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PubMed1976

Monamine oxidase in outer membrane of skeletal muscle mitochondria.

(1) Monoamine oxidase (EC 1.4.3.4) is present in rat skeletal muscle mitochondria. (2) A radioassay procedure for the assay of monoamine oxidase in muscle mitochondria is described. It is based on teh procedure using side-chain [2-14C]-tryptamine as substate described by Wurtman, R.J. and Axelrod, J. (1963) Biochem. Pharmacol. 12, 1439--1441 and employs a pH of 8.0 and a substrate concentration of 0.25 mM. (3) The Km of the muscle mitochondrial enzyme at pH 8.0 is 1.34 - 10(-5) M and that of the liver enzyme under the same conditions is 2.5 - 10(-5) M. Muscle mitochondria contain only one quarter of the activity of enzyme present in liver mitochondria. (4) Monoamine oxidase is shown to be in the outer membrane of skeletal muscle mitochondria and thus to be a suitable marker enzyme for use in the fractionation of these mitochondria.

Animals↗
PubMed1986

Anisakis simplex: uncoupling of oxidative phosphorylation in the muscle mitochondria of infected fish.

Adenosine triphosphatase activity stimulated by Mg2+ was greater in muscle mitochondria of fish infected with larval Anisakis simplex nematodes than in uninfected fish. When muscle mitochondria were isolated in a sucrose ethylene-glycol bis(beta-aminoethyl ether)N,N'-tetraacetic acid medium from fresh uninfected fish, they were loosely coupled, and their adenosine triphosphatase activity was comparable to that of mitochondria from rat tissue. Activity in infected fish was dose dependent, increasing with the number of worms per fish. Excretory secretory products or a cytoplasmic fraction of anisakines, when incubated with coupled rat mitochondria, also caused adenosine triphosphatase activity to increase. Storage of fish flesh caused an increase in adenosine triphosphatase activity, but such aging was not significant until 5 and 10 days after death in refrigerated and frozen samples, respectively. The Mg2+ stimulated adenosine triphosphatase activity of muscle mitochondria can be used to estimate the number of nematodes per market fish. The type of medium used to isolate the mitochondria is crucial in such studies; an ionic medium with Nagarse proteinase was optimal for fish muscle mitochondria.

2,4-Dinitrophenol↗
PubMed1980

Fatty acid metabolism in skeletal muscle mitochondria from two strains of dystrophic mice.

Several aspects of fatty acids metabolism have been examined in skeletal muscle mitochondria from both strain 129 dystrophic (dy/dy) and myodystrophic (myd/myd) mice. Skeletal muscle mitochondria from dy/dy mice showed significantly decreased state 3 respiratory rates with both palmityl- and acetyl-carnitine + malate as substrates when compared with their normal littermate controls. A similar, though less severe impairment in acylcarnitine oxidation by mitochondria from myd/myd skeletal muscle has also been shown by us in a previous study. In the present study, kinetic measurements revealed decreased activities of the reverse carnitine palmityltransferase (palmitylcarnitine + CoASH as substrates) in intact mitochondria from dy/dy muscle, and of citrate synthase in myd/myd muscle mitochondria. However, neither of these reactions appeared to be rate limiting for acylcarnitine oxidation in mouse skeletal muscle mitochondria. All other enzyme activities of cofactor contents measured were either comparable to those of controls or were higher. The results reported here indicate that neither of the impairments in acylcarnitine oxidation by skeletal muscle mitochondria from dy/dy or myd/myd mice is due to deficiencies in either carnitine palmityltransferase, carnitine acetyltransferase, citrate synthase, coenzyme A, or substrate-reducible flavoprotein.

Acetylcarnitine↗
PubMed2002

Artifactual uncoupling by uncoupling protein 3 in yeast mitochondria at the concentrations found in mouse and rat skeletal-muscle mitochondria.

Western blots detected uncoupling protein 3 (UCP3) in skeletal-muscle mitochondria from wild-type but not UCP3 knock-out mice. Calibration with purified recombinant UCP3 showed that mouse and rat skeletal muscle contained 0.14 microg of UCP3/mg of mitochondrial protein. This very low UCP3 content is 200-700-fold less than the concentration of UCP1 in brown-adipose-tissue mitochondria from warm-adapted hamster (24-84 microg of UCP1/mg of mitochondrial protein). UCP3 was present in brown-adipose-tissue mitochondria from warm-adapted rats but was undetectable in rat heart mitochondria. We expressed human UCP3 in yeast mitochondria at levels similar to, double and 7-fold those found in rodent skeletal-muscle mitochondria. Yeast mitochondria containing UCP3 were more uncoupled than empty-vector controls, particularly at concentrations that were 7-fold physiological. However, uncoupling by UCP3 was not stimulated by the known activators palmitate and superoxide; neither were they inhibited by GDP, suggesting that the observed uncoupling was a property of non-native protein. As a control, UCP1 was expressed in yeast mitochondria at similar concentrations to that of UCP3 and at up to 50% of the physiological level of UCP1. Low levels of UCP1 gave palmitate-dependent and GDP-sensitive proton conductance but higher levels of UCP1 caused an additional GDP-insensitive uncoupling artifact. We conclude that the uncoupling of yeast mitochondria by high levels of UCP3 expression is entirely an artifact and provides no evidence for any native uncoupling activity of the protein.

Adipose Tissue, Brown↗
PubMed1956

The structure of pigeon breast muscle mitochondria.

The structure of pigeon breast muscle mitochondria was studied both in whole muscle tissue and in mitochondrial fractions separated by differential centrifugation. No evidence was found to indicate that the mitochondria of pigeon breast muscle differ in any fundamental way from those of other tissues. In particular the absence of an enveloping membrane, claimed in recent reports, was not confirmed. The structure of the lipide bodies present in muscle has been described, and compared with that of similar bodies in other tissues.

Animals↗
PubMed1999

Electron Leak Causes Proton Leak in Skeletal Muscle Mitochondria in Exercise-induced Fatigue.

Using an animal model of exercise-induced fatigue by incremental exercise to exhaustion on a motor-driven treadmill, the changes of the mitochondrial proton leak and electron leak in mitochondria of skeletal muscle from rats immediately after exhaustive exercise were observed. The results showed that, in exercise-induced fatigue conditions, superoxide anions of rat skeletal muscle mitochondria increased State 4 respiration rate significantly accelerated and respiration control ratio clearly decreased. Results show that, in the condition of exercise-induced fatigue, the increased mitochondrial proton leak and electron leak may be important factors that cause the decrease in coupling of oxidative phosphorylation. Our results provide evidence supporting a hypothesis that electron leak causes proton leak in mitochondria.

Journal Article↗
PubMed1975

Properties of Ascaris muscle mitochondria. 1. Cytochromes.

1. The cytochrome system in Ascaris muscle mitochondria was further characterized using purer preparations. 2. Difference spectra (at 22 degrees C and -196 degrees C) of the mitochondrial preparations using succinate and ascorbate plus N,N,N' ,N'-tetramethyl-p-phenylenediamine show that Ascaris muscle mitochondria contain cytochromes c1, c and aa3, and also at least three b-type cytochromes. The b-type cytochrome is the predominant component. 3. Cytochrome c and Ascaris cytochrome b-560 can be extracted from the mitochondrial preparations with 150mM KCl, leaving the membrane-bound cytochromes c1, b and aa3 in the KCl residue.

Animals↗
PubMed1976

Age-related changes in the flight muscle mitochondria from the blowfly Sarcophaga bullata.

Flight muscle mitochondria have been isolated from female blowflies (Sarcophaga bullata) of different ages, alpha-Glycerophosphate and pyruvate-proline respiration rates increase during development. Only pyruvate-proline respiration declines toward senescence (30%). This decline can be overcome by ATP-NaHCO3. Cytochrome concentrations and hydrogen peroxide generation rates per protein increase during development but remain constant thereafter. Total NAD+ of metabolically completely oxidized mitochondria decreases during development; a small decline occurs between mature and senescent mitochondria. Respiring young mitochondria do not swell in potassium isethionate, very little in potassium chloride, and relatively slowly in potassium acetate. Mature and senescent mitochondria do swell in these three salts but cannot be differentiated from each other on this basis. None of the preparations swells in sodium chloride, sodium- or potassium Mops. While many differences exist between young and mature mitochondria, only the decline in pyruvate-proline respiration distinguishes mature from senescent mitochondria.

Aging↗
PubMed1983

[Oxidative metabolism of rat skeletal muscle mitochondria in adaptation to cold].

In control and cold-adapted rats the oxygen consumption was measured polarographically in isolated mitochondria of gastrocnemic and soleus muscles before denervation and 60 min afterwards. Muscle denervation decreased the direct oxidation intensity in both the groups of rats. Unlike, the intensity of phosphorylation in cold-adapted animals increased following the denervation in the soleus muscle, and decreased in the gastrocnemic muscle, whereas no changes were evident in the control rats. It is concluded that the adaptation to cold may augment the dependence of oxidative metabolism in muscle mitochondria on the central nervous control.

Adaptation, Physiological↗
PubMed2000

Comparative study on uncoupling effects of laurate and lauryl sulfate on rat liver and skeletal muscle mitochondria.

Uncoupling effects of laurate and lauryl sulfate have been studied in the isolated rat liver and skeletal muscle mitochondria. In the oligomycin-treated liver mitochondria, 0.02 mM laurate or 0.16 mM lauryl sulfate caused a two-fold stimulation of respiration, accompanied by a membrane potential decrease. Carboxyatractylate (CAtr) and glutamate (or aspartate) strongly decrease the effect of laurate and lauryl sulfate on respiratory rate and membrane potential (the recoupling effect). With both uncouplers, this effect is maximal for CAtr and glutamate (aspartate) at pH 7.8 and 7.0, respectively. Tetraphenyl phosphonium cations, which decrease negative membrane charges, cause an alkaline shift of these pH dependences. Small amounts of lauryl sulfate, which increase the membrane negative charge, induce the opposite shift when laurate is used as an uncoupler. ADP, but not GDP, partially recouple with both laurate and lauryl sulfate. We conclude that lauryl sulfate-induced uncoupling in rat liver, like the uncoupling induced by laurate, is mediated by the ATP/ ADP and glutamate/aspartate antiporters. In skeletal muscle mitochondria uncoupled by laurate, 200 microM GDP causes partial recoupling which can be enhanced by a subsequent additions of CAtr, glutamate and serum albumin. CAtr added before GDP promotes a larger recoupling than when added after GDP and prevents the subsequent effect of GDP. ADP is effective as recoupler at lower concentrations that GDP, whereas CDP is without influence. Lauryl sulfate uncoupling of skeletal muscle mitochondria is GDP-resistant but is sensitive to ADP, CAtr, glutamate and serum albumin. Our data suggest that in skeletal muscle mitochondria a GDP-sensitive mechanism is involved in uncoupling induced by laurate. This mechanism is absent in liver mitochondria. Possible mechanisms of laurate and lauryl sulfate-induced uncoupling are discussed.

Adenosine Triphosphate↗
PubMed1992

Regulating effect of mitochondrial lactate dehydrogenase on oxidation of cytoplasmic NADH via an "external" pathway in skeletal muscle mitochondria.

1. The specific activity of lactate dehydrogenase of skeletal muscle mitochondria was found to be 2.5 times lower than specific activity of total NADH-cytochrome c reductase. 2. The specific activity of mitochondrial LDH in skeletal muscle mitochondria was almost equal to the activity of rotenone-insensitive NADH-cytochrome c reductase. 3. Mitochondrial LDH acting as an oxidase of lactate to pyruvate may feed an "external" pathway, but the activity of the mitochondrial enzyme is a limiting factor in oxidation of lactate-derived NADH. 4. Mitochondrial LDH acting as a reductase of pyruvate to lactate successfully competes with an "external" pathway for cytoplasmic NADH. 5. Exogenous NADH oxidation via an "external" pathway was inhibited by pyruvic acid. This inhibition was overcome by addition of oxamic acid or hydrazine.

Animals↗
PubMedDate not supplied

[Various properties of the creatine transport system and the location of creatine kinase in skeletal muscle mitochondria].

Water and creatine contents were studied in rat skeletal muscle mitochondria after their 5 min. incubation in creatine solutions, pH 7.2 or 8.4. The content of water and creatine in mitochondria was found to be higher at pH 8.4, than at pH 72, the creatine content correlated with the water content. Structural creatine analogues, containing aminogroups with pKa greater than or equal to 9.5 or carboxyl groups, inhibited the infusion of creatine into mitochondria more strongly than substances having aminogroups with pKa less than 5. The penetrating form is creatine amphiion; the effect of pH on the permeability is probably due to the activation of the creatine transmitter. Rat skeletal muscle mitochondria contain creatine kinase at both sides of the inner membrane. This conclusion is based on the fact that under conditions, supplying the direct course of the creatine kinase reaction (the incubation medium contains Ca2+ and creatine; pH 7.8), ADP produces the stimulation of mitochondrial respiration up to the oxygen exhausting in a polarographic unit. Similarly, ADP irreversibly stimulates mitochondrial respiration in the presence of 1 mM EDTA, if EDTA and ADP are added after the preincubation of mitochondria in creatine-containing medium and after accumulating small amounts of Ca2+ by mitochondria.

Adenosine Diphosphate↗
PubMed1992

Proline transport by tsetse fly Glossina morsitans flight muscle mitochondria.

1. Proline accumulation by tsetse fly Glossina morsitans flight muscle mitochondria was studied in vitro by the swelling technique and direct measurement of (U-14C) proline. 2. Proline transport was inhibited by the uncharged liposoluble -SH reagent, N-ethylmaleimide but not by ionic reagent, mersalyl, suggesting that the -SH groups involved in the transport of proline are located in a hydrophobic part of the membrane or on the matrix side of the membrane. 3. The kinetic study of proline accumulation revealed saturation kinetics and a high temperature dependence. It gave a Km of 85 microM and a Vmax of 962 pmol/min/mg protein and an activation energy (Ea) of 11 kcal/mol. 4. Certain other amino acids (L-valine, L-alanine, L-methionine, L-phenylalanine, L-tryptophan and L-hydroxyproline) significantly stimulated proline uptake. 5. These observations indicate that tsetse fly Glossina morsitans flight muscle mitochondria contain a proline transport mechanism.

Adenosine Diphosphate↗