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  • 1
    Electronic Resource
    Electronic Resource
    Induction of ion transport in rat heart mitochondria by fluorescamine (1983)
    Springer
    Journal of bioenergetics and biomembranes 15 (1983), S. 207-215 
    Details
    ISSN: 1573-6881
    Keywords: Heart ; biomembranes ; mitochondria ; ions ; transport ; diffusion ; channels ; swelling ; fluorescamine ; fluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract This report describes experimental results which show that the fluorescent reagent fluorescamine induces mitochondrial energy-independent swelling when the incubation media contain the chloride salts of the cations Li+, Na+, K+, Rb+, and Cs+. The reaction depends on the concentration of the dye and is inhibited by Mg2+, and its extension is closely related to the amount of the primary amino groups titrated by fluorescamine. Analysis of the labeled inner membrane in polyacrylamide gel shows that the amount of aminofluorescamine complex is lower when mitochondria are in the presence of Mg2+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00743941
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  • 2
    Electronic Resource
    Electronic Resource
    Triphenyltin as inductor of mitochondrial membrane permeability transition (1994)
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 457-462 
    Details
    ISSN: 1573-6881
    Keywords: Triphenyltin ; mitochondrial Ca2+ ; trialkytin compound
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of triphenyltin on mitochondrial Ca2+ content was studied. It was found that this trialkyltin compound induces an increase in membrane permeability that leads to Ca2+ release, drop of the transmembrane potential, and efflux of matrix proteins. Interestingly, cyclosporin A was unable to inhibit triphenyltin-induced Ca2+ release. Based on these results it is proposed that the hyperpermeable state is produced by modification of 2.25 nmol of membrane thiol groups.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762786
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  • 3
    Electronic Resource
    Electronic Resource
    Identification of a 20-kDa protein with calcium uptake transport activity. Reconstitution in a membrane model (1994)
    Springer
    Journal of bioenergetics and biomembranes 26 (1994), S. 555-562 
    Details
    ISSN: 1573-6881
    Keywords: Calcium uptake ; uniporter ; mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract This paper presents results of experiments designed to further purify the membrane system involved in mitochondrial calcium transport. A partially purified extract, which transported calcium with a specific activity of 1194 nmol45Ca2+/mg protein/5 min, was used to obtain mouse hyperimmune serum. This serum inhibited calcium uptake both in mitoplasts and in vesicles reconstituted with mitochondrial proteins containing cytochrome oxidase. Western blot analysis of the semipurified fraction showed that the serum recognized specifically two antigens of 75 and 20 kDa. Both antibodies were purified by elution from the nitrocellulose sheets and their inhibition capacity was analyzed. The antibody that recognized the 20-kDa protein produced a higher degree of inhibition than the other one.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762740
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  • 4
    Electronic Resource
    Electronic Resource
    Extensive Ca2+ release from energized mitochondria induced by disulfiram (1989)
    Springer
    Journal of bioenergetics and biomembranes 21 (1989), S. 335-345 
    Details
    ISSN: 1573-6881
    Keywords: Disulfiram ; antabuse ; Ca2+ release ; mitochondria ; kidney
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of the alcohol-deterrent drug, disulfiram, on mitochondrial Ca2+ content was studied. Addition of this drug (20 µM) to mitochondria induces a complete loss of accumulated Ca2+. The calcium release is accompanied by a collapse of the transmembrane potential, mitochondrial swelling, and a diminution of the NAD(P)H/NAD(P) radio. These effects of disulfiram depend on Ca2+ accumulation; thus, ruthenium red reestablished the membrane δψ and prevents the oxidation of pyridine nucleotides. The binding of disulfiram to the membrane sulfhydryls appeared to depend on the metabolic state of mitochondria, as well as on the mitochondrial configuration. In addition, it is shown that modification of 9 nmol -SH groups per mg protein suffices to induce the release of accumulated Ca2+.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762725
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  • 5
    Electronic Resource
    Electronic Resource
    The mechanism of lead-induced mitochondrial Ca2+ efflux (1987)
    Springer
    Journal of bioenergetics and biomembranes 19 (1987), S. 285-295 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondria ; lead ; calcium ; NAD(P)H oxidation ; calcium transport ; mitochondrial calcium ; pyridine nucleotide oxidation ; kidney mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract Addition of Pb2+ to rat kidney mitochondria is followed by induction of several reactions: inhibition of Ca2+ uptake, collapse of the transmembrane potential, oxidation of pyridine nucleotides, and a fast release of accumulated Ca2+. When the incubation media are supplemented with ruthenium red, the effect of Pb2+ on NAD(P)H oxidation, membrane ΔΨ, and Ca2+ release are not prevented if malate-glutamate are the oxidizing substrates; however, the latter two lead-induced reactions are prevented by ruthenium red if succinate is the electron donor. It is proposed that in mitochondria oxidizing NAD-dependent substrates, Pb2+ induces Ca2+ release by promoting NAD(P)H oxidation and a parallel drop in ΔΨ due to its binding to thiol groups, located in the cytosol side of the inner membrane. In addition, it is proposed that with succinate as substrate, the Ca2+-releasing effect of lead is due to the collapse of the transmembrane potential as a consequence of the uptake of Pb2+ through the calcium uniporter, since such effect is ruthenium red sensitive.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00762418
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  • 6
    Electronic Resource
    Electronic Resource
    Control of mitochondrial Ca2+ retention by ADP-stimulated glutamic dehydrogenase (1987)
    Springer
    Journal of bioenergetics and biomembranes 19 (1987), S. 571-580 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondria ; calcium ; mitochondrial Ca2+ transport ; adenine nucleotides ; glutamic dehydrogenase ; kidney mitochondria ; ADP-stimulated glutamic dehydrogenase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The protective effect of ADP on unspecific Ca2+ release and collapse of the transmembrane potential was analyzed in mitochondria from kidneys of rats. The presence of ADP in the incubation mixture prevents Ca2+ leakage and collapse of δω in sucrose-containing medium, but fails to do so in KCl medium. The effect of the adenine nucleotide in sucrose media correlates with an increase in the level of reduced pyridine nucleotides; the increase was due to a stimulatory effect on the activity of glutamic dehydrogenase. It also was observed that in KCl media, in the presence and in the absence of ADP the rate of NADH oxidation through the respiratory chain was higher than in sucrose; in this latter medium a high level of reduced pyridine nucleotides was found, in comparison to KCl media. It is proposed that the role of ADP is to increase glutamic dehydrogenase activity and in consequence to provoke a higher rate of formation of NADH which in turn controls Ca2+ release.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00770038
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  • 7
    Electronic Resource
    Electronic Resource
    On the Protection by Inorganic Phosphate of Calcium-Induced Membrane Permeability Transition (1997)
    Springer
    Journal of bioenergetics and biomembranes 29 (1997), S. 571-577 
    Details
    ISSN: 1573-6881
    Keywords: Mitochondrial calcium ; inorganic phosphate ; membrane permeability transition ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of inorganic phosphate as inhibitor of mitochondrial membrane permeability transition was studied. It is shown that in mitochondria containing a high phosphate concentration, i.e., 68 nmol/mg, Ca2+ did not activate the pore opening. Conversely, at lower levels of matrix phosphate, i.e., 38 nmol/mg, Ca2+ was able to induce subsequent pore opening. The inhibitory effect of phosphate was apparent in sucrose-based media, but it was not achieved in KCl media. The matrix free Ca2+ concentration and matrix pH were lowered by phosphate, but they were always higher in K+-media. In the absence of ADP, phosphate strengthened the inhibitory effect of cyclosporin A on carboxyatractyloside-induced Ca2+ efflux. Acetate was unable to replace phosphate in the induction of the aforementioned effects. It is concluded that phosphate preserves selective membrane permeability by diminishing the matrix free Ca2+ concentration.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1022483018482
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  • 8
    Electronic Resource
    Electronic Resource
    Modulation of matrix Ca2+ content by the ADP/ATP carrier in brown adipose tissue mitochondria. Influence of membrane lipid composition (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 69-76 
    Details
    ISSN: 1573-6881
    Keywords: Matrix calcium ; BAT mitochondria ; membrane permeability transition ; adenine nucleotide translocase ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of the adenine nucleotide translocase on Ca2+ homeostasis in mitochondria from brown adipose tissue was examined. It was found that in mitochondria incubated with 50 μM Ca2+, ADP was not needed to retain the cation, but it was required for strengthening the inhibitory effect of cyclosporin on membrane permeability transition as induced by menadione. In addition, carboxyatractyloside was unable to promote matrix Ca2+ release, even though it inhibits the ADP exchange reaction. However, when the Ca2+ concentration was increased to 150 μM, carboxyatractyloside did induce Ca2+ release, and ADP favored Ca2+ retention. Determination of cardiolipin content in the inner membrane vesicles showed a greater concentration in brown adipose tissue mitochondria than that found in kidney mitochondria. It is suggested that the failure of the adenine nucleotide translocase to influence membrane permeability transition depends on the lipid composition of the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02109905
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  • 9
    Electronic Resource
    Electronic Resource
    Modulation of matrix Ca2+ content by the ADP/ATP carrier in brown adipose tissue mitochondria. Influence of membrane lipid composition (1996)
    Springer
    Journal of bioenergetics and biomembranes 28 (1996), S. 69-76 
    Details
    ISSN: 1573-6881
    Keywords: Matrix calcium ; BAT mitochondria ; membrane permeability transition ; adenine nucleotide translocase ; calcium transport
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The role of the adenine nucleotide translocase on Ca2+ homeostasis in mitochondria from brown adipose tissue was examined. It was found that in mitochondria incubated with 50 μM Ca2+, ADP was not needed to retain the cation, but it was required for strengthening the inhibitory effect of cyclosporin on membrane permeability transition as induced by menadione. In addition, carboxyatractyloside was unable to promote matrix Ca2+ release, even though it inhibits the ADP exchange reaction. However, when the Ca2+ concentration was increased to 150 μM, carboxyatractyloside did induce Ca2+ release, and ADP favored Ca2+ retention. Determination of cardiolipin content in the inner membrane vesicles showed a greater concentration in brown adipose tissue mitochondria than that found in kidney mitochondria. It is suggested that the failure of the adenine nucleotide translocase to influence membrane permeability transition depends on the lipid composition of the inner membrane.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02150680
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  • 10
    Electronic Resource
    Electronic Resource
    Dicyclohexylcarbodiimide as inducer of mitochondrial Ca2+ release (1990)
    Springer
    Journal of bioenergetics and biomembranes 22 (1990), S. 679-689 
    Details
    ISSN: 1573-6881
    Keywords: Dicylcohexylcarbodiimide: DCCD: Ca2+ release ; Kidney mitochondria
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Physics
    Notes: Abstract The effect of the alkylating reagent dicyclohexylcarbodiimide (DCCD) on mitochondrial Ca2+ content was studied. The results obtained indicate that DCCD at a concentration of 100 µM induces mitochondrial Ca2+ efflux. This reaction is accompanied by an increasing energy drain on the system, stimulation of oxygen consumption, and mitochondrial swelling. These DCCD effects can be partially suppressed by supplementing the incubation medium with 1 mM phosphate. By electrophoretic analysis on polyacrylamide-sodium dodecyl sulfate, it was found that DCCD binds to a membrane component with anM r of 20 to 29 kDa.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00809071
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