scholarly journals Electrical Properties of Mitochondrial Membranes

1960 ◽  
Vol 7 (4) ◽  
pp. 589-601 ◽  
Author(s):  
Helmut Pauly ◽  
Lester Packer ◽  
H. P. Schwan
Keyword(s):  
Potassium Chloride ◽  
Chloride Concentration ◽  
Liver Mitochondria ◽  
Ion Concentration ◽  
Rat Liver Mitochondria ◽  
Membrane Capacity ◽  
Internal Conductance ◽  
External Phase ◽  
Electrical Capacity ◽  
Range Of Values

The electrical capacity of the membrane of rat liver mitochondria is 0.5 to 0.6 µ./cm2. This membrane capacity is obtained from the analysis of the frequency dependence of the admittance of a suspension of swollen mitochondria. In potassium chloride media the mitochondrial membrane capacity does not depend on the ion concentration. The internal conductance of the mitochondria was approximately one-half that of the external medium; the same applies if the mitochondria are equilibrated in a medium with a 10-fold difference in potassium chloride concentration. Hence the swollen mitochondria investigated here appear to be able to adjust their internal ion concentration in proportion with that of the external phase. The similarity of the membrane capacity of isolated mitochondria with the range of values known for other membranes suggests a common molecular structure. The analysis of experimental data suggests an anisotropic electrical behavior of the interior of mitochondria. This anisotropy is readily explained by the existence of internal membranes.

scholarly journals The Relationship of Internal Conductance and Membrane Capacity to Mitochondrial Volume

1960 ◽  
Vol 7 (4) ◽  
pp. 603-612 ◽  
Author(s):  
Helmut Pauly ◽  
Lester Packer
Keyword(s):  
External Medium ◽  
Chloride Concentration ◽  
Guinea Pig Heart ◽  
Membrane Capacity ◽  
Internal Conductance ◽  
Electrical Capacity ◽  
Mitochondrial Volume ◽  
Internal Conductivity ◽  
Relationship Of ◽  
The Relationship

A study was made of the effect of mitochondrial size on the electrical properties of the membrane and the internal conductivity of mitochondria. The dielectric constant and electrical conductivity of suspensions of guinea pig heart mitochondria were examined in the frequency range 5 x 105 to 2.5 x 108 C.P.S. Membrane capacity was calculated to be 1.1 to 1.3 µf./cm.2 and was virtually the same in mitochondria whose surface area was made to vary by a factor of 4 by osmotic means. This finding suggested that some mechanism must exist for the transfer of mitochondrial material into membrane structure during fluctuations in mitochondrial size. The electrical capacity of the membrane was unaffected by a 33-fold change in potassium chloride concentration. The internal conductance of swollen mitochondria was 2 to 3 times lower than that of the external medium. In shrunken mitochondria the internal conductance was virtually independent of the conductivity of the external medium. These results were discussed in relation to current concepts of mitochondrial structure.

Characterization of the binding of 3,3′-di-iodo-l-thyronine to rat liver mitochondria

1997 ◽  
Vol 154 (1) ◽  
pp. 119-124
Author(s):  
A Lombardi ◽  
M Moreno ◽  
C Horst ◽  
F Goglia ◽  
A Lanni
Keyword(s):  
Rat Liver ◽  
Binding Capacity ◽  
Specific Binding ◽  
Local Environment ◽  
Liver Mitochondria ◽  
Ion Concentration ◽  
Affinity Constant ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Thyroid State

Abstract The binding of labelled 3,3′-di-iodo-l-thyronine (3,3′-T2) to isolated rat liver mitochondria has been characterized. Specific binding could be detected only in the inner mitochondrial membrane, not in other mitochondrial subfractions. The composition of the incubation medium influenced the binding capacity, the best combination of high specific binding and low non-specific binding being observed in phosphate buffer, pH 6·4. The specific binding of 3,3′-T2 to mitochondria requires low ionic strength: concentrations of K+ and Na+ higher than 10 mmol/l and 0·1 mmol/l respectively resulted in a decreased binding capacity. The optimal calcium ion concentration was in the range 0·01–1·0 mmol/l. Varying magnesium ion, over the range of concentrations used (0·1–100 mmol/l), had no effect. Both ADP and ATP, at over 1 mmol/l, resulted in an inhibition of the specific binding. Incubation with protease resulted in a decrease in specific binding and an increase in non-specific binding, thus indicating the proteic nature of the binding sites. In addition to the above factors in the local environment the thyroid state of the animal might influence the 3,3′-T2-binding capacity. In fact, the thyroid state of the animal seemed not to have an influence on the affinity constant, but it did affect binding capacity. Journal of Endocrinology (1997) 154, 119–124

scholarly journals The regulation of extramitochondrial free calcium ion concentration by rat liver mitochondria

1978 ◽  
Vol 176 (2) ◽  
pp. 463-474 ◽  
Author(s):  
David G. Nicholls
Keyword(s):  
Steady State ◽  
Membrane Potential ◽  
Rat Liver ◽  
Liver Mitochondria ◽  
Weak Acid ◽  
Ion Concentration ◽  
Rat Liver Mitochondria ◽  
Free Calcium ◽  
Electrochemical Gradient

The mechanism whereby rat liver mitochondria regulate the extramitochondrial concentration of free Ca2+ was investigated. At 30°C and pH7.0, mitochondria can maintain a steady-state pCa2+0 (the negative logarithm of the free extramitochondrial Ca2+ concentration) of 6.1 (0.8μm). This represents a true steady state, as slight displacements in pCa2+0 away from 6.1 result in net Ca2+ uptake or efflux in order to restore pCa2+0 to its original value. In the absence of added permeant weak acid, the steady-state pCa2+0 is virtually independent of the Ca2+ accumulated in the matrix until 60nmol of Ca2+/mg of protein has been taken up. The steady-state pCa2+0 is also independent of the membrane potential, as long as the latter parameter is above a critical value. When the membrane potential is below this value, pCa2+0 is variable and appears to be governed by thermodynamic equilibration of Ca2+ across a Ca2+ uniport. Permeant weak acids increase, and N-ethylmaleimide decreases, the capacity of mitochondria to buffer pCa2+0 in the region of 6 (1μm-free Ca2+) while accumulating Ca2+. Permeant acids delay the build-up of the transmembrane pH gradient as Ca2+ is accumulated, and consequently delay the fall in membrane potential to values insufficient to maintain a pCa2+0 of 6. The steady-state pCa2+0 is affected by temperature, incubation pH and Mg2+. The activity of the Ca2+ uniport, rather than that of the respiratory chain, is rate-limiting when pCa2+0 is greater than 5.3 (free Ca2+ less than 5μm). When the Ca2+ electrochemical gradient is in excess, the activity of the uniport decreases by 2-fold for every 0.12 increase in pCa2+0 (fall in free Ca2+). At pCa2+0 6.1, the activity of the Ca2+ uniport is kinetically limited to 5nmol of Ca2+/min per mg of protein, even when the Ca2+ electrochemical gradient is large. A steady-state cycling of Ca2+ through independent influx and efflux pathways provides a model which is kinetically and thermodynamically consistent with the present observations, and which predicts an extremely precise regulation of pCa2+0 by liver mitochondria in vivo.

scholarly journals Intramitochondrial regulation of fatty acid β-oxidation occurs between flavoprotein and ubiquinone A role for changes in the matrix volume

1986 ◽  
Vol 239 (3) ◽  
pp. 559-565 ◽  
Author(s):  
A P Halestrap ◽  
J L Dunlop
Keyword(s):  
Fatty Acid ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Hormonal Stimulation ◽  
Terminal Electron Acceptor ◽  
Matrix Volume ◽  
The Matrix ◽  
Range Of Values ◽  
Stimulation Of

Rat liver mitochondria were incubated in media of different osmolarities and in the presence of various substrates. Rates of oxygen consumption and mitochondrial matrix volumes were measured in the presence and absence of ADP and uncoupler. Duroquinol oxidation was insensitive to matrix volume, whereas other substrates tested showed increased rates of oxidation when the matrix volume increased from 1.0 to 1.5 microliter/mg of protein; this is the range of values measured in situ [Quinlan, Thomas, Armston & Halestrap (1983) Biochem. J. 214, 395-404]. Palmitoylcarnitine, octanoate and butyrate oxidations were particularly sensitive to the matrix volume, increasing from negligible rates to maximal rates within this range. Swelling induced by K+ uptake also stimulated palmitoylcarnitine oxidation. A similar effect of volume on substrate oxidation was seen when ferricyanide in the presence or absence of ubiquinone-1 replaced oxygen as terminal electron acceptor. Measurement of flavoprotein reduction (A 460-480) demonstrated that the locus of the effect of matrix volume is between the electron-transfer flavoprotein and ubiquinone. It is suggested that volume-mediated regulation of fatty acid and proline oxidation may be an important component of the hormonal stimulation of their oxidation.

Comparison of Some Enzyme Systems in Normal and Thyrotoxic Rat Livers

1956 ◽  
Vol 188 (1) ◽  
pp. 35-39 ◽  
Author(s):  
Gladys Feldott Maley
Keyword(s):  
Thyroid Hormone ◽  
Protein Level ◽  
Inorganic Phosphate ◽  
Adenosine Triphosphatase ◽  
Liver Mitochondria ◽  
Ion Concentration ◽  
Rat Liver Mitochondria ◽  
Phosphate Content ◽  
Enzyme Systems ◽  
Rat Livers

The activity of the following enzymes and enzyme systems have been shown to increase above the normal in the mitochondria from thyrotoxic rats' livers: over-all glutamate oxidation, succinoxidase, cytochrome oxidase, cytochrome c, and adenosine triphosphatase. During hypothyroidism the activity of these enzymes decreases. Mg++ ion concentration was not influenced by the thyroid hormone. The latent ATPase4 of thyrotoxic rat liver mitochondria is activated by shorter preaging periods at 37° than that of normal. In a whole homogenate of these same tissues the glucose-6-phosphatase activity, inorganic phosphate content and apparent protein level was also increased during thyrotoxicity.

Effects of 5-5'-Diphenyl-2-thiohydantoin (DPTH) and Thyroxine on the Ultrastructure and Chemical Composition of Rat Liver

1971 ◽  
Vol 29 ◽  
pp. 570-571
Author(s):  
E. A. Elfont ◽  
R. B. Tobin ◽  
D. G. Colton ◽  
M. A. Mehlman
Keyword(s):  
Chemical Composition ◽  
Rat Liver ◽  
Future Study ◽  
Mode Of Action ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Effective Inhibitor ◽  
Biochemical Effects ◽  
Glycerophosphate Dehydrogenase ◽  
Stimulation Of

Summary5,-5'-diphenyl-2-thiohydantoin (DPTH) is an effective inhibitor of thyroxine (T4) stimulation of α-glycerophosphate dehydrogenase in rat liver mitochondria. Because this finding indicated a possible tool for future study of the mode of action of thyroxine, the ultrastructural and biochemical effects of DPTH and/or thyroxine on rat liver mere investigated.Rats were fed either standard or DPTH (0.06%) diet for 30 days before T4 (250 ug/kg/day) was injected. Injection of T4 occurred daily for 10 days prior to sacrifice. After removal of the liver and kidneys, part of the tissue was frozen at -50°C for later biocheailcal analyses, while the rest was prefixed in buffered 3.5X glutaraldehyde (390 mOs) and post-fixed in buffered 1Z OsO4 (376 mOs). Tissues were embedded in Araldlte 502 and the sections examined in a Zeiss EM 9S.Hepatocytes from hyperthyroid rats (Fig. 2) demonstrated enlarged and more numerous mitochondria than those of controls (Fig. 1). Glycogen was almost totally absent from the cytoplasm of the T4-treated rats.

Two isoprenylated flavonoids from Dorstenia psilurus activate AMPK, stimulate glucose uptake, inhibit glucose production and lower glycemia

2019 ◽  
Vol 476 (24) ◽  
pp. 3687-3704 ◽  
Author(s):  
Aphrodite T. Choumessi ◽  
Manuel Johanns ◽  
Claire Beaufay ◽  
Marie-France Herent ◽  
Vincent Stroobant ◽  
...  
Keyword(s):  
Glucose Uptake ◽  
Human Cancer ◽  
Glucose Production ◽  
Liver Mitochondria ◽  
New Drugs ◽  
Structural Isomer ◽  
Rat Liver Mitochondria ◽  
Ionization Mass ◽  
Ampk Activation ◽  
Starting Point

Root extracts of a Cameroon medicinal plant, Dorstenia psilurus, were purified by screening for AMP-activated protein kinase (AMPK) activation in incubated mouse embryo fibroblasts (MEFs). Two isoprenylated flavones that activated AMPK were isolated. Compound 1 was identified as artelasticin by high-resolution electrospray ionization mass spectrometry and 2D-NMR while its structural isomer, compound 2, was isolated for the first time and differed only by the position of one double bond on one isoprenyl substituent. Treatment of MEFs with purified compound 1 or compound 2 led to rapid and robust AMPK activation at low micromolar concentrations and increased the intracellular AMP:ATP ratio. In oxygen consumption experiments on isolated rat liver mitochondria, compound 1 and compound 2 inhibited complex II of the electron transport chain and in freeze–thawed mitochondria succinate dehydrogenase was inhibited. In incubated rat skeletal muscles, both compounds activated AMPK and stimulated glucose uptake. Moreover, these effects were lost in muscles pre-incubated with AMPK inhibitor SBI-0206965, suggesting AMPK dependency. Incubation of mouse hepatocytes with compound 1 or compound 2 led to AMPK activation, but glucose production was decreased in hepatocytes from both wild-type and AMPKβ1−/− mice, suggesting that this effect was not AMPK-dependent. However, when administered intraperitoneally to high-fat diet-induced insulin-resistant mice, compound 1 and compound 2 had blood glucose-lowering effects. In addition, compound 1 and compound 2 reduced the viability of several human cancer cells in culture. The flavonoids we have identified could be a starting point for the development of new drugs to treat type 2 diabetes.

Energy and Antioxidant Status of Rat Liver Mitochondria during Hypoxia- Reoxygenation of Different Duration

2016 ◽  
Vol 7 (4) ◽  
pp. 349-361
Author(s):  
Olga A. Gonchar ◽  
Valentina I. Nosar ◽  
Larisa. V. Bratus ◽  
I. N. Tymchenko ◽  
N. N. Steshenko ◽  
...  
Keyword(s):  
Rat Liver ◽  
Antioxidant Status ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Hypoxia Reoxygenation

Modelling of Solute Transfer to Surface Runoff

1992 ◽  
Vol 26 (7-8) ◽  
pp. 1851-1856 ◽  
Author(s):  
J. L. Lai ◽  
K. S. L. Lo
Keyword(s):  
Potassium Chloride ◽  
Surface Runoff ◽  
Laboratory Experiments ◽  
Overland Flow ◽  
Chloride Concentration ◽  
Runoff Water ◽  
Mixing Depth ◽  
Change Rate ◽  
Solute Transfer ◽  
The Media

A mixing-based model for describing solute transfer to overland flow was developed. This model included a time-dependent mixing depth of the top layer and a complete-mixed surface runoff zone. In a series of laboratory experiments, runoff was passed at various velocities and depths over a medium bed. The media were saturated with uniform concentration of potassium chloride solution. Runoff water was sampled at the beginning and end of the flume and the potassium chloride concentration analyzed. Using this model, dimensionless ultimate mixing depth and dimensionless change rate of mixing depth from experimental data were investigated and implemented. The results showed that the Reynolds number and relative roughness are two important factors.

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