scholarly journals Hormone-initiated maturation of rat liver mitochondria after birth

1980 ◽  
Vol 186 (1) ◽  
pp. 361-367 ◽  
Author(s):  
R Sutton ◽  
J K Pollak
Keyword(s):  
Cyclic Amp ◽  
Rat Liver ◽  
Beta Blocker ◽  
Adenine Nucleotide ◽  
Respiratory Control ◽  
Liver Mitochondria ◽  
Energy Transduction ◽  
Rat Liver Mitochondria ◽  
Maturation Process ◽  
High Concentrations

1. The injection of adrenaline, glucagon or cyclic AMP into foetal rats in utero initiates the maturation of energy transduction in rat liver mitochondria before birth. 2. The injection of the beta-blocker, propranolol, prevents this maturation process. 3. The maturation of mitochondrial energy transduction is measured in terms of the increase in the respiratory control index and mitochondrial adenine nucleotide concentration. 4. It is postulated that the actions of the hormones, acting through cyclic AMP, affect glycogenolysis and glycolysis to give rise to transient localized high concentrations of ATP. 5. It is the ATP that acts as the molecular trigger, effecting mitochondrial maturation.

scholarly journals Inhibition by local anaesthetics of adenine nucleotide translocation in rat liver mitochondria

1974 ◽  
Vol 140 (3) ◽  
pp. 413-422 ◽  
Author(s):  
Terry L. Spencer ◽  
Fyfe L. Bygrave
Keyword(s):  
Rat Liver ◽  
Protein Interactions ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Local Anaesthetics ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Low Concentrations ◽  
High Concentrations ◽  
Lipid Protein Interactions

1. The mechanism of adenine nucleotide translocation in mitochondria isolated from rat liver was further examined by using the local anaesthetics procaine, butacaine, nupercaine and tetracaine as perturbators of lipid–protein interactions. Each of these compounds inhibited translocation of ADP and of ATP; butacaine was the most effective with 50% inhibition occurring at 30μm for 200μm-ATP and at 10μm for 200μm-ADP. The degree of inhibition by butacaine of both adenine nucleotides was dependent on the concentration of adenine nucleotide present; with low concentrations of adenine nucleotide, low concentrations of butacaine-stimulated translocation, but at high concentrations (greater than 50μm) low concentrations of butacaine inhibited translocation. Butacaine increased the affinity of the translocase for ATP to a value which approached that of ADP. 2. Higher concentrations of nupercaine and of tetracaine were required to inhibit translocation of both nucleotides; 50% inhibition of ATP translocation occurred at concentrations of 0.5mm and 0.8mm of these compounds respectively. The pattern of inhibition of ADP translocation by nupercaine and tetracaine was more complex than that of ATP; at very low concentrations (less than 250μm) inhibition ensued, followed by a return to almost original rates at 1mm. At higher concentrations inhibition of ADP translocation resulted. 3. That portion of ATP translocation stimulated by Ca2+ was preferentially inhibited by each of the local anaesthetics tested. In contrast, inhibition by the anaesthetics of ADP translocation was prevented by low concentrations of Ca2+. 4. The data provide further support for our hypothesis that lipid–protein interactions are important determinants in the activity of the adenine nucleotide translocase in mitochondria.

The membrane permeability transition in liver mitochondria of the great green goby Zosterisessor ophiocephalus (Pallas)

2000 ◽  
Vol 203 (22) ◽  
pp. 3425-3434 ◽  
Author(s):  
A. Toninello ◽  
M. Salvi ◽  
L. Colombo
Keyword(s):  
Membrane Potential ◽  
Rat Liver ◽  
Adenine Nucleotide ◽  
Respiratory Control ◽  
Permeability Transition ◽  
Liver Mitochondria ◽  
Transport Systems ◽  
Rat Liver Mitochondria ◽  
The Matrix ◽  
Zosterisessor Ophiocephalus

Liver mitochondria from the great green goby Zosterisessor ophiocephalus (Pallas) normally exhibit bioenergetic variables (membrane potential 165+/−7 mV; respiratory control ratio 6.6+/−0.4; ADP/O ratio 1.85+/−0.8; means +/− s.e.m., N=6) and activities of physiological transport systems (phosphate/proton symporter, adenine nucleotide antiporter, Ca(2+) electrophoretic uniporter) comparable with those of rat liver mitochondria. When incubated in the presence of Ca(2+) and an inducer agent such as phosphate, these mitochondria undergo a complete collapse of membrane potential accompanied by a large-amplitude swelling of the matrix, influx of sucrose from the incubation medium, release of endogenous Mg(2+) and K(+) (approximately 90% of the total) and of preaccumulated Ca(2+) and oxidation of endogenous pyridine nucleotides. All these phenomena, which are completely eliminated by cyclosporin A and inhibited with different efficacies by Mg(2+) and spermine, demonstrate that the induction of the permeability transition in this type of mitochondria has characteristics similar to those described in rat liver mitochondria. In contrast, the requirement for very high Ca(2+) concentrations (greater than 100 micromol l(−1) for the induction of the permeability transition represents a very important difference that distinguishes this phenomenon in fish and mammalian mitochondria.

Uptake of biotin by isolated rat liver mitochondria

1992 ◽  
Vol 263 (1) ◽  
pp. G81-G86 ◽  
Author(s):  
H. M. Said ◽  
L. McAlister-Henn ◽  
R. Mohammadkhani ◽  
D. W. Horne
Keyword(s):  
Rat Liver ◽  
Respiratory Control ◽  
Liver Mitochondria ◽  
Significant Inhibition ◽  
Rat Liver Mitochondria ◽  
Significant Stimulation ◽  
Overshoot Phenomenon ◽  
Ph Dependent ◽  
High Concentrations ◽  
Incubation Buffer

This study examined the mechanism of biotin uptake by liver mitochondria. Mitochondria were isolated from rat liver by an established procedure and demonstrated normal respiratory control ratios. Uptake of biotin with time at incubation buffer pH 6.1 was rapid and linear and occurred with a distinct "overshoot" phenomenon that peaked at approximately 1 min of incubation. At incubation buffer pH 7.4, however, uptake of biotin with time was significantly slower and no overshoot was observed. Gradual lowering of incubation buffer pH from 7.9 to 6.1 caused a similar pattern of increase in uptake of low (0.024 microM) and high (8 and 30 microM) concentrations of biotin. At incubation buffer pH 6.1 and 7.4, uptake of biotin as a function of concentration (0.012-30 microM) was linear and occurred at rates of 3.62 and 1.90 pmol.mg protein-1.5 s-1, respectively. Addition to the incubation medium of high concentrations of unlabeled biotin, its related compounds (biocytin, desthiobiotin, biotin methyl ester, thioctic acid, and thioctic amide), or substrates of known mitochondrial transporters (succinate, pyruvate, glutamate, malate, and phosphate) failed to cause any significant inhibition in uptake of [3H]biotin by mitochondria incubated in buffer pH 6.1 and 7.4. Furthermore, preloading mitochondria with unlabeled biotin, biocytin, malate, or aspartate failed to cause any significant stimulation in biotin uptake. At incubation buffer pH 6.1, treatment of mitochondria with the protonophore FCCP caused significant inhibition in pH-dependent overshoot of biotin uptake. However, treatment of mitochondria with the potassium ionophore valinomycin caused significant stimulation in the pH-dependent overshoot of biotin uptake.(ABSTRACT TRUNCATED AT 250 WORDS)

scholarly journals The effect of butacaine on adenine nucleotide binding and translocation in rat liver mitochondria

1975 ◽  
Vol 148 (3) ◽  
pp. 527-531 ◽  
Author(s):  
D R Fayle ◽  
G J Barritt ◽  
F L Bygrave
Keyword(s):  
Rat Liver ◽  
Local Anaesthetic ◽  
Binding Sites ◽  
Adenine Nucleotide ◽  
Adenine Nucleotides ◽  
Nucleotide Binding ◽  
Local Anaesthetics ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Mitochondrial Inner Membrane

The effect of the local anaesthetic, butacaine, on adenine nucleotide binding and translocation in rat liver mitochondria partially depleted of their adenine nucleotide content was investigated. The range of butacaine concentrations that inhibit adenine nucleotide translocation and the extent of the inhibition are similar to the values obtained for native mitochondria. Butacaine does not alter either the total number of atractyloside-sensitive binding sites of depleted mitochondria, or the affinity of these sites for ADP or ATP under conditions where a partial inhibition of the rate of adenine nucleotide translocation is observed. The data are consistent with an effect of butacaine on the process by which adenine nucleotides are transported across the mitochondrial inner membrane rather than on the binding of adenine nucleotides to sites on the adenine nucleotide carrier. The results are briefly discussed in relation to the use of local anaesthetics in investigations of the mechanism of adenine nucleotide translocation.

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