|mipnetlab=DE_Konstanz_Brdiczka D, EE_Tallinn_Saks VA, FR_Grenoble_Saks VA
|mipnetlab=DE_Konstanz_Brdiczka D, EE_Tallinn_Saks VA, FR_Grenoble_Saks VA, EE Tallinn Kaambre T
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
}}
}}
{{Labeling
{{Labeling
|area=Respiration
|organism=Rat
|tissues=Heart
|preparations=Permeabilized cells, Isolated mitochondria
|topics=ADP, ATP
|instruments=Oxygraph-2k
|instruments=Oxygraph-2k
|organism=Rat
|tissues=Cardiac Muscle
|preparations=Isolated Mitochondria, Permeabilized Cell or Tissue; Homogenate
|topics=Coupling; Membrane Potential, ATP; ADP; AMP; PCr
|discipline=Mitochondrial Physiology
|discipline=Mitochondrial Physiology
}}
}}

Latest revision as of 15:14, 3 November 2015

Publications in the MiPMap
Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA (2002) Bax and heart mitochondria: uncoupling and inhibition of respiration without permeability transition. Biochim Biophys Acta 1556:155-67.

» PMID: 12460673 Open Access

Appaix F, Guerrero K, Rampal D, Izikki M, Kaambre T, Sikk P, Brdiczka D, Riva-Lavieille C, Olivares J, Longuet M, Antonsson B, Saks VA (2002) Biochim Biophys Acta

Abstract: The effects of Bax (full-length, FL, and C-terminal truncated, ΔC) on respiration rate, membrane potential, MgATPase activity and kinetics of regulation of respiration were studied in isolated rat heart mitochondria and permeabilized cardiomyocytes. The results showed that while both Bax-FL and Bax-ΔC permeabilized the outer mitochondrial membrane, released cytochrome c and reduced the respiration rate, the latter could be fully restored by exogenous cytochrome c only in the case of Bax-ΔC, but not in presence of Bax-FL. In addition, Bax-FL but not Bax-ΔC increased the MgATPase activity, and their effects on the mitochondrial membrane potential were quantitatively different. None of these effects was sensitive to cyclosporin A (CsA).

It is concluded that Bax-FL affects both the outer and the inner mitochondrial membranes by: (1) opening large pores in the outer membrane; (2) inhibiting some segments of the respiratory chain in the inner membrane; and (3) uncoupling the inner mitochondrial membrane by increasing proton leak without opening the permeability transition pore (PTP). Keywords: Mitochondrion, Apoptosis, Heart, Oxidative phosphorylation, Bax

O2k-Network Lab: DE_Konstanz_Brdiczka D, EE_Tallinn_Saks VA, FR_Grenoble_Saks VA, EE Tallinn Kaambre T


Labels: MiParea: Respiration 


Organism: Rat  Tissue;cell: Heart  Preparation: Permeabilized cells, Isolated mitochondria 

Regulation: ADP, ATP 


HRR: Oxygraph-2k