Respiration and oxidative phosphorylation by mitochondria of red and white skeletal muscle

1970 ◽  
Vol 48 (1) ◽  
pp. 27-32 ◽  
Author(s):  
M. Yolanda Alvarado Rigault ◽  
M. C. Blanchaer
Keyword(s):  
Skeletal Muscle ◽  
White Muscle ◽  
Mitochondrial Protein ◽  
Respiratory Control ◽  
Carbohydrate Utilization ◽  
Muscle Mitochondria ◽  
Permeability Characteristics ◽  
Red Muscle ◽  
Muscle Types

Mitochondria from red and white skeletal muscle of the rabbit were compared polarographically with pyruvate–malate, α-glycerophosphate, and NADH as substrates. With pyruvate–malate, the organelles from the two muscle types did not differ in O2 uptake rate ([Formula: see text] mitochondrial protein per minute at 28°) or in ADP/O ratios [Formula: see text]. However, the respiratory control ratios (r.c.r.) were significantly higher in white than in red muscle mitochondria: 5.5 ± 0.3 versus 4.4 ± 0.2 (mean ± s.e.), respectively. The respiration of the white muscle mitochondria with α-glycerophosphate was similar to that with pyruvate–malate and exhibited ADP/O and r.c.r. values of 1.5 ± 0.1 and 3.0 ± 0.1, respectively. The corresponding values for red muscle mitochondria were all lower with this substrate. The organelles from both tissues were uncoupled with NADH as substrate and yielded O2 rates of less than 5% of those with pyruvate–malate.Assuming that the in vivo permeability characteristics of the organelles resemble those described above, it can be calculated that direct penetration of glycolytically generated NADH into the mitochondria would probably be too slow for its reoxidation to occur in either muscle type at a rate compatible with aerobic carbohydrate utilization. However, the intramitochondrial portion of the α-glycerophosphate shuttle has the capacity to transport reducing equivalents to the respiratory chain at the required rate. It is as yet uncertain whether it shares this role with a malate–oxaloacetate shuttle.

Physiological regulation of the expression of a GLUT4 homolog in fish skeletal muscle

2002 ◽  
Vol 283 (1) ◽  
pp. E44-E49 ◽  
Author(s):  
Encarnación Capilla ◽  
Mònica Dı́az ◽  
Joaquim Gutiérrez ◽  
Josep V. Planas
Keyword(s):  
Skeletal Muscle ◽  
Plasma Levels ◽  
White Muscle ◽  
Glucose Transporter ◽  
Physiological Regulation ◽  
Low Protein ◽  
Red Muscle ◽  
High Sequence Homology ◽  
Trout Muscle

We have recently cloned a glucose transporter from brown trout muscle (btGLUT) with high sequence homology to mammalian GLUT4 that is predominantly expressed in red and white skeletal muscle, the two major sites of glucose uptake in trout. To study the physiological regulation of this putative fish GLUT4, we have investigated the expression of btGLUT in red and white skeletal muscle of trout in which blood insulin levels have been altered experimentally. The expression of btGLUT in red muscle increased significantly when insulin plasma levels were elevated by either insulin or arginine treatment and decreased significantly when insulin plasma levels were reduced either by fasting or by feeding a low-protein, high-carbohydrate diet. In contrast, the expression of btGLUT in white muscle was not affected by changes in the plasma levels of insulin. These results strongly suggest that insulin could be regulating the expression of btGLUT in trout red muscle in vivo and set the ground to test the hypothesis that btGLUT may be considered a GLUT4 homolog in fish.

EVIDENCE FOR A DIFFERENT RESPONSE OF RED AND WHITE SKELETAL MUSCLE OF THE RAT IN DIFFERENT THYROID STATES

1978 ◽  
Vol 87 (4) ◽  
pp. 768-775 ◽  
Author(s):  
J. W. Janssen ◽  
C. van Hardeveld ◽  
A. A. H. Kassenaar
Keyword(s):  
Skeletal Muscle ◽  
Body Weight ◽  
Weight Gain ◽  
Protein Content ◽  
White Muscle ◽  
Mitochondrial Protein ◽  
The Body ◽  
Mitochondrial Enzymes ◽  
Muscle Weight ◽  
Red Muscle

ABSTRACT The influence of thyroid hormone depletion and experimental hyperthyroidism on red and white skeletal muscle of the rat during periods of 2, 4 and 8 weeks were studied. Body weight, muscle weight, mitochondrial protein content, and specific activities of the mitochondrial enzymes α-glycerophosphate dehydrogenase (EC 1.1.99.5) (α-GPD) and succinate dehydrogenase (EC 1.3.99.1) (SDH) were used as parameters. The largest differences in body weight gain and muscle weight gain (both red and white muscle) in the hypothyroid rats were seen after 8 weeks of T4 treatment. In the hyperthyroid rats the weight of the red muscle and the ratio of the red muscle weight to the body weight increased, whereas the white muscle weight and the ratio of the white muscle weight to the body weight decreased relative to the control animals. In hypothyroid rats the mitochondrial protein content was lowered in both red and white muscle, the specific α-GPD activity only in the latter. No changes in specific SDH activity were observed in either type of muscle. The hyperthyroid rats showed an increase in the mitochondrial protein content and the specific α-GPD and SDH activity in the red muscle, whereas no significant changes were observed in the white muscle. The changes in the parameters under study show that the effect of the thyroid state differs in red and white muscle. An explanation for a possibly greater sensitivity of red than of white muscle to thyroid hormones is discussed.

Respiration of mitochondria of red and white skeletal muscle

1964 ◽  
Vol 206 (5) ◽  
pp. 1015-1020 ◽  
Author(s):  
M. C. Blanchaer
Keyword(s):  
Skeletal Muscle ◽  
Oxygen Consumption ◽  
White Muscle ◽  
Mitochondrial Respiratory Chain ◽  
Direct Oxidation ◽  
Muscle Mitochondria ◽  
Red Muscle ◽  
Rate Of Oxygen Consumption ◽  
Tightly Coupled ◽  
Reduced Nicotinamide Adenine Dinucleotide

Mitochondria of guinea pig red and white skeletal muscle were isolated in a medium containing 0.25 m sucrose, 1 mm ethylenediamine tetraacetate, and 1% fraction V bovine albumin. Oxidative phosphorylation with pyruvate-malate as substrate was tightly coupled in both types of mitochondria when oxygen uptake was measured over a 2- to 4-min period with a platinum electrode. The P/O ratios approached the theoretical value of 3. Oxygen consumption was also determined manometrically with the substrates 10 mm pyruvate—1 mm malate, 10 mm succinate, 6 mm reduced nicotinamide adenine dinucleotide (NADH2), 20 mm dl-lactate, and 12–20 mm dl-α-glycerophosphate. White muscle mitochondria had a higher rate of oxygen consumption with α-glycerophosphate than with lactate, succinate, and NADH2. Those of red muscle were less active with α-glycerophosphate than with the other substrates. These results indicate that an α-glycerophosphate shuttle may couple the reactions generating NADH2 in the cytoplasm of white muscle with the mitochondrial respiratory chain. The properties of the red muscle mitochondria suggest that the direct oxidation of NADH2 may be more important in this tissue than the α-glycerophosphate shuttle.

Vitamin E prevents hypobaric hypoxia-induced mitochondrial dysfunction in skeletal muscle

2007 ◽  
Vol 113 (12) ◽  
pp. 459-466 ◽  
Author(s):  
José Magalhães ◽  
Rita Ferreira ◽  
Maria J. Neuparth ◽  
Paulo J. Oliveira ◽  
Franklim Marques ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Vitamin E ◽  
Mitochondrial Dysfunction ◽  
Hypobaric Hypoxia ◽  
Mitochondrial Membrane ◽  
Mitochondrial Protein ◽  
Membrane Integrity ◽  
Outer Mitochondrial Membrane ◽  
Hypoxia Exposure

In the present study, the effect of vitamin E (α-tocopherol) on mice skeletal muscle mitochondrial dysfunction and oxidative damage induced by an in vivo acute and severe hypobaric hypoxic insult (48 h at a barometric pressure equivalent to 8500 m) has been investigated. Male mice (n=24) were randomly divided into the following four groups (n=6): control (C), hypoxia (H), vitamin E (VE; 60 mg/kg of body weight intraperitoneally, three times/week for 3 weeks) and hypoxia+VE (HVE). A significant increase in mitochondrial protein CGs (carbonyl groups) was found in the H group compared with the C group. Confirming previous observations from our group, hypoxia induced mitochondrial dysfunction, as identified by altered respiratory parameters. Hypoxia exposure increased Bax content and decreased the Bcl-2/Bax ratio, whereas Bcl-2 remained unchanged. Inner and outer mitochondrial membrane integrity were significantly affected by hypoxia exposure; however, vitamin E treatment attenuated the effect of hypoxia on mitochondrial oxidative phosphorylation and on the levels of CGs. Vitamin E supplementation also prevented the Bax and Bcl-2/Bax ratio impairments caused by hypoxia, as well as the decrease in inner and outer mitochondrial membrane integrity. In conclusion, the results suggest that vitamin E prevents the loss of mitochondrial integrity and function, as well as the increase in Bax content, which suggests that mitochondria are involved in increased cell death induced by severe hypobaric hypoxia in mice skeletal muscle.

scholarly journals Low intrinsic running capacity is associated with reduced skeletal muscle substrate oxidation and lower mitochondrial content in white skeletal muscle

2011 ◽  
Vol 300 (4) ◽  
pp. R835-R843 ◽  
Author(s):  
Donato A. Rivas ◽  
Sarah J. Lessard ◽  
Misato Saito ◽  
Anna M. Friedhuber ◽  
Lauren G. Koch ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Insulin Sensitivity ◽  
Aerobic Capacity ◽  
Artificial Selection ◽  
White Muscle ◽  
Metabolic Diseases ◽  
Metabolic Health ◽  
Mitochondrial Content ◽  
Red Muscle ◽  
Selection For

Chronic metabolic diseases develop from the complex interaction of environmental and genetic factors, although the extent to which each contributes to these disorders is unknown. Here, we test the hypothesis that artificial selection for low intrinsic aerobic running capacity is associated with reduced skeletal muscle metabolism and impaired metabolic health. Rat models for low- (LCR) and high- (HCR) intrinsic running capacity were derived from genetically heterogeneous N:NIH stock for 20 generations. Artificial selection produced a 530% difference in running capacity between LCR/HCR, which was associated with significant functional differences in glucose and lipid handling by skeletal muscle, as assessed by hindlimb perfusion. LCR had reduced rates of skeletal muscle glucose uptake (∼30%; P = 0.04), glucose oxidation (∼50%; P = 0.04), and lipid oxidation (∼40%; P = 0.02). Artificial selection for low aerobic capacity was also linked with reduced molecular signaling, decreased muscle glycogen, and triglyceride storage, and a lower mitochondrial content in skeletal muscle, with the most profound changes to these parameters evident in white rather than red muscle. We show that a low intrinsic aerobic running capacity confers reduced insulin sensitivity in skeletal muscle and is associated with impaired markers of metabolic health compared with high intrinsic running capacity. Furthermore, selection for high running capacity, in the absence of exercise training, endows increased skeletal muscle insulin sensitivity and oxidative capacity in specifically white muscle rather than red muscle. These data provide evidence that differences in white muscle may have a role in the divergent aerobic capacity observed in this generation of LCR/HCR.

scholarly journals Inhibiting myosin-ATPase reveals a dynamic range of mitochondrial respiratory control in skeletal muscle

2011 ◽  
Vol 437 (2) ◽  
pp. 215-222 ◽  
Author(s):  
Christopher G. R. Perry ◽  
Daniel A. Kane ◽  
Chien-Te Lin ◽  
Rachel Kozy ◽  
Brook L. Cathey ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Dynamic Range ◽  
Energy Charge ◽  
Respiratory Control ◽  
Basic Research ◽  
Dependent Manner ◽  
Atpase Inhibitor ◽  
Wide Range ◽  
The Impact

Assessment of mitochondrial ADP-stimulated respiratory kinetics in PmFBs (permeabilized fibre bundles) is increasingly used in clinical diagnostic and basic research settings. However, estimates of the Km for ADP vary considerably (~20–300 μM) and tend to overestimate respiration at rest. Noting that PmFBs spontaneously contract during respiration experiments, we systematically determined the impact of contraction, temperature and oxygenation on ADP-stimulated respiratory kinetics. BLEB (blebbistatin), a myosin II ATPase inhibitor, blocked contraction under all conditions and yielded high Km values for ADP of >~250 and ~80 μM in red and white rat PmFBs respectively. In the absence of BLEB, PmFBs contracted and the Km for ADP decreased ~2–10-fold in a temperature-dependent manner. PmFBs were sensitive to hyperoxia (increased Km) in the absence of BLEB (contracted) at 30 °C but not 37 °C. In PmFBs from humans, contraction elicited high sensitivity to ADP (Km<100 μM), whereas blocking contraction (+BLEB) and including a phosphocreatine/creatine ratio of 2:1 to mimic the resting energetic state yielded a Km for ADP of ~1560 μM, consistent with estimates of in vivo resting respiratory rates of <1% maximum. These results demonstrate that the sensitivity of muscle to ADP varies over a wide range in relation to contractile state and cellular energy charge, providing evidence that enzymatic coupling of energy transfer within skeletal muscle becomes more efficient in the working state.

EFFECTS OF FEEDING AND FOOD DEPRIVATION ON OXYGEN CONSUMPTION, MUSCLE PROTEIN CONCENTRATION AND ACTIVITIES OF ENERGY METABOLISM ENZYMES IN MUSCLE AND BRAIN OF SHALLOW-LIVING (SCORPAENA GUTTATA) AND DEEP-LIVING (SEBASTOLOBUS ALASCANUS) SCORPAENID FISHES

1993 ◽  
Vol 181 (1) ◽  
pp. 213-232 ◽  
Author(s):  
T. H. Yang ◽  
G. N. Somero
Keyword(s):  
Skeletal Muscle ◽  
Metabolic Rate ◽  
Food Deprivation ◽  
Enzyme Activities ◽  
Protein Concentration ◽  
White Muscle ◽  
Muscle Protein ◽  
Metabolism Enzymes ◽  
Red Muscle ◽  
Ad Libitum

The effects of feeding and fasting were examined on the deep-living short-spine thornyhead (Sebastolobus alascanus) and the confamilial shallow-living spotted scorpionfish (Scorpaena guttata) to determine whether the low metabolic rate of the deeper-living species was in part a consequence of food deprivation in its habitat. Laboratory acclimation for periods of 90–115 days under either ad libitum feeding or complete fasting did not lead to similar rates of respiration in individuals of the two species held under identical conditions. Respiration of fish fed ad libitum was 52 % (S. guttata) or 68 % (S. alascanus) higher than for fasted fish of the same species. Furthermore, the metabolic rates of freshly collected specimens of S. alascanus resembled those of laboratory-fasted fish. In white skeletal muscle, both total protein concentration and the activities of four enzymes of ATP metabolism, lactate dehydrogenase (LDH) and pyruvate kinase (PK) of glycolysis, malate dehydrogenase (MDH) and citrate synthase (CS, a citric acid cycle indicator), were lower in S. alascanus than in S. guttata. Within a species, protein concentration and activities of the four enzymes in white muscle, but not in brain, were higher in fed than in starved fish, although these differences were greater in S. alascanus than in S. guttata. During fasting, LDH and PK activity in white muscle of S. alascanus decreased much more than MDH and CS activity; decreases in enzyme activities in red muscle were smaller than those in white muscle. Activities of enzymes in white skeletal muscle of field-collected S. alascanus generally resembled those of the fasted specimens. In contrast, red muscle of field- collected S. alascanus, compared with that of either fed or starved laboratory-held specimens, had a highly glycolytic poise (high LDH and PK activities relative to MDH and CS activities), which may suggest that muscle enzyme activities in the field-collected fish reflect adaptation to the low oxygen level in its adult habitat, the oxygen minimum layer. The strong correlations found between tissue biochemical properties and respiration rate allow us to develop a predictive index for metabolic rate from simple biochemical analyses, e.g. white muscle protein content or CS activity. We conclude that the low metabolic rate of S. alascanus is due to at least four depth-related factors: reduced abundance of food, low temperature, low ambient oxygen concentration and darkness, which may select for reduced locomotory activity.

Temperature effects on pH of mitochondria isolated from carp red muscle

1988 ◽  
Vol 254 (4) ◽  
pp. R611-R615 ◽  
Author(s):  
C. D. Moyes ◽  
L. T. Buck ◽  
P. W. Hochachka
Keyword(s):  
Intracellular Ph ◽  
Temperature Effects ◽  
Respiratory Control ◽  
Ph Gradient ◽  
Carp Cyprinus Carpio ◽  
Red Muscle ◽  
Effects Of Temperature ◽  
Increasing Temperature ◽  
Induced Changes

Mitochondria isolated from red muscle of carp (Cyprinus carpio) were used to investigate the effects of temperature and extramitochondrial pH (pHe) on the mitochondrial pH gradient and respiratory properties. Mitochondria from animals acclimated to 10 degrees C were isolated and incubated in KCl-based media with 0.2 mM lauroylcarnitine (C-12) as substrate. Maximal respiratory control ratios (RCR = state 3/state 4) were 16-18 between pH 6.7 and 7.4 at 10 degrees C; RCR values were 9-12 between pH 6.5 and 7.1 at 30 degrees C. Changes in RCR values were due primarily to changes in the state 3 rate (in the presence of ADP). Mitochondrial pH was determined by measuring 5,5-[2-14C]dimethyloxazolidine-2,4-dione distribution, using [14C]sucrose as an extramatrical marker. The pH gradient was inversely related to pHe. At any particular pHe, the mitochondrial pH gradient decreased with increasing temperature. However, if pHe was varied in the same manner that intracellular pH changes with temperature in vivo, the pH gradient was maintained constant at approximately 0.4 U at 10, 20, and 30 degrees C. These data suggest that carp red muscle mitochondria defend an appropriate mitochondrial pH gradient with temperature-induced changes in intracellular pH.

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

2001 ◽  
Vol 361 (1) ◽  
pp. 49-56 ◽  
Author(s):  
James A. HARPER ◽  
Jeff A. STUART ◽  
Mika B. JEKABSONS ◽  
Damien ROUSSEL ◽  
Kevin M. BRINDLE ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Adipose Tissue ◽  
Uncoupling Protein ◽  
Mitochondrial Protein ◽  
Yeast Mitochondria ◽  
Rat Skeletal Muscle ◽  
Muscle Mitochondria ◽  
Skeletal Muscle Mitochondria ◽  
Uncoupling Protein 3 ◽  
Brown Adipose

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 0.14μg 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 (24–84μg 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.

In Vivo Assimilation by Cod Muscle and Liver Tissue of Elemental Phosphorus from Polluted Sea Water

1970 ◽  
Vol 27 (6) ◽  
pp. 1131-1139 ◽  
Author(s):  
W. J. Dyer ◽  
D. F. Hiltz ◽  
R. G. Ackman ◽  
J. Hingley ◽  
G. L. Fletcher
Keyword(s):  
Lipid Content ◽  
Liver Tissue ◽  
White Muscle ◽  
Content Distribution ◽  
Sea Water ◽  
Elemental Phosphorus ◽  
Red Muscle ◽  
Seawater Environment ◽  
Exposure Levels

Cod rapidly assimilated elemental phosphorus from a seawater environment into their tissues. In a 16-hr exposure to a concentration of 20–80 ppb (parts per billion), phosphorus was concentrated a thousandfold in the liver (even more at lower exposure levels), from 10 to 25 times in white muscle, and about 50–100 times in red muscle. This distribution is roughly in proportion to lipid content. Distribution of the absorbed phosphorus is uniform throughout the white muscle of the fillet, thus facilitating sampling.

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