MITOCHONDRIAL SWELLING AT ACID pH

1966 ◽  
Vol 44 (6) ◽  
pp. 695-706 ◽  
Author(s):  
Roberto Cereijq-Santaló
Keyword(s):  
Hydrochloric Acid ◽  
Maximum Rate ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Buffering Capacity ◽  
Rat Liver Mitochondria ◽  
Isotonic Solution ◽  
Ph Values ◽  
Acid Ph ◽  
Protein Gel

The effect of variations of pH on swelling of rat liver mitochondria was studied.It was found that mitochondria swell at acid pH (5.0–6.0) when they are incubated in isotonic solution of potassium chloride. The extent of swelling increased with decreasing tonicity of the medium. However, mitochondria did not swell at acid pH when they were incubated in isotonic sucrose. The inhibitory effect of sucrose was partially released by the addition of electrolytes to the medium.When unbuffered suspensions of mitochondria with different pH values were prepared by the addition of hydrochloric acid or sodium hydroxide to the incubation medium, it was observed that the extent of swelling increased both with acidity (6.0 to 5.0) and with alkalinity (7.0 to 8.0).Titration of the unbuffered mitochondrial suspensions showed a maximum buffering capacity in the ranges of pH values where maximum rate of swelling occurred.These results suggest that the mitochondrion behaves as a combination of osmometer and protein gel.

P1, P5-Bis-(5′-adenosyl)pentaphosphate: Is this Adenylate Kinase Inhibitor Substrate for Mitochondrial Processes?

1977 ◽  
Vol 32 (9-10) ◽  
pp. 786-791 ◽  
Author(s):  
Josef Köhrle ◽  
Joachim Lüstorff ◽  
Eckhard Schlimme
Keyword(s):  
Adenylate Kinase ◽  
Kinase Inhibitor ◽  
Adenine Nucleotide ◽  
Nucleoside Diphosphate Kinase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Intermembrane Space ◽  
Rabbit Muscle ◽  
Inner Mitochondrial Membrane

Abstract 1. P1, P5-Bis-(5′-adenosyl)pentaphosphate (Ap5A) inhibits “soluble” adenylate kinase even when this enzyme is an integral part of the complete mitochondrion. The Ki is 10-5м , i. e. about two orders of magnitude higher than the inhibitor constants determined for the purified adenylate kinase of rabbit muscle and an enzyme preparation separated from the mitochondrial intermembrane space. The weaker inhibitory effect is due to a lower accessibility of the enzyme.2. As to be expected Ap5A which is of the “multisubstrate analogue”-type does not affect mito­ chondrial nucleoside diphosphate kinase.3. Though Ap5A owns the structural elements of both ATP and ADP it is not a substrate of the adenine nucleotide carrier, i.e. neither it is exchanged across the inner mitochondrial membrane nor specifically bound.4. Ap5A is not metabolized by rat liver mitochondria.

BIOCHEMICAL STUDIES ON TOFRANIL

1961 ◽  
Vol 39 (3) ◽  
pp. 551-558 ◽  
Author(s):  
P. N. Abadom ◽  
K. Ahmed ◽  
P. G. Scholefield
Keyword(s):  
Rat Brain ◽  
Rat Liver ◽  
Brain Cortex ◽  
Respiratory Activity ◽  
Liver Mitochondria ◽  
Brain Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Brain Cortex Slices ◽  
Cortex Slices

Tofranil inhibits the respiratory activity of rat brain cortex slices incubated in a glucose-containing medium. It also inhibits the uptake and incorporation of glycine-1-C14at concentrations which have only a slight inhibitory effect on the respiration of slices. Tofranil also inhibits oxidative phosphorylation in both rat liver and rat brain mitochondria but at higher concentrations respiration is greatly affected. Tofranil differs quantitatively from chlorpromazine in its greater inhibitory effect on the ATP–Pi32exchange reaction and its lesser effect on the cytochrome c oxidase activity of rat liver mitochondria.

Quantitation of effects on mitochondrial swelling: some effects of ATP and aging

1962 ◽  
Vol 17 (6) ◽  
pp. 979-984 ◽  
Author(s):  
Charles McGaughey
Keyword(s):  
Aging Time ◽  
Quantitative Measurement ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rate Of Change ◽  
Mitochondrial Swelling ◽  
Rat Liver Mitochondria ◽  
Logarithmic Function ◽  
Swelling Rate ◽  
Mitochondrial Volume

A method has been devised for the quantitative measurement of relative effects of substances or conditions on rate of change of mitochondrial volume. It can be used to study the effects progressively as the mitochondria swell. By this means, the effects of adenosine triphosphate (ATP) and aging on mitochondrial swelling were investigated. It was found that at constant mitochondrial volume, the rate of change of volume is a logarithmic function of aging time. The swelling of fresh mitochondria was mildly inhibited by ATP at very low volumes. Aging of rat liver mitochondria caused this inhibitory effect to be replaced by enhancement of swelling, which became greater in magnitude and was retained through larger volumes as aging time increased. The swelling enhancement was followed by inhibition, the magnitude of which increased with further swelling. The inhibitory effect of ATP on swelling of mouse liver mitochondria underwent a sudden marked increase at a particular mitochondrial volume independent of aging time and time of ATP exposure. At lower volumes the effect of ATP increased with aging time and swelling rate, whereas at larger volumes this relation ceased to be apparent. The possible significance of these results is discussed. Submitted on January 22, 1962

scholarly journals Synthesis and biological activity of N-substituted-tetrahydro-γ-carbolines containing peptide residues

2014 ◽  
Vol 10 ◽  
pp. 155-162 ◽  
Author(s):  
Nadezhda V Sokolova ◽  
Valentine G Nenajdenko ◽  
Vladimir B Sokolov ◽  
Daria V Vinogradova ◽  
Elena F Shevtsova ◽  
...  
Keyword(s):  
Lipid Peroxidation ◽  
Biological Activity ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Terminal Alkyne ◽  
Peptide Fragments ◽  
Prooxidant Activity ◽  
Peptide Conjugates

The synthesis of novel peptide conjugates of N-substituted-tetrahydro-γ-carbolines has been performed using the sequence of the Ugi multicomponent reaction and Cu(I)-catalyzed click chemistry. The effect of obtained γ-carboline–peptide conjugates on the rat liver mitochondria was evaluated. It was found that all compounds in the concentration of 30 µM did onot induce depolarization of mitochondria but possessed some inhibitory effect on the mitochondria permeability transition. The original N-substituted-tetrahydro-γ-carbolines containing an terminal alkyne group demonstrated a high prooxidant activity, whereas their conjugates with peptide fragments slightly inhibited both autooxidation and the t-BHP-induced lipid peroxidation.

scholarly journals The Effect of α-Tocopheryl Succinate on Succinate Respiration in Rat Liver Mitochondria

2015 ◽  
pp. S609-S615 ◽  
Author(s):  
O. SOBOTKA ◽  
Z. DRAHOTA ◽  
O. KUČERA ◽  
R. ENDLICHER ◽  
H. RAUCHOVÁ ◽  
...  
Keyword(s):  
Concentration Dependence ◽  
Rat Liver ◽  
Liver Homogenate ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Experimental Models ◽  
Rat Liver Mitochondria ◽  
Isolated Mitochondria ◽  
Significant Inhibitory Effect ◽  
Tocopheryl Succinate

We compared the effect of α-tocopheryl succinate (TOS) on succinate-dependent respiration in rat liver mitochondria, homogenate and permeabilized hepatocytes in both a coupled and uncoupled state. In isolated mitochondria, a significant inhibitory effect was observed at a concentration of 5 µM, in liver homogenate at 25 µM and in permeabilized hepatocytes at 50 µM. The inhibitory effect of TOS on succinate respiration in an uncoupled state was less pronounced than in a coupled state in all the experimental models tested. When the concentration dependence of the TOS inhibitory effect was tested, the most sensitive in both states were isolated mitochondria; the most resistant were permeabilized hepatocytes.

scholarly journals Peroxidative damage of mitochondrial respiration is substrate-dependent

2009 ◽  
pp. 685-692
Author(s):  
R Endlicher ◽  
P Křiváková ◽  
H Rauchová ◽  
H Nůsková ◽  
Z Červinková ◽  
...  
Keyword(s):  
Membrane Potential ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
Rat Liver Mitochondria ◽  
Succinate Oxidation ◽  
Peroxidative Damage ◽  
Palmitoyl Carnitine ◽  
Low Concentrations ◽  
Tert Butyl Hydroperoxide ◽  
Strong Inhibitory Effect

The concentration-dependence of tert-butyl hydroperoxide (BHP) inhibitory effect on oxygen consumption in isolated rat liver mitochondria was measured in the presence of various respiratory substrates. Strong inhibitory effect at low concentrations of BHP (15-30 µM) was found for oxoglutarate and palmitoyl carnitine oxidation. Pyruvate and glutamate oxidation was inhibited at higher concentrations of BHP (100-200 µM). Succinate oxidation was not affected even at 3.3 mM BHP. Determination of mitochondrial membrane potential has shown that in the presence of NADH-dependent substrates the membrane potential was dissipated by BHP but was completely restored after addition of succinate. Our data thus indicate that beside peroxidative damage of complex I also various mitochondrial NADH-dependent dehydrogenases are inhibited, but to a different extent and with different kinetics. Our data also show that succinate could be an important nutritional substrate protecting hepatocytes during peroxidative damage.

scholarly journals The inhibition of pyruvate and ls(+)-isocitrate oxidation by succinate oxidation in rat liver mitochondria

1969 ◽  
Vol 114 (3) ◽  
pp. 589-596 ◽  
Author(s):  
T. König ◽  
D. G. Nicholls ◽  
P. B. Garland
Keyword(s):  
Cytochrome B ◽  
Rat Liver ◽  
Rat Heart ◽  
Fold Increase ◽  
Liver Mitochondria ◽  
Inhibitory Effect ◽  
The Other ◽  
Rat Liver Mitochondria ◽  
Succinate Oxidation ◽  
Rapid Flow

1. The effects of succinate oxidation on pyruvate and also isocitrate oxidation by rat liver mitochondria were studied. 2. Succinate oxidation was without effect on pyruvate and isocitrate oxidation when respiration was maximally activated with ADP. 3. When respiration was partially inhibited by atractylate, succinate oxidation severely inhibited the oxidation of pyruvate and isocitrate. 4. This inhibitory effect of succinate was associated with a two- to three-fold increase in the reduction of mitochondrial NAD+ but no change in the reduction of cytochrome b. 5. It is concluded that, in the partially energy-controlled state, respiration is more severely inhibited at the first phosphorylating site than at the other two. 6. The effects of succinate oxidation are compared with those of palmitoylcarnitine oxidation. It is concluded that a rapid flow of electrons directly into the respiratory chain at the level of cytochrome b is in itself inadequate to inhibit the oxidation of intramitochondrial NADH. 7. The effects of succinate oxidation on pyruvate oxidation were similar in rat heart and liver mitochondria.

scholarly journals The action of trialkyltin compounds on mitochondrial respiration. The effect of pH

1974 ◽  
Vol 138 (3) ◽  
pp. 349-357 ◽  
Author(s):  
Alan P. Dawson ◽  
Michael J. Selwyn
Keyword(s):  
Maximum Rate ◽  
Ph Dependence ◽  
Acid Value ◽  
Alkaline Ph ◽  
Free Medium ◽  
Succinate Oxidation ◽  
Ph Values ◽  
Acid Ph ◽  
Internal Ph ◽  
Ph Range

1. Inhibition of 2,4-dinitrophenol-stimulated respiration by trialkyltins is dependent on the presence of Cl− in the assay medium and is only apparent at acid pH values. It appears to be a result of the Cl−–OH− exchange mediated by trialkyltins. 2. In a KCl medium at alkaline pH values, the maximum rate of respiration produced by uncouplers is further increased by the presence of trialkyltins. 3. The inhibition of uncoupled succinate oxidation at acid pH values is not reversed by increasing the external substrate concentration, suggesting that depletion of intramitochondrial succinate is not an important factor in the inhibition. 4. It is suggested that the probable explanation for these observations is that in the presence of Cl− trialkyltins alter the internal pH to a more acid value and this directly affects the activity of one or more steps in succinate oxidation. 5. The oligomycin-like action of trialkyltins in a Cl−-free medium shows considerable pH-dependence over the pH range 6.6–7.6 in the presence of 10mm-phosphate, but very much less pH-dependence in the presence of 1mm-phosphate. 6. The binding of triethyltin to mitochondria shows a pK at pH6.3 and does not change greatly over the pH range 6.6–7.6. 7. It is suggested that the pH-dependence of the oligomycin-like action described by Coleman & Palmer (1971) is the result of the pH-dependence of the formation of a hydrophilic complex between trialkyltins and Pi.

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