scholarly journals Oxidative properties of carp red and white muscle

1989 ◽  
Vol 143 (1) ◽  
pp. 321-331 ◽  
Author(s):  
C. D. Moyes ◽  
L. T. Buck ◽  
P. W. Hochachka ◽  
R. K. Suarez
Keyword(s):  
Amino Acids ◽  
White Muscle ◽  
Citrate Synthase ◽  
Ketone Bodies ◽  
Redox Balance ◽  
Fatty Acyl ◽  
Oxidation Rates ◽  
Substrate Preferences ◽  
Glycerophosphate Dehydrogenase ◽  
Wide Range

Substrate preferences of isolated mitochondria and maximal enzyme activities were used to assess the oxidative capacities of red muscle (RM) and white muscle (WM) of carp (Cyprinus carpio). A 14-fold higher activity of citrate synthase (CS) in RM reflects the higher mitochondrial density in this tissue. RM mitochondria oxidize pyruvate and fatty acyl carnitines (8:O, 12:O, 16:O) at similarly high rates. WM mitochondria oxidize these fatty acyl carnitines at 35–70% the rate of pyruvate, depending on chain length. WM has only half the carnitine palmitoyl transferase/CS ratio of RM, but similar ratios of beta-hydroxyacyl CoA dehydrogenase/CS. Ketone bodies are poor substrates for mitochondria from both tissues. In both tissues mitochondrial alpha-glycerophosphate oxidation was minimal, and alpha-glycerophosphate dehydrogenase was present at low activities, suggesting the alpha-glycerophosphate shuttle is of minor significance in maintaining cytosolic redox balance in either tissue. The mitochondrial oxidation rates of other substrates relative to pyruvate are as follows: alpha-ketoglutarate 90% (RM and WM); glutamate 45% (WM) and 70% (RM); proline 20% (WM) and 45% (RM). Oxidation of neutral amino acids (serine, glycine, alanine, beta-alanine) was not consistently detectable. These data suggest that RM and WM differ in mitochondrial properties as well as mitochondrial abundance. Whereas RM mitochondria appear to be able to utilize a wide range of metabolic fuels (fatty acids, pyruvate, amino acids but not ketone bodies), WM mitochondria appear to be specialized to use pyruvate.

scholarly journals Increase of the activity state and loss of total activity of the branched-chain 2-oxo acid dehydrogenase in rat diaphragm during incubation

1984 ◽  
Vol 224 (2) ◽  
pp. 491-496 ◽  
Author(s):  
A J M Wagenmakers ◽  
J T Schepens ◽  
J H Veerkamp
Keyword(s):  
Amino Acids ◽  
Citrate Synthase ◽  
Ketone Bodies ◽  
Total Activity ◽  
Acid Oxidation ◽  
Oxidation Rates ◽  
Acid Dehydrogenase ◽  
Activity State ◽  
Branched Chain

Actual and total branched-chain 2-oxo acid dehydrogenase activities were determined in homogenates of incubated diaphragms from fed and starved rats. Incubation in Krebs-Ringer buffer increased the activity state, but caused considerable loss of total activity. Palmitate oxidation rates and citrate synthase activities did not significantly change on incubation. Starved muscles showed a higher extent of activation after 15 min of incubation (not after 30 and 60 min) and a smaller loss of total activity. Experiments with the transaminase inhibitor amino-oxyacetate confirm that the contribution of endogenous amino acids to the oxidation precursor pool is also smaller in diaphragms from starved rats on incubation in vitro. These phenomena together cause the higher 14CO2 production from 14C-labelled branched-chain amino acids and 2-oxo acids in muscles from starved than from fed rats. High concentrations of branched-chain 2-oxo acids, and the presence of 2-chloro-4-methyl-pentanoate, octanoate or ketone bodies, increase the extent of activation of the dehydrogenase complex; glucose and pyruvate had no effect. The observed changes of the activity state by these metabolites are discussed in relation to their interaction with branched-chain 2-oxo acid oxidation in incubated hemidiaphragms.

scholarly journals Mitochondrial physiology and responses to elevated hydrogen sulphide in two isogenic lineages of an amphibious mangrove fish

2021 ◽  
Vol 224 (8) ◽  
Author(s):  
Keri E. Martin ◽  
Suzanne Currie ◽  
Nicolas Pichaud
Keyword(s):  
Hydrogen Sulphide ◽  
Citrate Synthase ◽  
Anaerobic Capacity ◽  
Terrestrial Environment ◽  
Lactate Dehydrogenase Activity ◽  
Oxidation Rates ◽  
Mitochondrial Functions ◽  
Wide Range ◽  
Mitochondrial Oxidation ◽  
Mangrove Rivulus

ABSTRACT Hydrogen sulphide (H2S) is toxic and can act as a selective pressure on aquatic organisms, facilitating a wide range of adaptations for life in sulphidic environments. Mangrove rivulus (Kryptolebias marmoratus) inhabit mangrove swamps and have developed high tolerance to environmental H2S. They are hermaphroditic and can self-fertilize, producing distinct isogenic lineages with different sensitivity to H2S. Here, we tested the hypothesis that observed differences in responses to H2S are the result of differences in mitochondrial functions. For this purpose, we performed two experimental series, testing (1) the overall mitochondrial oxidizing capacities and (2) the kinetics of apparent H2S mitochondrial oxidation and inhibition in two distinct lineages of mangrove rivulus, originally collected from Belize and Honduras. We used permeabilized livers from both lineages, measured mitochondrial oxidation, and monitored changes during gradual increases of sulphide. Ultimately, we determined that each lineage has a distinct strategy for coping with elevated H2S, indicating divergences in mitochondrial function and metabolism. The Honduras lineage has higher anaerobic capacity substantiated by higher lactate dehydrogenase activity and higher apparent H2S oxidation rates, likely enabling them to tolerate H2S by escaping aquatic H2S in a terrestrial environment. However, Belize fish have increased cytochrome c oxidase and citrate synthase activities as well as increased succinate contribution to mitochondrial respiration, allowing them to tolerate higher levels of aquatic H2S without inhibition of mitochondrial oxygen consumption. Our study reveals distinct physiological strategies in genetic lineages of a single species, indicating possible genetic and/or functional adaptations to sulphidic environments at the mitochondrial level.

scholarly journals Substrate selectivities differ for hepatic mitochondrial and peroxisomal β-oxidation in an Antarctic fish, Notothenia gibberifrons

1993 ◽  
Vol 289 (2) ◽  
pp. 427-433 ◽  
Author(s):  
E L Crockett ◽  
B D Sidell
Keyword(s):  
Antarctic Fish ◽  
Fatty Acyl ◽  
Beta Oxidation ◽  
Oxidation Rates ◽  
Substrate Preferences ◽  
Antarctic Marine ◽  
Marked Preference ◽  
Aerobic Energy Metabolism ◽  
High Concentrations ◽  
Rate Limiting

Hepatic mitochondrial and peroxisomal beta-oxidation were examined in an Antarctic marine teleost, Notothenia gibberifrons. Enzymic profiles and rates of beta-oxidation by intact organelles were determined by using a range of fatty acyl-CoA substrates to evaluate substrate preferences. Partitioning of beta-oxidation between organelles was estimated. Substrate selectivities are broader for peroxisomal beta-oxidation than for mitochondrial beta-oxidation. Mitochondria show marked preference for the oxidation of a monounsaturated substrate, palmitoleoyl-CoA (C16:1), and two polyunsaturates, eicosapentaenoyl-CoA (C20:5) and docosahexaenoyl-CoA (C22:6). Carnitine palmitoyltransferase activities with palmitoleoyl-CoA (C16:1) are 2.4-fold higher than activities with palmitoyl-CoA (C16:0). Most polyunsaturated acyl-CoA esters measured appear to inhibit by over 40% the oxidation of palmitoyl-CoA by peroxisomes. Our findings suggest that the polyunsaturates, eicosapentaenoic acid (C20:5) and docosahexaenoic acid (C22:6), found in high concentrations in Antarctic fishes [Lund and Sidell (1992) Mar. Biol. 112, 377-382], are utilized as fuels to support aerobic energy metabolism. Metabolic capacities of rate-limiting enzymes and beta-oxidation rates by intact organelles indicate that up to 30% of hepatic beta-oxidation in N. gibberifrons can be initiated by the peroxisomal pathway.

Maximal enzyme activities of energy production pathways in the heart, hepatopancreas, and white muscle of the giant scallop (Placopecten magellanicus) and lobster (Homarus americanus)

1992 ◽  
Vol 70 (4) ◽  
pp. 720-724 ◽  
Author(s):  
John M. Stewart ◽  
Molly E. Brass ◽  
Robert C. Carlin ◽  
Heather Black
Keyword(s):  
Cytochrome C ◽  
Cytochrome C Oxidase ◽  
White Muscle ◽  
Citrate Synthase ◽  
Ketone Bodies ◽  
Homarus Americanus ◽  
Carnitine Palmitoyltransferase ◽  
Placopecten Magellanicus ◽  
Flexor Muscle ◽  
Low Levels

The maximal activities of enzymes in energy pathways were measured in the ventricle, hepatopancreas, and white muscle of lobster (Homarus americanus; abdominal flexor) and giant scallop (Placopecten magellanicus; phasic adductor). Both animals show an energy metabolism based upon the utilization of carbohydrate. Carnitine palmitoyltransferase activity was not detected, and this was interpreted as an incapacity for mitochondrial β-oxidation of fatty acids; the absence of 3-hydroxybutyrate dehydrogenase and D-3-hydroxybutyrate indicated that ketone bodies were not a significant energy source. The levels of hexokinase, phosphofructokinase I, citrate synthase, and cytochrome c oxidase in the myocardia of both animals suggest a dependence on the aerobic processing of both blood-borne and glycogen-derived glucose. The significance of the enzyme activity data in the hepatopancreas of both animals was not immediately apparent. The abdominal flexor muscle of the lobster and the phasic adductor of the scallop showed enzyme profiles that suggest a reliance on glycolysis to fuel rapid bursts of activity. In the lobster flexor the presence of hexokinase and phosphofructokinase I along with low levels of citrate synthase and cytochrome c oxidase indicated that this tissue can utilize blood-borne and glycogenic glucose anaerobically. The absence of hexokinase, the low levels of citrate synthase and cytochrome c oxidase, and the presence of phosphofructokinase I in the scallop adductor suggested a reliance upon glycogen-fueled glycolysis to power burst activity. 3-Hydroxyacyl-CoA dehydrogenase was found in all tissues except the lobster flexor, which was curious in light of the undetectable activity of carnitine palmitoyltransferase.

Are there distinct subcellular populations of mitochondria in rainbow trout red muscle?

1998 ◽  
Vol 201 (16) ◽  
pp. 2455-2460 ◽  
Author(s):  
BJ Battersby ◽  
CD Moyes
Keyword(s):  
Rainbow Trout ◽  
Striated Muscle ◽  
Citrate Synthase ◽  
Mitochondrial Protein ◽  
Fatty Acyl ◽  
Striated Muscles ◽  
Oxidation Rates ◽  
Red Muscle ◽  
Two Populations

Ultrastructural analysis typically shows vertebrate striated muscles to possess mitochondria residing primarily in two locations. One population is interlaced throughout the myofibrils and another occurs directly beneath the cell membrane. The two populations of mitochondria can be separated and studied in vitro. Subsarcolemmal mitochondria (SSmt) are released by mechanical shearing of the tissue, whereas protease treatment is required to release the intermyofibrillar population (IMFmt). These methods were applied to rainbow trout (Oncorhynchus mykiss) red muscle to investigate the possible existence of distinct populations in this tissue. The two populations were very similar in mitochondrial DNA content (mtDNA mg-1 mitochondrial protein) and enzymatically (activities of carnitine palmitoyl transferase, &bgr ;-hydroxyacyl CoA dehydrogenase, complex I, citrate synthase, cytochrome c oxidase expressed per milligram of mitochondrial protein). Respiration rates were the same for pyruvate and succinate, but IMFmt oxidized palmitoyl carnitine 26 % faster than SSmt (P<0.05). Apart from these minor differences in fatty acyl carnitine oxidation rates, no differences in biochemical or genetic properties were detected between populations. The lack of distinct subcellular populations in fish, in contrast to the situation in mammalian striated muscle, probably relates to the high mitochondrial volume density in fish red muscle.

The Influence of Ultra-Low Concentrations of Potassium Anphen on the Bioenergetic Characteristics of Mitochondria

2020 ◽  
Vol 16 (4) ◽  
pp. 537-542
Author(s):  
Zhigacheva Irina ◽  
Volodkin Aleksandr ◽  
Rasulov Maksud
Keyword(s):  
Functional State ◽  
Membrane Lipids ◽  
Biological Effects ◽  
Dose Dependence ◽  
Stress Factors ◽  
Mitochondrial Membranes ◽  
Oxidation Rates ◽  
Pea Seedlings ◽  
Low Concentrations ◽  
Wide Range

Background: One of the main sources of ROS in stress conditions is the mitochondria. Excessive generation of ROS leads to oxidation of thiol groups of proteins, peroxidation of membrane lipids and swelling of the mitochondria. In this regard, there is a need to search for preparationsadaptogens that increase the body's resistance to stress factors. Perhaps, antioxidants can serve as such adaptogens. This work aims at studying the effect of antioxidant; the potassium anphen in a wide range of concentrations on the functional state of 6 day etiolated pea seedlings mitochondria (Pisum sativum L). Methods: The functional state of mitochondria was studied per rates of mitochondria respiration, by the level of lipid peroxidation and study of fatty acid composition of mitochondrial membranes by chromatography technique. Results: Potassium anphen in concentrations of 10-5 - 10-8 M and 10-13-10-16 prevented the activation of LPO in the mitochondrial membranes of pea seedlings, increased the oxidation rates of NAD-dependent substrates and succinate in the respiratory chain of mitochondria that probably pointed to the anti-stress properties of the drug. Indeed, the treatment of pea seeds with the preparation in concentrations of 10-13 M prevented the inhibition of growth of seedlings in conditions of water deficiency. Conclusion: It is assumed that the dose dependence of the biological effects of potassium anphen and the manifestation of these effects in ultra-low concentrations are due to its ability in water solutions to form a hydrate containing molecular ensembles (structures).

scholarly journals Autophagy Deficiency by Atg4B Loss Leads to Metabolomic Alterations in Mice

Metabolites ◽  
2021 ◽  
Vol 11 (8) ◽  
pp. 481
Author(s):  
Gemma G. Martínez-García ◽  
Raúl F. Pérez ◽  
Álvaro F. Fernández ◽  
Sylvere Durand ◽  
Guido Kroemer ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Mammalian Cells ◽  
Tissue Homeostasis ◽  
In Vivo Studies ◽  
Protective Mechanism ◽  
Cardiac Damage ◽  
Wide Range ◽  
First Time

Autophagy is an essential protective mechanism that allows mammalian cells to cope with a variety of stressors and contributes to maintaining cellular and tissue homeostasis. Due to these crucial roles and also to the fact that autophagy malfunction has been described in a wide range of pathologies, an increasing number of in vivo studies involving animal models targeting autophagy genes have been developed. In mammals, total autophagy inactivation is lethal, and constitutive knockout models lacking effectors of this route are not viable, which has hindered so far the analysis of the consequences of a systemic autophagy decline. Here, we take advantage of atg4b−/− mice, an autophagy-deficient model with only partial disruption of the process, to assess the effects of systemic reduction of autophagy on the metabolome. We describe for the first time the metabolic footprint of systemic autophagy decline, showing that impaired autophagy results in highly tissue-dependent alterations that are more accentuated in the skeletal muscle and plasma. These changes, which include changes in the levels of amino-acids, lipids, or nucleosides, sometimes resemble those that are frequently described in conditions like aging, obesity, or cardiac damage. We also discuss different hypotheses on how impaired autophagy may affect the metabolism of several tissues in mammals.

scholarly journals Destruxin A Interacts with Aminoacyl tRNA Synthases in Bombyx mori

2021 ◽  
Vol 7 (8) ◽  
pp. 593
Author(s):  
Jingjing Wang ◽  
Alexander Berestetskiy ◽  
Qiongbo Hu
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Bombyx Mori ◽  
Metarhizium Anisopliae ◽  
Free Amino ◽  
Molecular Target ◽  
Trna Synthetases ◽  
Interaction Mode ◽  
Aminoacyl Trna Synthetases ◽  
Wide Range

Destruxin A (DA), a hexa-cyclodepsipeptidic mycotoxin produced by the entomopathogenic fungus Metarhizium anisopliae, exhibits insecticidal activities in a wide range of pests and is known as an innate immunity inhibitor. However, its mechanism of action requires further investigation. In this research, the interactions of DA with the six aminoacyl tRNA synthetases (ARSs) of Bombyx mori, BmAlaRS, BmCysRS, BmMetRS, BmValRS, BmIleRS, and BmGluProRS, were analyzed. The six ARSs were expressed and purified. The BLI (biolayer interferometry) results indicated that DA binds these ARSs with the affinity indices (KD) of 10−4 to 10−5 M. The molecular docking suggested a similar interaction mode of DA with ARSs, whereby DA settled into a pocket through hydrogen bonds with Asn, Arg, His, Lys, and Tyr of ARSs. Furthermore, DA treatments decreased the contents of soluble protein and free amino acids in Bm12 cells, which suggested that DA impedes protein synthesis. Lastly, the ARSs in Bm12 cells were all downregulated by DA stress. This study sheds light on exploring and answering the molecular target of DA against target insects.

scholarly journals Combined Effect of Arginine, Valine, and Serine on Exercise-Induced Fatigue in Healthy Volunteers: A Randomized, Double-Blinded, Placebo-Controlled Crossover Study

Nutrients ◽  
2019 ◽  
Vol 11 (4) ◽  
pp. 862 ◽  
Author(s):  
Yuichi Tsuda ◽  
Makoto Yamaguchi ◽  
Teruyuki Noma ◽  
Eiji Okaya ◽  
Hiroyuki Itoh
Keyword(s):  
Amino Acids ◽  
Healthy Volunteers ◽  
Perceived Exertion ◽  
Ketone Bodies ◽  
Blood Analysis ◽  
Rating Of Perceived Exertion ◽  
Physical Parameters ◽  
Positive Effects ◽  
Exercise Induced ◽  
Double Blinded

Although several kinds of amino acids (AAs) are known to affect physiological actions during exercise, little is known about the combined effects of a mixture of several AAs on fatigue during exercise. The aim of the present study was to investigate the effect of an AA mixture supplement containing arginine, valine, and serine on exercise-induced fatigue in healthy volunteers. These AAs were selected because they were expected to reduce fatigue during exercise by acting the positive effects synergistically. A randomized, double-blinded, placebo-controlled crossover trial was conducted. Thirty-nine males ingested an AA mixture containing 3600 mg of arginine, 2200 mg of valine, and 200 mg of serine or a placebo each day for 14 days. On the 14th day, the participants completed an exercise trial on a cycle ergometer at 50% of VO2max for 120 min. After the two-week washout period, the participants repeated the same trial with the other test sample. The participant’s feeling of fatigue based on a visual analog scale (VAS) and a rating of perceived exertion (RPE), as well as blood and physical parameters were evaluated. The feeling of fatigue based on VAS and RPE were significantly improved in AA compared to those in placebo. In the blood analysis, the increase in serum total ketone bodies during exercise and plasma tryptophan/branched-chain amino acids were significantly lower in AA than those in placebo. The present study demonstrated that supplementation with an AA mixture containing arginine, valine, and serine reduced the feeling of fatigue during exercise. The AA mixture also changed several blood parameters, which may contribute to the anti-fatigue effect.

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