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Effects of Temperature on Infected Cell O2 Concentration and Adenylate Levels in Attached Soybean Nodules.

To assess the role of O2 in the regulation of nodule metabolism following a decrease or an increase in temperature, the fractional oxygenation of leghemoglobin (FOL) was measured in soybean (Glycine max L. Merr.) nodules during rapid and gradual changes in temperature from 20[deg]C to either 15 or 25[deg]C. The affinity of leghemoglobin for O2 was also measured at each temperature and the values were used to calculate the infected cell O2 concentration (Oi). After nodules were transferred to 15[deg]C, FOL and Oi increased and adenylate energy charge (AEC = [ATP + 0.5ADP]/[ATP + ADP + AMP]) increased from 0.70 to 0.78. The temperature increase was associated with a decrease in FOL and Oi. We concluded that changes in nodule temperature alter the respiratory demand of the nodules for O2, resulting in a change in Oi and a shift in the balance between ATP consumption and ATP production within the nodule tissue.

Journal Article↗

The stoicheiometry of sodium ion movement from frog muscle.

1. Further measurements of the consumption of high energy phosphate during the active extrusion of sodium ions from frog muscle were made in the presence of iodoacetate or dinitrofluorobenzene.2. In the presence of iodoacetate the consumption of ATP for phosphorylation of hexose is appreciable and so a deduction is made from the total ATP consumption during the ion movement.3. In the presence of dinitrofluorobenzene the deamination of adenosine monophosphate makes the changes in adenosine triphosphate and diphosphate unequal so that both substances have to be measured.4. The present results point to the active movement of between 2.5 and 3 sodium ions per high energy phosphate bond split.

Adenine Nucleotides↗

Chemo-mechanical energy transduction in relation to myosin isoform composition in skeletal muscle fibres of the rat.

1. ATP consumption and force development were determined in single skinned muscle fibres of the rat at 12 degrees C. Myofibrillar ATPase consumption was measured photometrically from NADH oxidation which was coupled to ATP hydrolysis. Myosin heavy chain (MHC) and light chain (MLC) isoforms were identified by gel electrophoresis. 2. Slow fibres (n = 14) containing MHCI and fast fibres (n = 18) containing MHCIIB were compared. Maximum shortening velocity was 1.02 +/- 0.63 and 3.05 +/- 0.23 lengths s-1, maximum power was 1.47 +/- 0.22 and 9.59 +/- 0.84 W l-1, and isometric ATPase activity was 0.034 +/- 0.003 and 0.25 +/- 0.01 mM s-1 in slow and in fast fibres, respectively. 3. In fast as well as in slow fibres ATP consumption during shortening increased above isometric ATP consumption. The increase was much greater in fast fibres than in slow fibres, but became similar when expressed relative to the isometric ATPase rate. 4. Efficiency was calculated from mechanical power and free energy change associated with ATP hydrolysis. Maximum efficiency was larger in slow than in fast fibres (0.38 +/- 0.04 versus 0.28 +/- 0.03) and was reached at a lower shortening velocity. 5. Within the group of fast fibres efficiency was lower in fibres which contained more MLC3f. We conclude that both MHC and essential MLC isoforms contribute to determine efficiency of chemo-mechanical transduction.

Adenosine Triphosphatases↗

Calcium pool size modulates the sensitivity of the ryanodine receptor channel and calcium-dependent ATPase of heavy sarcoplasmic reticulum to extravesicular free calcium concentration.

UNLABELLED: We have examined calcium cycling and associated ATP consumption by isolated heavy sarcoplasmic reticulum (HSR) vesicles incubated in conditions believed to exist in resting muscle. Our goals were to estimate the magnitude of calcium cycling under those conditions and identify the main mechanisms involved in its regulation. The integrity of the HSR vesicles was documented by the retention of [14C]-sucrose and electron microscopy. HSR actively exchanged Ca2+ with the medium through a partially open ryanodine-binding channel (RyR), as evidenced by the rapid attainment of a steady-state gradient between HSR and medium, which was promptly increased by the closure of the channel with ruthenium red (RR) or collapsed by its opening with caffeine. The ATP dependency was evidenced by the sustained ATP consumption after the steady state was attained and by the abrogation of the gradient following inhibition of the pump with thapsigargin (Tg) or the omission of ATP. When HSR vesicles were incubated in a comparatively large pool of calcium (approximately 1 micromol/mg HSR protein), ATP consumption was 1-1.5 micromol x [min x mg protein](-1) at 0.1 microM free Ca2+. Under such conditions, the main regulator of the sarcoplasmic Ca2+-dependent ATPase (SERCA) was extravesicular-free Ca2+ concentration, with a four- to fivefold increase between 0.1 and 2 microM Ca2+, whereas RyR channel activity and the replenishment of the HSR vesicles had only a modest effect on ATP consumption. When calcium pool size was reduced to 0.1 micromol/mg HSR protein, a steady state was established at a lower level of HSR calcium. In spite of a slightly lower free extravesicular Ca2+ at equilibrium (approximately 0.07 microM following an initial concentration of 0.1 microM), both ATP consumption and the open probability of the RyR channel were increased by a factor of three to five. Compared to the large calcium pool, the sensitivity of both RyR channel and SERCA to extravesicular free Ca2+ concentration as well as to caffeine and RR was markedly enhanced. CONCLUSIONS: 1) In conditions present in resting muscle, HSR calcium is in dynamic equilibrium with the medium through a partially open RyR channel, which requires continuous ATP hydrolysis. 2) The availability of calcium is a major determinant of the sensitivity of both RyR channel and SERCA to free extravesicular Ca2+ and possibly other stimuli. 3) These observations are consistent with the concept that calcium cycling in resting muscle may account for a significant fraction of muscle energy demands and further suggest that restricting calcium availability may enhance the energetic demands of this process.

Adenosine Triphosphate↗

High K+,Na+-deficient solution inhibits tension, O2 consumption, and ATP synthesis in smooth muscle.

In guinea pig taenia coli, added 45.4 mM K+ induced a sustained contraction, increased the rate of oxygen consumption, and slightly decreased the ATP content. In substituted 154.2 mM K+, Na+-deficient solution, only a transient contraction was induced. Oxygen consumption also showed only a transient increase and ATP content of the muscle rapidly decreased. Such an inhibition of sustained contraction and the decrease in both oxygen consumption and ATP content were recovered when 5.5 mM pyruvate or 50 mM NaCl was added during the 154.2 mM K+-induced contraction. In rabbit aorta, substituted 80 mM K+, 74.2 mM Na+ solution induced a sustained contraction, increase in oxygen consumption, and no change in ATP content. The 80 mM K+ solution without added glucose also induced a sustained contraction followed by a slight increase in oxygen consumption and a slight decrease in ATP content. The 154.2 mM K+, Na+-deficient solution produced similar changes in both oxygen consumption and ATP content as the 80 mM K+, glucose depleted solution. However, the 154.2 mM K+ solution induced only a transient contraction in the vascular smooth muscle. When 100 mM sucrose was hyperosmotically added to the 154.2 mM K+ solution, the suppressed muscle tension increased again, although the ATP content did not increase. From these and the previous results, it is concluded that glucose utilization by the taenia coli is inhibited in the 154.2 mM K+, Na+-deficient solution, and the decreased energy production of the muscle cell does not compensate the increased energy consumption induced by the high concentration of K+. In the aorta, although the Na+-deficient solution also decreases ATP production, it is the cell swelling induced by a high KCI concentration in the medium, not the decrease in energy metabolism, that has a direct inhibitory effect on muscle tension.

Adenosine Triphosphate↗

The importance of ATPase microenvironment in muscle fatigue: a hypothesis.

A broadly held opinion is that fatigue is not due to an insufficient supply of ATP to the energy consuming mechanisms because tissue [ATP] always remains at least one order of magnitude higher than Km for ATP of any ATPase. In general these findings also suggest that ATP consumption is well balanced with ATP regeneration even in the fatigued muscles. This balance is achieved by down-regulation of ATP consumption. Potentially this down-regulation could be accomplished by any product of the ATPase reaction and the role of Pi and H+ accumulation in this regulation has been discussed in the literature. The purpose of this paper is to describe known compartmentalization of ATP regeneration systems in muscle cell, their importance in the regulation of [adenine nucleotide] in the vicinity of ATPases and how such local ATP regeneration maybe important in the etiology of muscle fatigue. Available experimental evidence suggests that the binding of creatine kinase and glycolytic enzymes in the vicinity of sites where ATP is hydrolyzed and functional coupling between these ATP regenerating mechanisms and ATPase can generate ATPase microenvironments that have an important role in the regulation of ATPase function. Main function of this ATP regeneration is to keep the local ADP/ATP ratios favorable for ATPase function, which seems to be especially important when ATPase turnover is high. Unfortunately, the maximum rate of local ATP regeneration relative to that of ATP hydrolysis in vivo is not known, mainly because in vitro determinations underestimate this value due to a decrease in the fractional of loosely abound enzyme to the preparation during isolation procedure.(ABSTRACT TRUNCATED AT 250 WORDS)

Adenine Nucleotides↗

Endogenous nitric oxide enhances coupling between O2 consumption and ATP synthesis in guinea pig hearts.

Endogenous nitric oxide (eNO) modulates tissue respiration. To test whether eNO modulates myocardial O2 consumption (MVO2), ATP synthesis, and metabolic efficiency, we used isolated isovolumic guinea pig hearts perfused at a constant flow. N(omega)-nitro-L-arginine (L-NNA; 5 x 10(-5) mol/l) was used to inhibit eNO production. MVO2 was measured at different levels of cardiac work, estimated as the rate-pressure product (RPP). ATP content and synthesis rate were determined using (31)P NMR and magnetization transfer during high cardiac work. L-NNA increased coronary vascular resistance (19 +/- 3%, P < 0.05) and MVO2 (12 +/- 3%, P < 0.05) without an increase in the RPP. In contrast, vehicle infusion resulted in insignificant changes in coronary vascular resistance (3 +/- 2%, P > 0.05) and MVO2 (-2 +/- 1%, P > 0.05). Compared with vehicle, L-NNA caused a higher MVO2 both during KCl arrest (L-NNA 5.6 +/- 0.5 vs. vehicle 3.0 +/- 0.4 micromol x min(-1) x mg x dry wt(-1), P < 0.05) and during increased cardiac work elicited by elevating perfusate Ca2+, indicating an upward shift in the relationship between contractile performance (measured as RPP) and MVO2. However, neither ATP contents nor ATP synthesis rates were different in the two groups during high cardiac work. Thus, because inhibition of eNO production by L-NNA increased MVO2 without a change in the ATP synthesis rate, these data suggest that eNO increases myocardial metabolic efficiency by reducing MVO2 in the heart.

Adenosine Triphosphate↗

Energy consumption by phospholipid metabolism in mammalian brain.

Until recently, brain phospholipid metabolism was thought to consume only 2% of the ATP consumed by the mammalian brain as a whole. In this paper, however, we calculate that 1.4% of total brain ATP consumption is consumed for the de novo synthesis of ether phospholipids and that another 5% is allocated to the phosphatidylinositide cycle. When added to previous estimates that fatty acid recycling within brain phospholipids and maintenance of membrane lipid asymmetries of acidic phospholipids consume, respectively, 5% and 8% of net brain ATP consumption, it appears that phospholipid metabolism can consume up to 20% of net brain ATP consumption. This new estimate is consistent with recent evidence that phospholipids actively participate in brain signaling and membrane remodeling, among other processes.

Adenosine Triphosphate↗

A possible role of the ATP-sensitive potassium ion channel in determining the duration of spike-bursts in mouse pancreatic beta-cells.

The pancreatic beta-cell displays an electrical activity consisting of spike bursts and silent phases at glucose concentrations of about 10 mM. The mechanism of initial depolarization induced by glucose is well defined. However, the mechanism inducing the silent phase has not been fully elucidated. In the present study, the possibility of involvement of ATP-sensitive K+ channels in repolarization was examined using the patch-clamp technique in the cell-attached recording configuration. Ouabain (0.1 mM), an inhibitor of Na+/K+-ATPase, caused a complete suppression of ATP-sensitive K+ channel activity followed by typical biphasic current deflections, which were due to action potentials. The channel activity was also inhibited by removal of K+ from a perifusion solution. Furthermore, the activity of ATP-sensitive K+ channels was markedly inhibited either by replacement of external NaCl with LiCl or by addition of amiloride (0.2 mM), a blocker of Na+/H+ antiport. Addition of L-type Ca2+ channel blockers such as Nifedipine for Mn2+ induced the complete suppression of K+ channel activity. These findings strongly suggest that a fall in ATP consumption results in sustained depolarization, and that the repolarizations interposed between spike-bursts under normal ionic conditions are due to the periodical fall of ATP concentration brought about by periodical acceleration of ATP consumption at Na+/K+-pumps. It is concluded that the elevation of intracellular Na+ concentration as a consequence of accelerated Na+/Ca2+-countertransport during the period of spike-burst enhances ATP consumption, leading to a fall in ATP concentration which is responsible for termination of spike-burst and initiation of repolarization.

Action Potentials↗

ATP-dependent aminophospholipid translocation in erythrocyte vesicles: stoichiometry of transport.

Vesicles released from human red blood cells by incubation with a suspension of sonicated dimyristoylphosphatidylcholine were purified by gel filtration. Purified vesicles and intact red cells had a very similar composition with respect to phospholipids and integral membrane proteins, but spectrin, the major component of the membrane skeleton, was not found in vesicles. Comparison of red cell and vesicle ATP levels (expressed as micromolar ATP per millimolar hemoglobin) showed a marked difference with a reduced content of only about 30% in vesicles, whatever the initial concentration in the erythrocytes. Spin-labeled aminophospholipids (phosphatidylserine and phosphatidylethanolamine) were translocated to the inner vesicle membrane layer at a comparable rate as in intact red cells provided that vesicles contained enough ATP. The maximum fraction of spin-labeled phospholipids translocated to the inner membrane layer was 84% for phosphatidylserine, 65% for phosphatidylethanolamine, 20-40% for phosphatidylcholine, and below 20% for sphingomyelin. The apparent Km of translocation, expressed as percent of total membrane phospholipid, was 0.14% for spin-labeled phosphatidylserine and 1.19% for spin-labeled phosphatidylethanolamine. This compares well to values established earlier for intact red blood cells. The fact that no ATP was synthesized in vesicles allowed determination of ATP consumption by aminophospholipid transport. The basic ATP hydrolysis rate was increased upon the addition of labeled aminophospholipids but not of labeled phosphatidylcholine or sphingomyelin. The stoichiometry between lipid translocation and ATP consumption, calculated from the respective initial velocities, was 1.13 +/- 0.2 for phosphatidylserine and 1.11 +/- 0.16 for phosphatidylethanolamine.

Adenosine Triphosphate↗

Adrenergic stimulation of sea bream (Sparus aurata) red blood cells in normoxia and anoxia: effects on metabolism and on the oxygen affinity of haemoglobin

The metabolic response of sea bream (Sparus aurata) red blood cells to adrenergic stimulation was determined in normoxia and anoxia. In the presence of oxygen, red blood cells swelled and then recovered their resting volume. Continuous monitoring of oxygen uptake displayed the kinetics of the increase in the oxygen affinity of haemoglobin. Cell volume recovery correlated with an activation of ATP consumption, and the energy equilibrium was restored by increasing the rates of respiration and glycolysis. When the respiratory chain was blocked, adrenergic stimulation increased the rates of ATP consumption and glycolysis of red blood cells. Moreover, adrenergic stimulation of deoxygenated erythrocytes also increased cell volume but did not enhance glycolysis or ATP consumption, and the cells remained swollen. Our results suggest that there is an oxygen-linked signal transducer that activates ATP-consuming processes, provided that the adrenergic stimulation occurs in the presence of oxygen.

Journal Article↗

The Frank-Starling mechanism is not mediated by changes in rate of cross-bridge detachment.

We tested the hypothesis that the Frank-Starling relationship is mediated by changes in the rate of cross-bridge detachment in cardiac muscle. We simultaneously measured isometric force development and the rate of ATP consumption at various levels of Ca2+ activation in skinned rat cardiac trabecular muscles at three sarcomere lengths (2.0, 2.1, and 2.2 microns). The maximum rate of ATP consumption was 1.5 nmol.s-1.microliter fiber vol-1, which represents an estimated adenosinetriphosphatase (ATPase) rate of approximately 10 s-1 per myosin head at 24 degrees C. The rate of ATP consumption was tightly and linearly coupled to the level of isometric force development, and changes in sarcomere length had no effect on the slope of the force-ATPase relationships. The average slope of the force-ATPase relationships was 15.5 pmol.mN-1.mm-1. These results suggest that the mechanisms that underlie the Frank-Starling relationship in cardiac muscle do not involve changes in the kinetics of the apparent detachment step in the cross-bridge cycle.

Adenosine Triphosphate↗

Interdependence of mitochondrial ATP production and extramitochondrial ATP utilization in intact spermatozoa.

The dependence of both respiration and total activity of ATP-consuming reactions on the cellular adenine nucleotide pattern was investigated in intact bovine spermatozoa. ATP consumption was manipulated by inhibition with vanadate and activation with caffeine, leading to a decrease or increase in the rate of respiration up to 70% or 20%, respectively. Oligomycin blocked the respiration to the same extent as did vanadate, suggesting that the total extramitochondrial ATP-consuming activity is vanadate-sensitive. The major part of ATP utilization must be linked to dynein ATPase, since inhibition of (Na+, K+) ATPase by ouabain showed only a small effect on respiration (-17%). Being a potent inhibitor of dynein ATPase, vanadate drastically reduced the amount of motile cells, whereas caffeine tended to increase the intensity of motion. The effects of vanadate or caffeine on respiration were paralleled by changes in cellular ATP, reflecting the response of mitochondrial respiration on the cellular ATP/ADP ratio. Respiration was found to depend on changes in the ATP/ADP ratio in the range from about 3 (+caffeine) to 9 (+vanadate). The range of response of ATP consumption to the ATP/ADP ratio was determined by varying the mitochondrial ATP production via the concentration of lactate which was used as substrate. The measured effects on both respiratory rate and ATP/ADP ratio suggested that ATP consumption was markedly dependent on ATP/ADP ratios below 5. It is concluded that lactate concentrations above 1 mM sufficiently supply bovine spermatozoa with substrate and the energy turnover is mainly limited by the activity of dynein ATPase rather than by the capacity of mitochondrial oxidative phosphorylation.

Adenosine Diphosphate↗

Factors limiting adenosine triphosphatase function during high intensity exercise. Thermodynamic and regulatory considerations.

It is widely accepted that a structural organisation favouring interaction between functionally-related enzymes is required for the economy and efficiency of metabolic reactions. Many functionally-related enzymes have been shown to be reversibly bound to cellular structures and to other enzymes at the sites where they are required. Resulting from this binding, close structural proximity and concentration of enzymes, a microenvironment is generated where the product of one enzyme is the substrate of the other. This reduces the diffusion distance for the substrate, saturates binding sites with maximal speed and, as a final outcome, increases the efficiency and economy of function behind these metabolic reactions. Available data indicate that the above-described association between adenosine triphosphatase (ATPase) and enzymes regenerating ATP has an important role in the regulation of ATPase function. A general consensus exists among published studies that the concentration of ATP ([ATP]) is not significantly decreased in fatigued muscle, even in those with severely diminished power output. However, in studies with isolated perfused hearts it has been possible to significantly reduce [ATP] in muscle cells without compromising mechanical activity. An explanation for this discrepancy is connected with local ATP regeneration in the vicinity of ATPase. Furthermore, when ATP regeneration is unable to balance ATP consumption a critical drop in the free energy of ATP hydrolysis is avoided by down-regulation of ATP consumption. The main function of local ATP regeneration is to maintain a low concentration of adenosine diphosphate ([ADP]), and the ADP/ATP ratio in the vicinity of the ATP-binding site of ATPase that is a prerequisite for high thermodynamic efficiency of ATP hydrolysis. Close proximity of creatine kinase and glycolytic enzymes to ATPase and high-affinity binding of substrates generate an ATPase microenvironment, where ADP and ATP are not in free equilibrium with those adenine nucleotides in the surrounding medium. In the physiological range of operation for important cellular ATPases (free energy change of 55 to 60 kJ/mol ATP) only a small fraction of energy, available in ATP, can be utilised, provided that no ATP regeneration takes place. However, ATP regeneration allows utilisation of most of the regenerating capacity, before ATP hydrolysis drops below the critical 55 kJ/mol. The importance of local ATP regeneration increases in parallel with an increase in the rate of ATPase turnover.(ABSTRACT TRUNCATED AT 400 WORDS)

Adenosine Triphosphatases↗

Balance of production and consumption of ATP in ammonium-starved Saccharomyces cerevisiae.

To establish a balance between the ATP produced in catabolism and the ATP consumed in net biosynthesis of cellular components the energy metabolism of Saccharomyces cerevisiae utilizing glucose in the absence of a nitrogen source (resting cells) was studied. The following results were obtained. (i) Cell number and biomass increased 2- and 2.5-fold, respectively, during the first 8 h of ammonium starvation. After this period, both values remained constant. (ii) The rate of sugar consumption and ATP production decreased with the duration of starvation to about 20% of the original in 24 h. (iii) About 60% of the sugar consumed was fermented to ethanol and about 10% assimilated as cellular material. Of the assimilated sugar, as much as 80% was accumulated as carbohydrate. (iv) Only 15% of the total ATP produced in catabolism seems to be consumed in net biosynthesis and maintenance of intracellular pH. The fate of the remaining 85% is unknown.

Adenosine Triphosphate↗

Myofibrillar ATPase activity in skinned human skeletal muscle fibres: fibre type and temperature dependence.

1. Myofibrillar ATP consumption and isometric tension (P0) were determined in chemically skinned skeletal muscle fibres from human rectus abdominis and vastus lateralis muscle. Fibres were classified in four groups (I, IIA, IIB, IIA/B or mixed) based on myosin heavy chain composition. 2. ATP consumption (+/- S.E.M.) at 20 degrees C varied from 0.41 +/- 0.06 mmol l-1 s-1 in type IIB fibres (n = 5) to 0.10 +/- 0.01 mmol l-1 s-1 in type I fibres (n = 13). 3. The ratio between ATPase activity and P0 (tension cost) differed significantly between fast type II and slow type I fibres. At 12 degrees C tension cost was lower than the values found previously in corresponding fibre types in the rat. 4. The relative increase in ATPase activity for a 10 degrees C temperature change (Q10), determined in the range from 12 to 30 degrees C, was temperature independent and amounted to 2.60 +/- 0.06. The increase in P0 with temperature was smaller and declined when the temperature increased. 5. From these measurements, estimates were obtained for the maximum rate of isometric ATP consumption and force development at muscle temperature in vivo (35 degrees C).

Adenosine Triphosphatases↗

Age-dependent changes in myosin composition correlate with enhanced economy of contraction in guinea-pig hearts.

1. The composition of myosin heavy chains (MHCs) was investigated in young (1- to 8-week-old) and mature (9- to 26-week-old) guinea-pigs using two monoclonal antibodies directed specifically against alpha-MHC and beta-MHC. In addition, maximum force and the rate of ATP consumption during isometric contraction were measured in chemically skinned trabeculae taken from the same hearts. 2. An age-dependent shift in the MHC composition was found. The alpha-MHC fraction decreased from 0.17 +/- 0.02 (mean +/- S.E.M.; n = 24) in young to 0.04 +/- 0.01 (n = 43) in mature hearts. This shift was correlated with a decrease in tension cost (i.e. ATP consumption per second per trabecula volume/force per cross-sectional area) from 4.1 +/- 0.2 mmol kN-1 m-1 s-1 (n = 23) in young to 2.5 +/- 0.1 mmol kN-1 m-1 s-1 (n = 57) in mature hearts. 3. From the results it follows that the slow beta-MHC isoform, which predominates in hearts of mature guinea-pigs, is about 5 times more economical than the fast alpha-MHC isoform. Calcium sensitivity of force and ATP consumption decreased with age, but stabilized within a few weeks after birth. The pronounced dependence of cardiac energetics on MHC composition should be taken into account in long-term studies of cardiac overload.

Adenosine Triphosphatases↗

Cardiac mechanoenergetics in silico.

The aim of this thesis is to investigate the link between biochemical intracellular processes and mechanical contraction of the cardiac muscle. First, the regulation of intracellular energy fluxes between mitochondria and myofibrils is studied. It is shown, that the experimentally observed metabolic stability of the cardiac muscle is reproducible by a simple feedback regulation mechanism, i.e., ATP consumption in myofibrils and ATP production in mitochondria are balanced by the changes of the high energy phosphate concentrations. Second, an important property of energy transformation from biochemical form to mechanical work in the cardiac muscle, the linear relationship between the oxygen consumption and the stress-strain area, is replicated by a cross-bridge model. Third, by using the developed cross-bridge model, the correlation between ejection fraction of the left ventricle and heterogeneity of sarcomere strain, developed stress and ATP consumption in the left ventricular wall is established. Fourth, an experimentally observed linear relationship between oxygen consumption and the pressure-volume area can be predicted theoretically from a linear relationship between the oxygen consumption and the stress-strain area. Summing up, it is shown how the macrovariables of a cardiac muscle are interwoven with intracellular physiological processes into a whole.

Actomyosin↗