Activity and molecular changes in right and left ventricular myosins during right ventricular volume overload.
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Adenosine Triphosphatases↗
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Enzymatic activities, activation by actin, and synthesis of cardiac atrial myosin: distinctive enzymatic properties compared with cardiac ventricular myosin.
ATPase activity and synthesis of atrial and ventricular myosin were compared in the dog and rabbit heart. Atrial myosin showed enzymatic properties characterized by high Ca2+- and Mg2+-activated ATPase activities, low activation energy, lower rate of inactivation at alkaline pH, and no activation by N-ethylmalemide compared with the same properties in ventricular myosin. These findings suggest a difference in the myosin molecule at or near the active site involfing the SH-1 thiols. Also, actin activation of ATPase activities was studied to determine the physiological significance of this observation, since, in living muscle cell, MgATP is hydrolyzed by myosin under the activating effect of actin. Actin extracted from skeletal muscle was used in this experiment. Vmax for the actin-activated Mg2+-ATPase of atrial myosin was about twice that of ventricular myosin, whereas no significant difference was observed in the apparent dissociation constant for actin. This result suggests that the change in the enzymatic properties of myosin is reflected in the contractility of atrial and ventricular muscles. However, [3H]leucine incorporation into the myosin was approximately the same, suggesting that the difference in work load between atrium and ventricle is not associated with alteration of synthesis of cardiac myosin.
Actins↗
Cardiac atrial myosin adenosine triphosphatase of animals and humans: distinctive enzymatic properties compared with cardiac ventricular myosin.
Cardiac myosin obtained from atria had a higher Ca2+-activated ATPase activity than did cardiac myosin from ventricles in various species of animals and in humans. The increased specific activity of Ca2+-activated adenosine triphosphatase (ATPase) of atrial myosin appeared to correlate with the level of the activity of ventricular myosin ATPase in the animal, since the same order in ATPase activity, as observed in ventricular myosins from various animals, was noted in atrial myosins. The enzymatic properties of atrial myosin also were characterized by no activation by N-ethylmaleimide, low activating energy, and a lower rate of inactivation at alkaline pH compared with the same properties of ventricular myosin. These findings suggest a difference in the myosin molecule at or near the active site, involving some sulfhydryl groups, between the two types of cardiac myosin. The Mg2+-activated ATPase activity, both in the presence and absence of actin (which is thought to be closely related to the basic contraction mechanism), also was enhanced in atrial myosin. Thus, the ATPase activities of atrial and ventricular myosins were different with special reference to the reaction pathway involving calcium and magnesium ions and appear to account for the difference in the velocity of contraction between the atria and the ventricles.
Adenosine Triphosphatases↗
Atrial and ventricular myosins from human hearts. II. Isoenzyme distribution after myocardial infarction.
Human atrial and ventricular myosins were prepared from autopsy specimens from subjects with coronary heart disease. Cardiac myosin light chain isotypes were resolved using two-dimensional gel electrophoresis, whereas myosin isozymes were detected by pyrophosphate gel electrophoresis. Myocardial infarction and associated work overload cause a transition in the light chain complements of the myosins. Thus ventricular myosin light chains were found in pressure overloaded atria and atrial light chains have also been identified in the infarct ventricle of the human heart. Two molecular isoenzymes of the human atrial myosin, the relative proportions of which are changed after infarction, were separated under non-dissociating conditions by gel electrophoresis. A decrease in HA-3 and a corresponding increase in HA-1 were observed. Ventricular hypertrophy in patients with coronary insufficiency induces a second ventricle isomyosin, called HV-1, with the same electrophoretic mobility as HA-1. The relative part of this myosin type amounts to 20%. Comparative peptide mapping studies were carried out on myosin subfragment-1 preparations from normal and infarct ventricles. In the primary structures, the chymotrypsic digestions produced slight differences. These data demonstrate the heterogeneity of human atrial and ventricular myosins in patients with coronary heart disease.
Aged↗
Transient expression of a ventricular myosin heavy chain isoform in developing chicken intrafusal muscle fibers.
Sections of chicken tibialis anterior and extensor digitorium longus muscles were incubated with monoclonal antibodies against myosin heavy chains (MHC). Ventricular myosin was present in developing secondary intrafusal myotubes when they were first recognized at embryonic days (E) 13-14, and in developing extrafusal fibers prior to that date. The reaction in intrafusal fibers began to fade at E17, and in 2-week-old postnatal and older muscles the isoform was no longer recognized. Only those intrafusal fibers which also reacted with a monoclonal antibody against atrial and slow myosin contained ventricular MHC. Intrafusal myotubes which developed into fast fibers did not express the isoform. Hence, based on the presence or absence of ventricular MHC, two lineages of intrafusal fiber are evident early in development. Strong immunostaining for ventricular MHC was observed in primary extrafusal myotubes at E10, but the isoform was already downregulated at E14, when secondary intrafusal myotubes were still forming and expressed ventricular MHC. Only light to moderate and transient immunostaining was observed in coexisting secondary extrafusal myotubes, most of which developed into fast fibers. Thus at the time when nascent muscle spindles are first recognized, differences in MHC profiles already exist between prospective intrafusal and extrafusal fibers. If intrafusal fibers stem from a pool of primordial muscle cells, which is common to intrafusal and extrafusal myotubes, they diverged from it some time prior to E13.
Animals↗
Cross-hybridization of light chains of cardiac myosin isozymes: atrial and ventricular myosins.
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Adenosine Triphosphatases↗
Expression of ventricular myosin subunits in the atria of children with congenital heart malformations.
The presence of ventricular myosin light chains in the atria of children with congenital heart disease was demonstrated by two-dimensional polyacrylamide gel electrophoresis, peptide mapping, and Western blot analysis. Ventricular myosin light chains were present in 27% of biopsies from 91 children with different forms of congenital heart disease. Perimembranous ventricular septal defects and tetralogy of Fallot were associated with the presence of ventricular myosin light chains in 50% of patients. The presence of ventricular myosin light chains in these atria did not correlate with pressure or volume overload. Analysis of myosin heavy chain isotype in the same biopsies by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, peptide mapping, and Western blot analysis indicated that there was no detectable expression of ventricular myosin heavy chain (beta-subunit), suggesting that the genes for the myosin heavy chains and light chains are not expressed coordinately.
Blood Pressure↗
Levels of ventricular myosin fragments in human sera after myocardial infarction, determined with monoclonal antibodies to myosin heavy chains.
Serum levels of ventricular myosin heavy chains were quantitated in patients with acute myocardial infarction using a competitive radioimmunoassay involving monoclonal antibodies to the b-type myosin heavy chains of a human ventricle. Among the seven antibodies selected for their higher affinity for ventricular myosin heavy chains, only four antibodies detected significant and variable myosin amounts in the serum samples of nineteen patients with acute myocardial infarction; the same antibodies occasionally detected, if at all, low myosin amounts in the sera of patients with no clinical sign of myocardial infarction, and no myosin in the serum of the healthy control subjects. The peak levels of myosin release were observed 4.6 +/- 0.5 days (n = 13, P less than 0.01) after myocardial infarction and correlated rather well with the measured creatine kinase peak levels (the correlation coefficients were between 0.75 and 0.81, P less than 0.01, depending on the monoclonal antibody used for myosin determination). The time courses of myosin release varied according to the complexity of the heart attack observed. It was concluded that the titration of serum myosin was probably of little clinical value for therapeutic intervention during the acute phase of myocardial infarction; it could, however be an effective tool for retroactive detection of an infarct and for late estimation of infarct size.
Adult↗
A comparative study of atrial and ventricular myosin light subunits from different species.
Comparison of atrial and ventricular myosin light chains was performed using peptide mapping of electrophoretically purified proteins. In birds atrial and ventricular myosin light chain composition was identical. In mammals atrial and ventricular myosin light chains are different and species specific.
Animals↗
Comparative studies of atrial and ventricular myosin from normal, thyrotoxic, and thyroidectomized rabbits.
Changes in enzymatic and structural properties of ventricular myosin in thyrotoxic rabbit hearts have been investigated extensively. However, there is little information regarding the effect of thyroid hormone on the atrial myosin. In this study, we have compared enzymatic and structural changes of ventricular and atrial myosin from euthyroid, hypothyroid, and hyperthyroid rabbits. In euthyroid rabbits, Ca++- and actin-activated ATPase activities of atrial myosin were 2-fold greater than those of the ventricular myosin. The Ca++- and actin-activated ATPase activities of atrial myosin from hypothyroid and hyperthyroid rabbits were identical with the values for atrial myosin from euthyroid rabbits. The same ATPase activities of ventricular myosin decreased in hypothyroid hearts but increased in hyperthyroid rabbits. The K+ (EDTA)-ATPase activities of all myosins were the same, irrespective of the thyroid status of the animal. Pyrophosphate-polyacrylamide gel electrophoresis patterns showed two isoenzymes (designated as A1 and A3) of atrial myosin in euthyroid hearts. The same electrophoretic patterns also showed in atrial myosin from hypothyroid and hyperthyroid hearts. The ventricular myosin from euthyroid hearts also exhibited two isoenzymes (designated as V1 and V3) but each with slower electrophoretic mobilities than the corresponding atrial myosin. In hypothyroid hearts, only V3 isoenzyme was seen, whereas, in hyperthyroid hearts, only V1 isoenzyme was seen. These results suggest that thyroid hormone controls ventricular myosin ATPase activity by controlling synthesis of a specific ventricular isoenzyme, whereas thyroid hormone does not affect atrial myosin ATPase, possibly due to its inability to control atrial myosin synthesis.
Actins↗
Ventricular myosin heavy chain isoform expression is altered in vitro in low score normal chickens.
The low score normal (LSN) chicken exhibits a genetic muscle weakness and altered in vitro myogenesis compared to the normal White Leghorn chicken. The ventricular myosin heavy chain isoform has been reported to be the initial muscle-specific contractile protein expressed during myogenesis. The goals of this study were to determine whether altered myogenesis of the LSN satellite cells in culture was accompanied by delayed ventricular myosin heavy chain expression and to further characterize the altered myogenic events exhibited by the LSN chicken. Immunocytochemical and ELISA analyses were employed to document the temporal expression of the ventricular myosin heavy chain during LSN chicken myogenesis. Satellite cells derived from the LSN chicken pectoralis major exhibited lower (P </= 0.05) expression of ventricular myosin heavy chain during proliferation and differentiation in culture than did satellite cells derived from White Leghorn chickens. Low score normal cells failing to express the ventricular myosin heavy chain generally remained mononucleated and unfused, whereas cells that were multinucleated appeared to express ventricular myosin heavy chain regardless of the avian source. These results suggest that the altered myogenesis observed in LSN chickens is associated with delayed ventricular myosin heavy chain expression.
Animals↗
Reconstitution of ventricular myosin with atrial light chains 1 improves its functional properties.
Atrial light chain 1 (ALC-1) is expressed in embryonic and hypertrophied human ventricles but not in normal adult human ventricles. We investigated the effects of recombinant human atrial light chains (hALC-1) on the structure and enzymatic activity of synthetic filaments of ventricular myosin. The endogenous ventricular myosin light chain 1 (VLC-1) was partially replaced by recombinant hALC-1 yielding hALC-1 levels of 12%, 24% and 42%. This reconstitution of ventricular myosin with hALC-1 did not change the length of synthetic myosin filaments but led to more rounded myosin heads in comparison with those of control filaments. Actin-activated ATPase activity of myosin, a parameter of functional activity of molecular motor, amounted to 79.5 nmol P(i)/mg per min in control myosin filaments. Reconstitution with hALC-1 caused a profound increase of the actin-activated myosin ATPase activity in a dose dependent manner, for example, synthetic myosin filaments formed with 12%, 24% and 42% hALC-1 reconstituted myosin revealed the actin-activated ATPase activity increased by 18%, 26% and 36%, respectively, as compared to control. These results strongly suggest that in vivo expression of ALC-1 enhances ventricular myosin function, thereby contributing to cardiac compensation.
Electrophoresis, Polyacrylamide Gel↗
Ventricular myosin pattern of spontaneously hypertensive turkeys is unaffected by labetalol treatment.
In most animal species, left ventricular hypertrophy due to pressure overload is associated with an advantageous increase of the "slow" V3 isomyosin. In contrast, in spontaneously hypertensive turkeys, the development of left ventricular hypertrophy is associated with the synthesis of a "fast" V1-like isomyosin, with high incidence of cardiac failure. This could be related to the high catecholamine levels found in these animals. This is why we studied the ventricular myosin pattern after lowering of blood pressure and regression of cardiac hypertrophy obtained by means of labetalol, and alpha- and beta-blocking drug which inhibits the effects of catecholamines. From the 2nd to the 32nd week of age, 22 turkeys were treated with increasing doses of p.o. labetalol (from 20 to 35 mg/kg body weight daily) and 16 other turkeys were given daily p.o. placebo. Blood pressure and heart rate were periodically measured by an indirect method. After sacrifice, the degree of cardiac hypertrophy was evaluated by the biventricular weight to body weight ratio, ventricular myosin was purified, Ca++-activated ATPase activity assessed, and ventricular myosin pattern was determined by two-dimensional gel electrophoresis of myosin heavy chains. Plasma and cardiac catecholamines were measured by high performance liquid chromatography. Throughout the study period, blood pressure and heart rate were significantly reduced in the labetalol-treated animals as compared to the untreated ones. At the end of the study period, the ventricular mass was significantly lower in the labetalol group. Nevertheless, no differences were observed in ventricular myosin pattern and Ca++-activated ATPase activity levels between the two groups. In the labetalol group, an increase in plasma catecholamines and only a slight, but not significant, increase in cardiac catecholamines was found. These data indicate that in spontaneously hypertensive turkeys, the synthesis of the "fast" V1-like isomyosin is not influenced by known pathophysiological stimuli like blood pressure, cardiac hypertrophy and catecholamines.
Animals↗
Myocardial contractility and ventricular myosin isoenzymes as influenced by cardiac hypertrophy and its regression.
Changes in myocardial contractility and ventricular myosin isoenzymes were examined during pressure-overloaded cardiac hypertrophy in rats. Effects of regression of cardiac hypertrophy were also examined. Cardiac hypertrophy was induced by abdominal aortic constriction in 7-week-old male Wistar rats. Regression of cardiac hypertrophy was obtained by opening the aortic band. Myocardial contractility was estimated by measuring isometrically developed tension and maximum rate of tension rise (+dT/dtmax) in isolated left-ventricular papillary muscles perfused with Tyrode solution (32 degrees C, pH 7.4, bubbled with 95% O2.5% CO2, stimulation frequency: 0.2 Hz). Left-ventricular myosin isoenzymes were separated by pyrophosphate gel electrophoresis and the isoenzyme pattern was determined by densitometry. Isometrically developed tension (T) in hypertrophic myocardium remained unchanged, but +/-dT/dtmax decreased as compared with hearts of normal rats. Decreased +/-dT/dtmax recovered near to the level in normal rats by regression of cardiac hypertrophy. Left-ventricular myosin isoenzyme pattern shifted towards VM-3 in hypertrophied myocardium and shifted again toward VM-1 by regression of cardiac hypertrophy. In conclusion, myocardial contractility and ventricular myosin isoenzymes were changed in pressure-overloaded hypertrophy in rats and these changes were reversible to a normal level by regression of cardiac hypertrophy.
Animals↗
Effects of regression of cardiac hypertrophy on myocardial contractility and ventricular myosin isoenzymes.
The effects of regression of cardiac hypertrophy on myocardial contractility and ventricular myosin isoenzymes were investigated in rats with renovascular hypertension. Six-week-old male Wistar rats were made hypertensive by constriction of one renal artery with a silver clip. Regression of cardiac hypertrophy was induced following the lowering of blood pressure by nephrectomy on the affected side 5-6 weeks after constriction of the renal artery and was maintained for 5-6 weeks. In contrast, myocardial hypertrophy was induced by 10-11 weeks of the hypertensive state. Isometric developed tension of isolated left ventricular papillary muscles was measured, while they were being perfused with Tyrode solution. Left ventricular myosin isoenzymes were separated by pyrophosphate gel electrophoresis. The ventricular to body weight ratio of the nephrectomized group was significantly lower than that of the hypertensive group, although it was greater than that of age-matched normal control rats. There were no significant differences in the isometric developed tension among three groups, the nephrectomized, hypertensive, and normal control rats. However, dT/dtmax tended to decrease in the hypertensive rats and recovered to normal in the nephrectomized rats. The left ventricular myosin isoenzyme pattern was shifted toward VM-3 in hypertensive rats and was shifted back toward VM-1 again in nephrectomized rats.
Animals↗
Comparative analysis of chicken atrial and ventricular myosins.
1. Structural and enzymic properties of myosins from atrial and ventricular cardiac muscle of the chicken were investigated and compared with myosins from the fast skeletal pectoralis and the slow skeletal anterior latissimus dorsi muscle. 2. The Ca2+-ATPase activity, both in function of pH and [K+], of atrial myosin closely resembled that of the fast pectoralis myosin, whereas the enzymic properties of ventricular myosin were similar to those of slow skeletal myosin. 3. By sodium dodecyl sulphate polyacrylamide gel electrophoresis on gradient gel and two-dimensional electrophoresis, involving isoelectric focusing in the first dimension and SDS gel electrophoresis in the second dimension, no difference could be demonstrated in the light-chain pattern of atrial and ventricular myosin. Complete identity was also found between anterior latissimus dorsi and cardiac light chains. 4. Electrophoretic analysis of soluble peptides released by tryptic digestion of myosin and electron microscopic study of light meromyosin paracrystals showed significant differences between the heavy chains of atrial and ventricular myosins, as well as between the heavy chains of cardiac and skeletal myosins. 5. The results confirm previous immunochemical findings and provide direct biochemical evidence for the existence of a new, unique type of myosin in the chicken atrial tissue.
Animals↗
Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains.
The myosin light chain complement and proteolytic peptide patterns of myosin heavy chains were studied by two-dimensional and one-dimensional electrophoretic techniques respectively, in a total of 57 samples from ventricular and atrial tissues of normal and hypertrophied human hearts. Hypertrophies were classified haemodynamically as due to pressure-overload and volume-overload. In addition to the occurrence of ventricular light chains in hypertrophied atria we also observed the atrial light chain-1 (ALC-1) in hypertrophied ventricular tissues. On average over 6% of total light-chain-1 comprised ALC-1 in pressure-overloaded ventricles and around 3% in volume-overloaded ventricles. In single cases of pressure-overload ALC-1 amounted up to over 20% of total light chain-1. With regard to the myosin heavy chains limited digestion by two different proteinases produced over 200 clearly resoluble peptides. The absence of any detectable differences in the peptide patterns between myosin heavy chains from normal and hypertrophic tissues of left or right ventricle is in line with the findings of J. J. Schier and R. S. Adelstein (J Clin Invest 1982; 69: 816-825). In atrial tissues however, reproducible qualitative differences in the peptide patterns indicated that during hypertrophy a different type of myosin heavy chains becomes expressed. No differences were seen between the myosin heavy chains from normal left and right atria.
Cardiomegaly↗
Comparison of ATPase activities and heavy chains of rabbit atrial and thyrotoxic ventricular myosin subfragment-1.
Subfragment-1 of rabbit atrial and thyrotoxic ventricular myosin (V1 isomyosin) has been prepared and purified by DEAE-cellulose column chromatography. Pyrophosphate-polyacrylamide gel electrophoretic patterns and column chromatographic profile of the atrial subfragment differ from those of thyrotoxic ventricular myosin subfragment-1. On the other hand, Ca2+, Mg2+ and actin-activated ATPase activities of these subfragments are identical. Comparison of the peptide mapping by limited proteolysis in the presence of sodium dodecyl sulfate of the heavy and the light subunits of these subfragments reveals that the patterns for the heavy chain peptides of these subfragments are substantially similar but their light chain peptide patterns differ. The results suggest that the enzymatic and structural similarities that have been recognized between these isoenzymes using intact myosin hold true for the myosin subfragment-1. The differences between these subfragments are due to the differences in the light chains associated with them.
Animals↗