Phospholipid topology of the inner mitochondrial membrane of rat liver

Biochemistry ◽  
1979 ◽  
Vol 18 (11) ◽  
pp. 2407-2414 ◽  
Author(s):  
Richard C. Crain ◽  
Guido V. Marinetti
Keyword(s):  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Inner Mitochondrial Membrane

scholarly journals Uptake of protoporphyrin IX by isolated rat liver mitochondria

1980 ◽  
Vol 188 (2) ◽  
pp. 329-335 ◽  
Author(s):  
M E Koller ◽  
I Romslo
Keyword(s):  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Protoporphyrin Ix ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Erythropoietic Protoporphyria ◽  
Inner Membrane ◽  
Isolated Rat Liver ◽  
Isolated Rat

Rat liver mitochondria accumulate protoporphyrin IX from the suspending medium into the inner membrane in parallel with the magnitude of the transmembrane K+ gradient (K+in/K+out). Only protoporphyrin IX taken up in parallel with the transmembrane K+ gradient is available for haem synthesis. Coproporphyrins (isomers I and III) are not taken up by the mitochondria. The results support the suggestion by Elder & Evans [(1978) Biochem. J. 172, 345-347] that the prophyrin to be taken up by the inner mitochondrial membrane belongs to the protoporphyrin(ogen) IX series. Protoporphyrin IX at concentrations above 15 nmol/mg of protein has detrimental effects on the structural and functional integrity of the mitochondria. The relevance of these effects to the hepatic lesion in erythropoietic protoporphyria is discussed.

scholarly journals The maturation of the inner membrane of foetal rat liver mitochondria. An example of a positive-feedback mechanism

1975 ◽  
Vol 150 (3) ◽  
pp. 477-488 ◽  
Author(s):  
J K Pollak
Keyword(s):  
Oxidative Phosphorylation ◽  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Respiratory Control ◽  
Liver Mitochondria ◽  
Neonatal Rat ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Mature Adult ◽  
Foetal Rat

A new method was devised for the isolation of foetal and neonatal rat lvier mitochondria, giving higher yields than conventional methods. 2. During development from the perinatal period to the mature adult, the ratio of cytochrome oxidase/succinate-cytochrome c reductase changes. 3. The inner mitochondrial membrane of foetal liver mitochondria possesses virtually no osmotic activity; the permeability to sucrose decreases with increasing developmental age. 4. Foetal rat liver mitochondria possess only marginal respiratory control and do not maintain Ca2+-induced respiration; they also swell in respiratory-control medium in the absence of substrate. ATP enhances respiratory control and prevents swelling, adenylyl imidodiphosphate, ATP+atractyloside enhance the R.C.I. (respiratory control index), Ca2+-induced respiratory control and prevent swelling, whereas GTP and low concentrations of ADP have none of these actions. It is concluded that the effect of ATP depends on steric interaction with the inner mitochondrial membrane. 5. When 1-day pre-partum foetuses are obtained by Caesarean section and maintained in a Humidicrib for 90 min, mitochondrial maturation is ‘triggered’, so that their R.C.I. is enhanced and no ATP is required to support Ca2+-dependent respiratory control or to inhibit mitochondrial swelling. 6. It is concluded that foetal rat liver mitochondria in utero do not respire, although they are capable of oxidative phosphorylation in spite of their low R.C.I. The different environmental conditions which the neonatal rat encounters ex utero enable the hepatic mitochondria to produce ATP, which interacts with the inner mitochondrial membrane to enhance oxidative phosphorylation by an autocatalytic mechanism.

scholarly journals Intramitochondrial localization of δ-aminolaevulate synthetase and ferrochelatase in rat liver

1969 ◽  
Vol 114 (3) ◽  
pp. 455-461 ◽  
Author(s):  
Roxane McKay ◽  
R. Druyan ◽  
G. S. Getz ◽  
M. Rabinowitz
Keyword(s):  
Glutamate Dehydrogenase ◽  
Density Gradient ◽  
Malate Dehydrogenase ◽  
Rat Liver ◽  
Mitochondrial Biogenesis ◽  
Mitochondrial Membrane ◽  
Density Gradient Centrifugation ◽  
Gradient Centrifugation ◽  
Differential Centrifugation ◽  
Inner Mitochondrial Membrane

Intramitochondrial loci for δ-aminolaevulate synthetase and ferrochelatase, the initial and final enzymes in haem synthesis, have been found in rat liver. Two different methods of fractionation were applied to mitochondria: (a) sonication and density-gradient centrifugation; (b) treatment with digitonin and differential centrifugation. Similar results were obtained with each technique. δ-Aminolaevulate synthetase is distributed similarly to two known matrix enzymes, malate dehydrogenase and glutamate dehydrogenase. Ferrochelatase is firmly bound to the the inner mitochondrial membrane. These results are considered in terms of the regulation of haem synthesis and in relation to mitochondrial biogenesis.

Accumulation of D-arginine by rat liver mitochondria

1987 ◽  
Vol 65 (12) ◽  
pp. 1057-1063 ◽  
Author(s):  
Rafael Villalobos-Molina ◽  
J. Pablo Pardo ◽  
Alfredo Saavedra-Molina ◽  
Enrique Piña
Keyword(s):  
Membrane Potential ◽  
Rat Liver ◽  
Mitochondrial Respiration ◽  
Mitochondrial Membrane ◽  
Liver Mitochondria ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Osmotic Swelling ◽  
Dose Dependent Fashion ◽  
Dose Dependent

The permeability of the inner mitochondrial membrane from rat liver to D-arginine was studied. By using safranin as a probe of the membrane potential, depolarization of energized liver mitochondria occurred in a dose-dependent fashion starting at 3.3 mmol/L of D- or DL-arginine. When ethidium bromide fluorescence was employed, a decrease in the membrane potential due to D- or DL-arginine was observed. A parallel significant change in succinate-induced respiration in rat liver mitochondria was found in response to osmotic swelling in 125 mmol/L of D-arginine salts. L-Arginine, L-glutamine, L-asparagine, L-ornithine, D-ornithine, and L-lysine did not modify the membrane potential at the concentrations tested. D-Arginine was not transformed into citrulline, but 1.0 mmol/L of the D-amino acid inhibited, by 42%, the state 3 of mitochondrial respiration using succinate as substrate. When D-arginine was used in combination with nigericin, a 40% inhibition of mitochondrial respiration in state 3 was recorded with succinate and with glutamate–malate as substrates.

scholarly journals Structural properties of phospholipids in the rat liver inner mitochondrial membrane. A 31P-NMR study

1980 ◽  
Vol 600 (3) ◽  
pp. 625-635 ◽  
Author(s):  
P.R. Cullis ◽  
B. de Kruijff ◽  
M.J. Hope ◽  
R. Nayar ◽  
A. Rietveld ◽  
...  
Keyword(s):  
Structural Properties ◽  
Rat Liver ◽  
Mitochondrial Membrane ◽  
31P Nmr ◽  
Inner Mitochondrial Membrane ◽  
Nmr Study

scholarly journals Acetyl-coenzyme A hydrolase, an artifact? The conversion of acetyl-coenzyme A into acetate by the combined action of carnitine acetyltransferase and acetylcarnitine hydrolase

1975 ◽  
Vol 152 (2) ◽  
pp. 167-172 ◽  
Author(s):  
N. D. Costa ◽  
A. M. Snoswell
Keyword(s):  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Hydrolase Activity ◽  
Carnitine Acetyltransferase ◽  
Inner Mitochondrial Membrane ◽  
Acetyl Coa ◽  
Acetyl Coenzyme A ◽  
Sheep Liver ◽  
Liver Homogenates ◽  
Coa Hydrolase

1. The nature of the acetyl-CoA hydrolase (EC 3.1.2.1) reaction in rat and sheep liver homogenates was investigated. 2. The activity determined in an incubated system was 5.10 and 3.28nmol/min per mg of protein for rat and sheep liver homogenate respectively. This activity was not affected by the addition of l-carnitine, but was decreased by the addition of d-carnitine. 3. No acetyl-CoA hydrolase activity could be detected in rat or sheep liver homogenates first treated with Sephadex G-25. This treatment decreased the carnitine concentrations of the homogenates to about one-twentieth. Subsequent addition of l-carnitine, but not d-carnitine, restored the apparent acetyl-CoA hydrolase activity. 4. Sephadex treatment did not affect acetyl-carnitine hydrolase activity of the homogenates, which was 5.8 and 8.1nmol/min per mg of protein respectively for rat and sheep liver. 5. Direct spectrophotometric assay of acetyl-CoA hydrolase, based on the reaction of CoA released with 5,5′-dithiobis-(2-nitrobenzoic acid), clearly demonstrated that after Sephadex treatment no activity could be measured. 6. Carnitine acetyltransferase (EC 2.3.1.7) activity measured in the same assay system in response to added l-carnitine was very low in normal rat liver homogenates, owing to the apparent high acetyl-CoA hydrolase activity, but was increased markedly after Sephadex treatment. The Vmax. for this enzyme in rat liver homogenates was increased from 3.4 to 14.8nmol/min per mg of protein whereas the Km for l-carnitine was decreased from 936 to 32μm after Sephadex treatment. 7. Acetyl-CoA hydrolase activity could be demonstrated in disrupted rat liver mitochondria but not in separated outer or inner mitochondrial membrane fractions. Activity could be demonstrated after recombination of outer and inner mitochondrial membrane fractions. The outer mitochondrial membrane fraction showed acetylcarnitine hydrolase activity and the inner mitochondrial membrane fraction showed carnitine acetyltransferase activity. 8. The results presented here demonstrate that acetyl-CoA hydrolase activity in rat and sheep liver is an artifact and the activity is due to the combined activity of carnitine acetyltransferase and acetylcarnitine hydrolase.

01 A proteomic database of rat liver inner mitochondrial membrane proteins

2002 ◽  
Vol 34 (7) ◽  
pp. A29
Author(s):  
Todd McDonald ◽  
Irina Neverova ◽  
Young Ko ◽  
Pete L. Pedersen ◽  
Jennifer E. Van Eyk
Keyword(s):  
Membrane Proteins ◽  
Rat Liver ◽  
Mitochondrial Membrane ◽  
Inner Mitochondrial Membrane

scholarly journals Calcium ion cycling in rat liver mitochondria

1978 ◽  
Vol 174 (2) ◽  
pp. 613-620 ◽  
Author(s):  
Chidambaram Ramachandran ◽  
Fyfe L. Bygrave
Keyword(s):  
Rat Liver ◽  
Calcium Ion ◽  
Mitochondrial Membrane ◽  
Initial Rate ◽  
Liver Mitochondria ◽  
Ruthenium Red ◽  
Rat Liver Mitochondria ◽  
Inner Mitochondrial Membrane ◽  
Subsequent Addition ◽  
Unique Mechanism

1. Addition of N-ethylmaleimide to rat liver mitochondria respiring with succinate as substrate decreases both the initial rate of Ca2+ transport and the ability of mitochondria to retain Ca2+. As a result, Ca2+ begins to leave the mitochondria soon after it has entered. Half-maximal effects occur at an N-ethylmaleimide concentration of about 100nmol/mg of protein. 2. The efflux of Ca2+ induced by N-ethylmaleimide is not prevented by Mg2+ or by Ruthenium Red at concentrations known to prevent Ca2+ efflux when exogenous phosphate also is present. Swelling of mitochondria does not accompany N-ethylmaleimide-induced Ca2+ efflux. 3. Addition of Ca2+ to rat liver mitochondria in the presence of N-ethylmaleimide produces an immediate decrease in ΔE (membrane potential), which decreases further to only a slight extent over the next 8min. Concomitant with this is an immediate increase and then levelling off of the −59ΔpH (transmembrane pH gradient). 4. Preincubation of rat liver mitochondria with p-chloromercuribenzenesulphonate, which by contrast with N-ethylmaleimide is unable to penetrate the inner mitochondrial membrane, also prevents Ca2+ retention. The ΔE and −59ΔpH respond to Ca2+ addition in a manner similar to that which occurs when N-ethylmaleimide is present. Subsequent addition of mercaptoethanol produces an immediate increase in both ΔE and −59ΔpH. At the same time Ca2+ is rapidly accumulated by the organelles. 5. The above data are interpreted as indicating that under the conditions of Ca2+ efflux seen here, the mitochondria retain their functional integrity. This contrasts with the uncoupling effect of Ca2+ seen in the presence of Pi, which generally leads to a loss of mitochondrial integrity. We suggest that a unique mechanism of Ca2+ cycling is able to take place when mitochondria have been treated with N-ethylmaleimide.

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