Tolerance of unacclimated and cold-acclimated rats to exercise in the cold: serum, red and white muscle enzymes, and histological changes

1970 ◽  
Vol 48 (10) ◽  
pp. 723-731 ◽  
Author(s):  
M. P. Dieter ◽  
P. D. Altland ◽  
B. Highman
Keyword(s):  
Enzyme Activity ◽  
White Muscle ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
Muscle Enzymes ◽  
Histological Changes ◽  
Glycerophosphate Dehydrogenase ◽  
Cold Room ◽  
Aerobic Function ◽  
Red Muscle

Unacclimated and cold-acclimated rats were exercised for 3 h, 5 h, or 9 h in a cold room maintained at 1.7 °C. The cold-acclimated rats tolerated these exercise periods, but two-thirds of the unacclimated rats died during 9 h exercise. In red and white muscle the intermediate exercise interval (5 h) induced significantly greater increases in the activities in muscle of creatinephosphokinase and glycolytic enzymes of unacclimated rats, while during 9 h exercise enzyme activity declined in muscles of unacclimated rats and increased in cold-acclimated ones. The rise in serum enzyme activity during exercise was consistently greater in unacclimated than in cold-acclimated rats. Apparently the reduction in exercise tolerance was associated with and may have been in part due to loss of enzyme content and activity in muscles. Collectively, these and other biochemical responses suggested that homeostatic mechanisms had been exhausted in the rats dually stressed by cold exposure and exercise. Except for the activities of aldolase and the ratio of lactic dehydrogenase to alpha-glycerophosphate dehydrogenase, those enzymes associated with "aerobic" function (transaminases) showed the predominant changes in red muscle, and those associated with "anaerobic" function (glycolytic enzymes) the predominant changes in white muscle. The greater responses of the glycolytic enzymes in a predominantly "aerobic" tissue suggest that the biochemical adaptability of red muscle is greater than that of white muscle.

Metabolic biochemistry of water- vs. air-breathing fishes: muscle enzymes and ultrastructure

1978 ◽  
Vol 56 (4) ◽  
pp. 736-750 ◽  
Author(s):  
P. W. Hochachka ◽  
M. Guppy ◽  
H. E. Guderley ◽  
K. B. Storey ◽  
W. C. Hulbert
Keyword(s):  
White Muscle ◽  
Large Diameter ◽  
Oxidative Capacity ◽  
The Body ◽  
Muscle Enzymes ◽  
Air Breathing ◽  
Red Muscle ◽  
Phosphofructokinase Activity ◽  
Metabolic Biochemistry ◽  
Myotomal Muscle

To delineate what modifications in muscle metabolic biochemistry correlate with transition to air breathing in fishes, the myotomal muscles of aruana, an obligate water breather, and Arapaima, a related obligate air breather, were compared using electron microscopy and enzyme methods. White muscle in both species maintained a rather similar ultrastructure, characterized by large-diameter fibers, very few mitochondria, and few capillaries. However, aruana white muscle displayed nearly fivefold higher levels of pyruvate kinase, threefold higher levels of muscle-type lactate dehydrogenase, and a fourfold higher ratio of fructose diphosphatase –phosphofructokinase activity; at the same time, enzymes in aerobic metabolism occurred at about one-half the levels in Arapaima. Red muscle was never found in the myotomal mass of aruana, but in Arapaima, red muscle was present and seemed fueled by glycogen, lipid droplets never being observed. From these and other data, it was concluded that in myotomal muscle two processes correlate with the transition to air breathing in Amazon osteoglossids: firstly, an emphasis in oxidative metabolism, and secondly, a retention of red muscle. However, compared with more active water-breathing species, Arapaima sustains an overall dampening of enzyme activities in its myotomal muscle, which because of the large myotome mass explains why its overall metabolic rate is relatively low. By keeping the oxidative capacity of its myotomal muscle low, Arapaima automatically conserves O2 either for a longer time or for other more O2-requiring organs in the body, a perfectly understandable strategy for an air-breathing, diving fish, comparable with that observed in other diving vertebrates. A similar comparison was also made of two erythrinid fishes, one that skimmed the O2-rich surface layers of water and one that obtained three quarters of its O2 from water, one quarter from air. Ultrastructural and enzyme data led to the unexpected conclusion that the surface skimmer sustained a higher oxidative capacity in its myotomal muscles than did the facultative air breather.

Regulation of glycolytic enzymes during anoxia in the turtle Pseudemys scripta

1989 ◽  
Vol 257 (2) ◽  
pp. R278-R283 ◽  
Author(s):  
S. P. Brooks ◽  
K. B. Storey
Keyword(s):  
Heart Muscle ◽  
Glycogen Phosphorylase ◽  
White Muscle ◽  
Fold Increase ◽  
Glycolytic Enzymes ◽  
Phosphorylase Activity ◽  
Enzyme Form ◽  
Red Muscle ◽  
Km Value ◽  
Glycogen Phosphorylase Activity

The glycolytic enzymes glycogen phosphorylase, phosphofructokinase (PFK), and pyruvate kinase (PK) were assessed in liver, heart, red muscle, and white muscle of aerobic and 5-h anoxic turtles (Pseudemys scripta) for changes in total activity and kinetic parameters. Anoxia induced statistically significant changes in these glycolytic enzymes in each of the four organs assayed. Compared with normoxic controls, anoxic liver showed a 3.3-fold increase in glycogen phosphorylase activity, a 1.5-fold increase in the PFK I50 value for citrate (concentration that inhibits initial activity by 50%), a 1.5-fold increase in the PFK Michaelis constant (Km) value for fructose 6-phosphate (P), and an increased maximal activity of PK. Anoxic heart muscle showed a 2.6-fold decrease in glycogen phosphorylase activity and, for PFK, a 1.7-fold decrease in the Km value for ATP and a twofold increase in the I50 value for citrate. In anoxic white muscle, PFK showed a fivefold lower Km value for fructose-6-P and a threefold lower activator concentration producing half-maximal activation (A50) for potassium phosphate than the aerobic enzyme form. Changes in anoxic white muscle PK included a twofold increase in the Km value for ADP and a 1.7-fold decrease in the I50 value for alanine. In red muscle, anoxia affected only the Km value for ATP, which was 50% higher than the value for the aerobic enzyme form. Fructose 2,6-diphosphate (P2) levels also decreased in heart muscle and increased in red and white muscle during anoxia.(ABSTRACT TRUNCATED AT 250 WORDS)

CARBOHYDRATE METABOLISM IN THE TWO-SPOTTED SPIDER MITE, TETRANYCHUS TELARIUS L.: II. EMBDEN–MEYERHOF PATHWAY

1963 ◽  
Vol 41 (7) ◽  
pp. 1595-1602 ◽  
Author(s):  
K. N. Mehrotra
Keyword(s):  
Carbohydrate Metabolism ◽  
Spider Mite ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
Glycolytic Pathway ◽  
Glycerophosphate Dehydrogenase ◽  
End Products ◽  
Two Spotted Spider Mite

Evidence demonstrating the occurrence of some of the glycolytic enzymes in the two-spotted spider mite, Tetranychus telarius L., has been obtained. The glycolytic pathway in mites appears to be similar to the Embden–Meyerhof type described for other organisms.The enzymes shown to be present in the mite are: phosphohexoisomerase, phosphofructokinase, aldolase, α-glycerophosphate dehydrogenase, and glyceraldehyde-3-phosphate dehydrogenase. The hexokinase and lactic dehydrogenase, if present, are in very low titre. The end products of glycolysis in the mites were shown to be α-glycerophosphate and pyruvate.

The potential for lactate utilization by red and white muscle of the eel Anguilla rostrata L.

1978 ◽  
Vol 56 (1) ◽  
pp. 128-135 ◽  
Author(s):  
W. C. Hulbert ◽  
T. W. Moon
Keyword(s):  
Lactate Dehydrogenase ◽  
White Muscle ◽  
Anguilla Rostrata ◽  
Lactate Oxidase ◽  
American Eel ◽  
Muscle Enzymes ◽  
Phosphoenol Pyruvate ◽  
Red Muscle ◽  
Lactate Utilization

The activities of lactate dehydrogenase (LDH) (L-lactate: NAD+ oxidoreductase, EC 1.1.1.27) can be divided into a lactate oxidase (lactate to pyruvate) and pyruvate reductase (pyruvate to lactate) component. These activities were examined in red and white muscle excised from the American eel Anguilla rostrata as an estimate of tissue lactate utilization, and compared with the kidney, gill, heart, and liver patterns. Phosphoenol pyruvate carboxykinase (PEP CK) activities in red and white muscle and liver were estimated as a marker for tissue gluconeogenic potential. Consistent with the possibility of lactate utilization for gluconeogenesis, both red muscle and liver possessed an active PEP CK and a bifunctional LDH, where oxidase activities were of the same magnitude as reductase activities. Kidney, which in mammals possesses gluconeogenic capabilities, together with heart and gill, also demonstrated LDH profiles consistent with the liver and red muscle enzymes. White muscle LDH was found to be essentially a pyruvate reductase and no PEP CK activity could be detected. These results suggest that eel red muscle has the potential to utilize lactate and has at least some of the enzymes required for gluconeogenesis. Therefore, the capacity of red muscle to perform a metabolic recycling function in addition to contraction cannot be excluded.

CARBOHYDRATE METABOLISM IN THE TWO-SPOTTED SPIDER MITE, TETRANYCHUS TELARIUS L.: II. EMBDEN–MEYERHOF PATHWAY

1963 ◽  
Vol 41 (1) ◽  
pp. 1595-1602
Author(s):  
K. N. Mehrotra
Keyword(s):  
Carbohydrate Metabolism ◽  
Spider Mite ◽  
Lactic Dehydrogenase ◽  
Glycolytic Enzymes ◽  
Glycolytic Pathway ◽  
Glycerophosphate Dehydrogenase ◽  
End Products ◽  
Two Spotted Spider Mite

Evidence demonstrating the occurrence of some of the glycolytic enzymes in the two-spotted spider mite, Tetranychus telarius L., has been obtained. The glycolytic pathway in mites appears to be similar to the Embden–Meyerhof type described for other organisms.The enzymes shown to be present in the mite are: phosphohexoisomerase, phosphofructokinase, aldolase, α-glycerophosphate dehydrogenase, and glyceraldehyde-3-phosphate dehydrogenase. The hexokinase and lactic dehydrogenase, if present, are in very low titre. The end products of glycolysis in the mites were shown to be α-glycerophosphate and pyruvate.

scholarly journals THE EFFECT OF THERMAL ACCLIMATION AND EXERCISE UPON THE BINDING OF GLYCOLYTIC ENZYMES IN MUSCLE OF THE GOLDFISH CARASSIUS AURATUS

1993 ◽  
Vol 175 (1) ◽  
pp. 195-209 ◽  
Author(s):  
M. Huber ◽  
H. Guderley
Keyword(s):  
Carassius Auratus ◽  
White Muscle ◽  
Specific Activity ◽  
Ph Dependence ◽  
Thermal Acclimation ◽  
Glycolytic Enzymes ◽  
Acclimation Temperature ◽  
Exhausting Exercise ◽  
Goldfish Carassius Auratus ◽  
Red Muscle

To examine whether the changes in metabolic organization induced by thermal acclimation modify glycolytic enzyme-binding, we acclimated goldfish, Carassius auratus, to 8 and 25 °C and measured the binding of phosphofructokinase (PFK), aldolase, pyruvate kinase and lactate dehydrogenase to subcellular particles in red and white muscle. When fish were sampled at rest at their acclimation temperature, only the percentage binding of PFK in red muscle was altered by thermal acclimation. By contrast, exhausting exercise at 15 sC led to markedly higher levels of binding of PFK in muscle of warm- than of cold-acclimated fish. This pattern was apparent in both red and white muscle. The specific activity of PFK in red muscle declined with exhausting exercise in warm- but not in cold-acclimated fish. In contrast, the units of PFK bound per gram of muscle did not differ in exhausted warm- and cold-acclimated fish. Cold- and warm-acclimated fish did not differ in their accumulation of lactate in white muscle at exhaustion. Furthermore, the PFK from white muscle of warm- and cold-acclimated fish did not differ in the pH dependence of binding to subcellular particles. These changes in the dynamics of PFK binding with temperature acclimation suggest that soluble PFK may be more susceptible to exercise-induced inhibition in warm- than in cold-acclimated goldfish. While the percentage binding and the specific activity of the other glycolytic enzymes were little affected by exhausting exercise, the units of aldolase bound per gram of white muscle decreased with exercise in warm-acclimated fish.

Skeletal muscle enzymes and fiber composition in male and female track athletes

1976 ◽  
Vol 40 (2) ◽  
pp. 149-154 ◽  
Author(s):  
D. L. Costill ◽  
J. Daniels ◽  
W. Evans ◽  
W. Fink ◽  
G. Krahenbuhl ◽  
...  
Keyword(s):  
Enzyme Activities ◽  
Female Athletes ◽  
Lactic Dehydrogenase ◽  
Muscle Enzymes ◽  
Muscle Enzyme ◽  
Male Athletes ◽  
Fiber Composition ◽  
Glycerophosphate Dehydrogenase ◽  
Genetic Endowment ◽  
Track Athletes

Muscle samples were obtained from the gastrocnemius of 17 female and 23 male track athletes, 10 untrained women, and 11 untrained men. Portions of the specimen were analyzed for total phosphorylase, lactic dehydrogenase (LDH), and succinate dehydrogenase (SDH) activities. Sections of the muscle were stained for myosin adenosine triphosphatase, NADH2 tetrazolium reductase, and alpha-glycerophosphate dehydrogenase. Maximal oxygen uptake (VO2max) was measured on a treadmill for 23 of the volunteers (6 female athletes, 11 male athletes, 10 untrained women, and 6 untrained men). These measurements confirm earlier reports which suggest that the athlete's preference for strength, speed, and/or endurance events is in part a matter of genetic endowment. Aside from differences in fiber composition and enzymes among middle-distance runners, the only distinction between the sexes was the larger fiber areas of the male athletes. SDH activity was found to correlate 0.79 with VO2max, while muscle LDH appeared to be a function of muscle fiber composition. While sprint- and endurance-trained athletes are characterized by distinct fiber compositions and enzyme activities, participants in strength events (e.g., shot-put) have relatively low muscle enzyme activities and a variety of fiber compositions.

Isozymes of lactic dehydrogenase in skeletal muscle

1962 ◽  
Vol 202 (5) ◽  
pp. 827-829 ◽  
Author(s):  
M. C. Blanchaer ◽  
M. Van Wijhe
Keyword(s):  
Skeletal Muscle ◽  
Guinea Pig ◽  
Dehydrogenase Activity ◽  
White Muscle ◽  
Lactic Dehydrogenase ◽  
Human Muscle ◽  
Isozyme Pattern ◽  
Rabbit Muscle ◽  
Red Muscle ◽  
Dehydrogenase Isozyme

The lactic dehydrogenase (LD) isozyme patterns of red and white muscle of the guinea pig, rabbit, and mouse were examined by electrophoresis in barbiturate-buffered agar. Red muscle consistently yielded five bands of lactic dehydrogenase activity, but white muscle usually produced only two bands corresponding to isozymes IV and V. Traces of isozyme III were noted occasionally in the white muscle of the rabbit and mouse, but bands I and II were absent from the white muscle of all three species. Crystalline rabbit muscle lactic dehydrogenase produced an isozyme pattern resembling that of a mixture of red and white rabbit muscle. The lactic dehydrogenase isozyme pattern of human muscle reported by previous workers resembles that of a mixture of the red and white muscle patterns.

Myosin expression levels and enzyme activity in juvenile spotted wolffish (Anarhichas minor) muscle: a method for monitoring growth rates

2006 ◽  
Vol 63 (9) ◽  
pp. 1959-1967 ◽  
Author(s):  
Albert K Imsland ◽  
Nathalie R. Le François ◽  
Simon G Lamarre ◽  
Delphine Ditlecadet ◽  
Sindri Sigurðsson ◽  
...  
Keyword(s):  
Growth Rate ◽  
Enzyme Activity ◽  
Growth Rates ◽  
Positive Relationship ◽  
White Muscle ◽  
Glycolytic Enzymes ◽  
Growth Potential ◽  
Individual Growth ◽  
Expression Levels ◽  
Spotted Wolffish

The activity of glycolytic enzymes and the expression levels of myosin RNA was monitored in the white muscle of juvenile spotted wolffish (Anarhichas minor) reared under different temperature regimes. A group of individually tagged juvenile spotted wolffish was reared for 6 months at 4, 6, 8, and 12 °C. After the rearing trial, biopsy samples were taken from white muscle of each individual and the relationship between individual growth, enzyme activity, and myosin expression was investigated. A positive relationship between the activities of two glycolytic enzymes (pyruvate kinase and lactate dehydrogenase) and individual growth rate was observed. Using real-time polymerase chain reaction (PCR) and specially developed primers for myosin mRNA and 18S rRNA for spotted wolffish, we were able to detect differences in the relative myosin expression between experimental groups, and a positive relationship between myosin expression and specific growth rates was observed. These methods may be useful as an indicator of growth rate in wild fish and a fast and reliable indicator of growth potential under culture conditions. The method also has the potential to measure differences in white muscle synthesis in fish reared under variable environmental parameters and during different life history stages.

Electrical and Mechanical Properties of the Red and White Muscles in the Silver Carp

1972 ◽  
Vol 57 (2) ◽  
pp. 551-567
Author(s):  
T. YAMAMOTO
Keyword(s):  
Mechanical Properties ◽  
White Muscle ◽  
Silver Carp ◽  
Membrane Resistance ◽  
Resting Potential ◽  
Resting Membrane Potential ◽  
Mechanical Responses ◽  
Red Muscle ◽  
Red And White Muscles ◽  
Specific Membrane

1. Electrical and mechanical properties of the red muscle (M. levator pinnae pectoralis) and white muscle (M. levator pinnae lateralis abdominis) in the silver carp (Carassius auratus Linné) were investigated by using caffeine and thymol. 2. A complete tetanus could be produced in the red muscle. But in the white muscle no tetanus was produced and there was a gradual decrease in tension during continuous stimulation, even at a frequency of 1 c/s or less. 3. Caffeine (0.5-1 mM) and thymol (0.25-0.5 mM) potentiated the twitch tension in both muscles without an increase in the resting tension; they produced a contracture in both muscles when the concentration was increased further. 4. The falling phase of the active state of contraction was nearly the same in both muscles and was prolonged by caffeine (0.5 mmM) and by thymol (0.25 mM). 5. The resting membrane potential of the red muscle was scarcely affected by caffeine (0.5-5 mM), whereas in the white muscles a depolarization of 10 mV was observed with caffeine of more than 2 mM. The resting potential of both muscles was little changed by o.25 mm thymol. However, at a concentration of more than 0.5mM thymol depolarized the membrane in both muscles to the same extent. 6. In caffeine (2-3 mM) solution the mean specific membrane resistance was reduced from 8.8 kΩ cm2 to 6.0 kΩ cm2 in the red muscle, and from 5.0 kΩ cm2 to 2.7 kΩ cm2 in the white muscle. In thymol (0.5-1 mM) solution it was reduced from 11.2 kΩcm2 to 6.5 kΩ cm2 in the red muscle, and from 5.4kΩ cm2 to 3.1 kΩ) cm2 in the white muscle. The specific membrane capacitance, calculated from the time constant and the membrane resistance, remained more or less the same in both muscles after a treatment with these agents. 7. Electrical properties of the muscles and the effects of caffeine and thymol on mechanical responses suggest that there are no fundamental differences between red and white muscles except for the excitation-contraction coupling. A lack of summation of twitch, a successive decline of twitch, and inability to produce potassium contracture in the white muscle may be due to the fact that the Ca-releasing mechanism is easily inactivated by depolarization of the membrane.

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