scholarly journals Effects of calcium ions and adenosine diphosphate on the activities of NAD+-linked isocitrate dehydrogenase from the radular muscles of the whelk and flight muscles of insects

1976 ◽  
Vol 154 (3) ◽  
pp. 677-687 ◽  
Author(s):  
V A. Zammit ◽  
E A. Newsholme
Keyword(s):  
Enzyme Activity ◽  
Isocitrate Dehydrogenase ◽  
Flight Muscle ◽  
Schistocerca Gregaria ◽  
Insect Flight ◽  
Maximum Activity ◽  
Glycerol Phosphate ◽  
Energy Formation ◽  
Flight Muscles ◽  
Glycerol Phosphate Dehydrogenase

1. The activity of NAD+-linked isocitrate dehydrogenase from the radular muscle of the whelk is higher than those in many vertebrate muscles and only slightly lower than in the flight muscles of insects. The enzyme activity from the whelk (Buccinum undatum) is stable for several hours after homogenization of the radular muscle, whereas that from insect flight muscle is very unstable. Consequently, the enzyme from the whelk muscle is suitable for a systematic investigation of the effects of Ca2+ and ADP. 2. The sigmoid response of the enzyme activity to isocitrate concentration is markedly increased by raising the Ca2+ concentration from 0.001 to 10 muM, but it is decreased by ADP. The inhibitory effect of Ca2+ is most pronounced at pH7.1; it is not observed at pH 6.5. Similar effects are observed for the enzyme from the flight muscle of the locust (Schistocerca gregaria) and the water bug (Lethocerus cordofanus). The percentage activation by ADP of the enzyme from either the whelk or the insects is greater at 10 muM-Ca2+, and 50% of the maximum activation is obtained at 0.10 and 0.16 mM-ADP for the enzyme from whelk and locust respectively at this Ca2+ concentration. At 10 muM-Ca2+ in the absence of added ADP, the apparent Km for isocitrate is markedly higher than in other conditions. Ca2+ concentrations of 0.01, 0.1 and 0.2 muM cause 50% inhibition of maximum activity of the enzyme from the muscles of the whelk, locust and water bug respectively. 3. Recent work has indicated that mitochondria may play a complementary role to the sarcoplasmic reticulum in the control of the distribution of Ca2+ in muscle. The opposite effects of Ca2+ on the activities of isocitrate dehydrogenase and mitochondrial glycerol phosphate dehydrogenase from muscle tissue are consistent with the hypothesis that changes in the intracellular distribution of Ca2+ control the activities of these two enzymes in order to stimulate energy production for the contraction process in the muscle. Although both enzymes are mitochondrial, glycerol phosphate dehydrogenase resides on the outer surface of the inner membrane and responds to sarcoplasmic changes in Ca2+ concentration (i.e. an increase during contraction), whereas the isocitrate dehydrogenase resides in the matrix of the mitochondria and responds to intramitochondrial concentrations of Ca2+ (i.e. a decrease during contraction). It is suggested that changes in intramitochondrial Ca2+ concentrations are primarily responsible for regulation of the activity of NAD+-isocitrate dehydrogenase in order to control energy formation for the contractile process. However, when the muscle is at rest, changes in intramitochondrial concentrations of ADP may regulate energy formation for non-contractile processes.

scholarly journals Activities of citrate synthase and NAD+-linked and NADP+-linked isocitrate dehydrogenase in muscle from vertebrates and invertebrates

1976 ◽  
Vol 154 (3) ◽  
pp. 689-700 ◽  
Author(s):  
P R. Alp ◽  
E A. Newsholme ◽  
V A. Zammit
Keyword(s):  
Citric Acid ◽  
Isocitrate Dehydrogenase ◽  
Citric Acid Cycle ◽  
Citrate Synthase ◽  
Insect Flight ◽  
Mechanical Activity ◽  
Activity Data ◽  
Acid Cycle ◽  
Equilibrium Reaction ◽  
Flight Muscles

1. The activities of citrate synthase, NAD+-linked and NADP+-linked isocitrate dehydrogenase were measured in muscles from a large number of animals, in order to provide some indication of the importance of the citric acid cycle in these muscles. According to the differences in enzyme activities, the muscles can be divided into three classes. First, in a number of both vertebrate and invertebrate muscles, the activities of all three enzymes are very low. It is suggested that either the muscles use energy at a very low rate or they rely largely on anaerobic glycolysis for higher rates of energy formation. Second, most insect flight muscles contain high activities of citrate synthase and NAD+-linked isocitrate dehydrogenase, but the activities of the NADP+-linked enzyme are very low. The high activities indicate the dependence of insect flight on energy generated via the citric acid cycle. The flight muscles of the beetles investigated contain high activities of both isocitrate dehydrogenases. Third, other muscles of both vertebrates and invertebrates contain high activities of citrate synthase and NADP+-liniked isocitrate dehydrogenase. Many, if not all, of these muscles are capable of sustained periods of mechanical activity (e.g. heart muscle, pectoral muscles of some birds). Consequently, to support this activity fuel must be supplied continually to the muscle via the circulatory system which, in most animals, also transports oxygen so that energy can be generated by complete oxidation of the fuel. It is suggested that the low activities of NAD+-linked isocitrate dehydrogenase in these muscles may be involved in oxidation of isocitrate in the cycle when the muscles are at rest. 2. A comparison of the maximal activities of the enzymes with the maximal flux through the cycle suggests that, in insect flight muscle, NAD+-linked isocitrate dehydrogenase catalyses a non-equilibrium reaction and citrate synthease catalyses a near-equilibrium reaction. In other muscles, the enzyme-activity data suggest that both citrate synthase and the isocitrate dehydrogenase reactions are near-equilibrium.

scholarly journals The role of creatine kinase and arginine kinase in muscle

1978 ◽  
Vol 172 (3) ◽  
pp. 533-537 ◽  
Author(s):  
E A Newsholme ◽  
I Beis ◽  
A R Leech ◽  
V A Zammit
Keyword(s):  
Creatine Kinase ◽  
Maximum Rate ◽  
Skeletal Muscles ◽  
Flight Muscle ◽  
Insect Flight ◽  
Arginine Kinase ◽  
Maximum Activity ◽  
Insect Flight Muscle ◽  
Atp Turnover

Arginine and creatine kinase activities in different muscles are compared with calculated maximum rates of ATP turnover. The magnitude of the kinase activities decreases in the following order: anaerobic muscles and vertebrate skeletal muscles greater than heart muscle greater than insect flight muscle. The maximum activity of phosphagen kinases (i.e. creatine kinase and arginine kinase), in the direction of phosphagen formation, is lower than the calculated maximum rate of ATP turnover in insect flight muscle or rat heart.

scholarly journals THE FILAMENT LATTICE OF COCKROACH THORACIC MUSCLE

1968 ◽  
Vol 36 (3) ◽  
pp. 433-442 ◽  
Author(s):  
Martin Hagopian ◽  
David Spiro
Keyword(s):  
Fine Structure ◽  
Electron Microscope ◽  
Flight Muscle ◽  
Insect Flight ◽  
Thick Filament ◽  
Leucophaea Maderae ◽  
Thick Filaments ◽  
Femoral Muscle ◽  
Flight Muscles ◽  
Characteristic 3

The fine structure of the tergo-coxal muscle of the cockroach, Leucophaea maderae, has been studied with the electron microscope. This muscle differs from some other types of insect flight muscles inasmuch as the ratio of thin to thick filaments is 4 instead of the characteristic 3. The cockroach flight muscle also differs from the cockroach femoral muscle in thin to thick filament ratios and diameters and in lengths of thick filaments. A comparison of these latter three parameters in a number of vertebrate and invertebrate muscles suggests in general that the diameters and lengths of the thick filaments and thin to thick filament ratios are related.

The Role of Cyclic AMP in the Octopaminergic Modulation of Flight Muscle in the Locust

1991 ◽  
Vol 161 (1) ◽  
pp. 423-438
Author(s):  
MATTHEW D. WHIM ◽  
PETER D. EVANS
Keyword(s):  
Cyclic Amp ◽  
Flight Muscle ◽  
Schistocerca Gregaria ◽  
Phosphodiesterase Inhibitors ◽  
Motor Units ◽  
Blocking Agent ◽  
Receptor Activation ◽  
Octopamine Receptors ◽  
Flight Muscles

The role of cyclic AMP in the octopaminergic modulation of the dorsal longitudinal flight muscles of the locust Schistocerca gregaria has been investigated. Several techniques have been used to elevate cyclic AMP levels in this tissue by mechanisms that bypass the receptor activation stage. These include the use of phosphodiesterase inhibitors to block the metabolism of cyclic nucleotides, the use of forskolin, the diterpene activator of adenylate cyclase, and the direct application of permeable and phosphodiesterase-resistant analogues of cyclic AMP. All these approaches can be shown to mimic the modulatory effects of octopamine on the flight muscle. Surprisingly, the phosphodiesterase inhibitors used were not able to potentiate the actions of octopamine on this preparation. Octopamine increases cyclic AMP levels in a similar fashion in all five motor units of this muscle, an effect that is selectively blocked by phentolamine, an α-adrenergic blocking agent that blocks octopamine receptors in other preparations. In addition, stimulation of the dorsal unpaired median neurone to the dorsal longitudinal flight muscles (DUMDL) results in a frequency-dependent increase in cyclic AMP levels in the muscle that is also blocked by phentolamine. The data presented suggest that the octopamine-mediated modulation of neurally evoked tension in this muscle is brought about by a mechanism that involves an increase in cyclic AMP levels in the tissue.

scholarly journals The activities of phosphorylase, hexokinase, phosphofructokinase, lactate dehydrogenase and the glycerol 3-phosphate dehydrogenase in muscles from vertebrates and invertebrates

1972 ◽  
Vol 126 (1) ◽  
pp. 49-58 ◽  
Author(s):  
B. Crabtree ◽  
E. A. Newsholme
Keyword(s):  
White Muscle ◽  
Flight Muscle ◽  
Insect Flight ◽  
Maximum Activity ◽  
Glycolytic Flux ◽  
Insect Flight Muscle ◽  
Glycerophosphate Dehydrogenase ◽  
Vertebrate Muscle ◽  
Activity Measurements ◽  
Glycerol 3 Phosphate Dehydrogenase

1. The maximum activities of hexokinase, phosphorylase and phosphofructokinase have been measured in extracts from a variety of muscles and they have been used to estimate the maximum rates of operation of glycolysis in muscle. These estimated rates of glycolysis are compared with those calculated for the intact muscle from such information as oxygen uptake, glycogen degradation and lactate formation. Reasonable agreement between these determinations is observed, and this suggests that such enzyme activity measurements may provide a useful method for comparative investigations into quantitative aspects of maximum glycolytic flux in muscle. 2. The enzyme activities from insect flight muscle confirm and extend much of the earlier work and indicate the type of fuel that can support insect flight. The maximum activity of hexokinase in some insect flight muscles is about tenfold higher than that in vertebrate muscles. The activity of phosphorylase is greater, in general, in vertebrate muscle (particularly white muscle) than in insect flight muscle. This is probably related to the role of glycogen breakdown in vertebrate muscle (particularly white muscle) for the provision of ATP from anaerobic glycolysis and not from complete oxidation of the glucose residues. The activity of hexokinase was found to be higher in red than in white vertebrate muscle, thus confirming and extending earlier reports. 3. The maximum activity of the mitochondrial glycerophosphate dehydrogenase was always much lower than that of the cytoplasmic enzyme, indicating that the former enzyme is rate-limiting for the glycerol 3-phosphate cycle. From the maximum activity of the mitochondrial enzyme it can be calculated that the operation of this cycle would account for the reoxidation of all the glycolytically produced NADH in insect flight muscle but it could account for only a small amount in vertebrate muscle. Other mechanisms for this NADH reoxidation in vertebrate muscle are discussed briefly.

scholarly journals Time-dependence of the effect of X-irradiation on the formation of glycerol phosphate dehydrogenase and other dehydrogenases in the developing rat brain

1968 ◽  
Vol 107 (2) ◽  
pp. 259-264 ◽  
Author(s):  
J. De Vellis ◽  
O. A. Schjeide
Keyword(s):  
Isocitrate Dehydrogenase ◽  
Glycerol Phosphate ◽  
Age Dependent ◽  
X Irradiation ◽  
Enzyme Formation ◽  
Nad Oxidoreductase ◽  
Developing Rat ◽  
Dose Dependent ◽  
The Brain ◽  
Glycerol Phosphate Dehydrogenase

X-irradiation (100–1500 r) administered to the heads of rats 8–30 days of age inhibited the development of glycerol phosphate dehydrogenase (l-glycerol 3-phosphate–NAD oxidoreductase, EC 1.1.1.8) in the brain stem and cerebral hemispheres. At 40 days of age and older no effect was observed. This inhibition was a delayed phenomenon, dose-dependent and with no recovery. It is proposed that the inhibition of enzyme formation is related to radiation damage caused to DNA. Actinomycin D inhibited the development of glycerol phosphate dehydrogenase in a manner similar to ionizing radiation. Four other dehydrogenases also showed age-dependent radiosensitivities. ‘Malic enzyme’ (EC 1.1.1.40), lactate dehydrogenase (EC 1.1.1.27) and malate dehydrogenase (EC 1.1.1.37) ceased to be radiosensitive at about 8 days of age and isocitrate dehydrogenase (NADP) (EC 1.1.1.42) at 16 days. The correlation between developmental increase in enzyme activity and radiosensitivity held closely for glycerol phosphate dehydrogenase and isocitrate dehydrogenase and to a smaller extent for the others.

scholarly journals The activities of pyruvate carboxylase, phosphoenolpyruvate carboxylase and fructose diphosphatase in muscles from vertebrates and invertebrates

1972 ◽  
Vol 130 (2) ◽  
pp. 391-396 ◽  
Author(s):  
B. Crabtree ◽  
S. J. Higgins ◽  
E. A. Newsholme
Keyword(s):  
Phosphoenolpyruvate Carboxylase ◽  
Pyruvate Carboxylase ◽  
Flight Muscle ◽  
Insect Flight ◽  
Tricarboxylic Acid Cycle ◽  
Mitochondrial Fraction ◽  
Bumble Bee ◽  
Insect Flight Muscle ◽  
Carboxylase Activity ◽  
Flight Muscles

1. The activities of pyruvate carboxylase, phosphoenolpyruvate carboxylase and fructose diphosphatase in crude homogenates of vertebrate and invertebrate muscles are reported. 2. Pyruvate carboxylase activity was present in all insect flight muscles that were investigated: in homogenates of bumble-bee flight muscle the activity was inhibited by ADP and activated by acetyl-CoA, and it was distributed mainly in the mitochondrial fraction. This is the first demonstration of pyruvate carboxylase activity in muscle. However, the activity appears to be restricted to insect flight muscle, since it was not found in other invertebrate or vertebrate muscles. 3. Since the three enzymes were never found together in the same muscle, it is concluded that these enzymes cannot provide a pathway for the synthesis of glycogen from lactate or pyruvate in muscle. Other roles for these enzymes in muscle are suggested. In particular, pyruvate carboxylase may be present in insect flight muscle for the provision of oxaloacetate to support the large increase in activity of the tricarboxylic acid cycle which occurs when an insect takes flight.

scholarly journals Power and efficiency of insect flight muscle

1985 ◽  
Vol 115 (1) ◽  
pp. 293-304 ◽  
Author(s):  
C. P. Ellington
Keyword(s):  
Power Output ◽  
Flight Muscle ◽  
Insect Flight ◽  
Power Input ◽  
Mechanical Power ◽  
Insect Flight Muscle ◽  
Muscle Properties ◽  
System A ◽  
Mechanical Power Output ◽  
Flight Muscles

The efficiency and mechanical power output of insect flight muscle have been estimated from a study of hovering flight. The maximum power output, calculated from the muscle properties, is adequate for the aerodynamic power requirements. However, the power output is insufficient to oscillate the wing mass as well unless there is good elastic storage of the inertial energy, and this is consistent with reports of elastic components in the flight system. A comparison of the mechanical power output with the metabolic power input to the flight muscles suggests that the muscle efficiency is quite low: less than 10%.

The calcium sensitivity of ATP ase activity of myofibrils and actomyosins from insect flight and leg muscles

1968 ◽  
Vol 169 (1016) ◽  
pp. 229-240 ◽  
Keyword(s):  
Flight Muscle ◽  
Insect Flight ◽  
Locusta Migratoria ◽  
Calcium Sensitivity ◽  
Mechanical Activity ◽  
Rabbit Muscle ◽  
Leg Muscles ◽  
Structural Peculiarities ◽  
Flight Muscles ◽  
Leg Muscle

Myofibrils and actomyosin suspension were prepared from the fibrillar flight and non-fibrillar leg muscles of the water-bug, Lethocerus maximus , and their ATP ase activity measured in solutions of various ionic strength containing Mg ATP . Leg muscle showed a low ATP ase in the absence of Ca 2+ , and a large increase of ATPase over a narrow range of Ca 2+ concentration. Flight muscle had a greater ATPase in the absence of Ca 2+ but showed a much smaller increase over a wider range of Ca 2+ concentration. A similar difference between flight and leg muscle was found in the honey-bee, Apis mellifera , and the beetle, Oryctes rhinoceros , both of which have fibrillar flight muscles, but was not found in the locust, Locusta migratoria , which has non-fibrillar flight muscle. Tryptic digestion raised the ATP ase in the absence of Ca 2+ , and abolished the Ca 2+ -activation, in both flight and leg-muscle preparations from the water-bug; addition of ‘native tropomyosin5 prepared from rabbit muscle partially reversed the effect. These results are discussed in relation to the structural peculiarities and oscillatory mechanical activity of fibrillar flight muscle.

scholarly journals The activities of fructose diphosphatase in flight muscles from the bumble-bee and role of this enzyme in heat generation

1972 ◽  
Vol 128 (1) ◽  
pp. 89-97 ◽  
Author(s):  
E. A. Newsholme ◽  
B. Crabtree ◽  
S. J. Higgins ◽  
S. D. Thornton ◽  
Carole Start
Keyword(s):  
Flight Muscle ◽  
Maximum Activity ◽  
The Body ◽  
Bumble Bee ◽  
Rest Periods ◽  
Flight Muscles ◽  
Glucose 6 Phosphate Dehydrogenase ◽  
Hydrolysis Of ◽  
Low Activity

1. The maximum catalytic activities of fructose diphosphatase from flight muscles of bumble-bees (Bombus spp.) are at least 30-fold those reported for the enzyme from other tissues. The maximum activity of fructose diphosphatase in the flight muscle of any particular bee is similar to that of phosphofructokinase in the same muscle, and the activity of hexokinase is similar to or greater than the activity of phosphofructokinase. There is no detectable activity of glucose 6-phosphatase and only a very low activity of glucose 6-phosphate dehydrogenase in these muscles. The activities of both fructose diphosphatase and phosphofructokinase vary inversely with the body weight of the bee, whereas that of hexokinase is relatively constant. 2. There is no significant hydrolysis of fructose 1-phosphate, fructose 6-phosphate, glucose 1,6-diphosphate and glycerol 3-phosphate by extracts of bumble-bee flight muscle. 3. Fructose 1,6-diphosphatase from bumble-bee flight muscle and from other muscles is inhibited by Mn2+and univalent cations; the potency of inhibition by the latter varies in the order Li+>Na+>K+. However, the fructose diphosphatase from bumble-bee flight muscle is different from the enzyme from other tissues in that it is not inhibited by AMP. 4. The contents of ATP, hexose monophosphates, fructose diphosphate and triose phosphates in bumble-bee flight muscle showed no significant changes between rest and flight. 5. It is proposed that both fructose diphosphatase and phosphofructokinase are simultaneously active and catalyse a cycle between fructose 6-phosphate and fructose diphosphate in resting bumble-bee flight muscle. Such a cycle would produce continuous hydrolysis of ATP, with the release of energy as heat, which would help to maintain the thoracic temperature during rest periods at a level adequate for flight.

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