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.

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.

scholarly journals Neuromuscular control of anguilliform locomotion: patterns of red and white muscle activity during swimming in the american eel anguilla rostrata

1998 ◽  
Vol 201 (23) ◽  
pp. 3245-3256 ◽  
Author(s):  
G. B. Gillis
Keyword(s):  
Swimming Speed ◽  
Muscle Activity ◽  
White Muscle ◽  
Neuromuscular Control ◽  
Emg Activity ◽  
Anguilla Rostrata ◽  
Significant Shift ◽  
Muscle Strain ◽  
Body Form ◽  
Red Muscle

Two areas that have received substantial attention in investigations of muscle activity during fish swimming are (1) patterns of fiber type recruitment with swimming speed and (2) the timing of muscle activation in relation to muscle strain. Currently, very little is known about either of these areas in eels, which represent an extreme body form among fishes and utilize a mode of locomotion found at one end of the undulatory spectrum(anguilliform locomotion). To assess how this swimming mode and body form influence the neuromuscular control of swimming, I recorded electromyographic data from red and white muscle at four positions, 0.3L,0.45L, 0.6L and 0.75L, where L is body length, in eels (Anguilla rostrata)simultaneously video-taped (250 fields s-1) swimming at three speeds, 0.5,0.75 and 1.0 L s-1. As in other fish, exclusively red muscle is used at slow swimming speeds and white muscle is additionally recruited at higher swimming speeds. However, this study also revealed a novel posterior-to-anterior pattern of muscle recruitment with increasing swimming speed. At slow speeds, anteriorly located muscles are never active, muscle strain is negligible and forward thrust must be generated by posterior muscles. As speed increases, more anterior muscles are additionally recruited. Electromyogram (EMG) burst durations typically occupy between 0.2 and 0.3 undulatory cycles, irrespective of speed or position. EMG burst intensity increases significantly with swimming speed. The onset of EMG activity typically occurred near the end of muscle lengthening, whereas the offset of EMG activity occurred during shortening(typically before the muscle's return to resting length). There was a significant shift in red muscle onset times such that anterior muscles were typically active later in their strain cycle than posterior muscles. When red muscle activity patterns across various fish taxa are compared,differences in propulsive wavelength among species are related to differences in muscle activity, providing insight into the underlying neuromuscular bases of differences among undulatory swimming modes.

Lactate dehydrogenase isozymes from heart and white muscle of water-breathing and air-breathing fish from the Amazon

1978 ◽  
Vol 56 (4) ◽  
pp. 769-773 ◽  
Author(s):  
C. J. French ◽  
P. W. Hochachka
Keyword(s):  
Lactate Dehydrogenase ◽  
White Muscle ◽  
Substrate Inhibition ◽  
Dual Function ◽  
Kinetic Properties ◽  
General Phenomenon ◽  
Closely Related Species ◽  
Arapaima Gigas ◽  
Red Muscle ◽  
Sigmoidal Kinetics

Lactate dehydrogenase (LDH, EC 1.1.1.27) isozymes were studied from the white muscle and hearts of four species of Amazon fish, Osteoglossum bicirrhosum, an obligate water breather, and the closely related air breather, Arapaima gigas; Hoplias malabaricus, an obligate water breather, and Hoplerythrinus unitaeniatus, a facultative air breather. The LDH pattern was similar in closely related species but could not be correlated with changes in respiratory habits. All the isozymes from both heart and white muscle showed low substrate inhibition by pyruvate. The LDH from Osteoglossum skeletal white muscle showed sigmoidal kinetics with respect to pyruvate, rendered hyperbolic by the addition of 20 mM phosphocreatine. The kinetic properties appear to facilitate a dual function for white muscle in the absence of red muscle in the myotome. Phosphocreatine inhibition of LDH was observed in all the tissues studied and is suggested to be a more general phenomenon than has been previously supposed.

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.

Relating American Eel Anguilla rostrata abundance to environmental DNA concentration in the Bronx River

2021 ◽  
Author(s):  
Sam C. Chin ◽  
John Waldman ◽  
Mike Bednarski ◽  
Merry Camhi ◽  
Jake LaBelle ◽  
...  
Keyword(s):  
Environmental Dna ◽  
Anguilla Rostrata ◽  
American Eel ◽  
Dna Concentration ◽  
Bronx River

scholarly journals American eel,Anguilla rostrata, growth in fresh and salt water: implications for conservation and aquaculture

2009 ◽  
Vol 16 (4) ◽  
pp. 306-314 ◽  
Author(s):  
H. M. LAMSON ◽  
D. K. CAIRNS ◽  
J.-C. SHIAO ◽  
Y. IIZUKA ◽  
W.-N. TZENG
Keyword(s):  
Salt Water ◽  
Anguilla Rostrata ◽  
American Eel

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.

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)

Sign in / Sign up

Export Citation Format

Share Document