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PubMed1978

[Ultrastructural morphometric analysis of normally loaded human myocardial left ventricles from young and old patients (author's transl)].

An ultrastructural and morphometric analysis was performed on human myocardial left ventricle, obtained during surgical heart operations on normally loaded ventricles. The diagnoses of the patients were a) Persistant foramen ovale b) Atrial septal defect stage (I.-II) c) Mitral stenosis (stage III.-IV.). The median values of left ventricular pressure were not pathologically elevated. The patients were divided in 2 groups, the younger one ranging from 5-15 years, the older from 42-78 years. It was shown that the volume density of the interstitial tissue does not differ with the aging process. The number of the nuclei per test area of the heart muscle cells decreased within age (P less than 0.001). This finding suggests a decreasing process in the number of the heart muscle cells and an increase in size of the individual myocardial cell. Increase in the volume density of myofibrils was demonstrated at electron microscopical level with aging (P less than 0.02). The volume density of mitochondria is the same in both groups, whereas the volume density of the remaining cytoplasm (without myofibrils and mitochondria) decreases (P less than 0.05). The numberical density of the mitochondria increased in the older patient group (P less than 0.001).

Adolescent↗
PubMed1976

[Experimentally induced heart muscle fiber necroses after premedication with strophanthin (author's transl)].

Number and degree of angiotensin-induced heart muscle necrosis in the rat (75 mg/kg body weight) are diminuished by premedication with strophanthin (2 X 10(-2) MG/KG BODY WEIGHT). The electron-microscopic findings are also changed: the application of angiotensin only results in vacuolization of mitochondria and a dilatation of theendoplasmatic reticulum while myofibrils are unaltered. Angiotensin in combination with strophanthin has a direct destructive effect on the myofibrils without evident changes of the mitochondria and tubular system of the heart. The protective action of Strophanithin on the heart muscle cell is discussed in the sense of an exonomization of the cellular metabolism under conditions of relative coronary insufficiency, induced by the vasoconstructive effect of angiotensin.

Angiotensin II↗
PubMed1975

Mixed Müllerian tumors of the uterus. Ultrastructural studies on the differentiation of rhabdomyoblasts.

In the present study the differentiation of rhabdomyoblasts of two carcinosarcomas of the uterus is analysed electronmicroscopically. During the development of rhabdomyoblasts three cell types can be distinguished: 1. the undifferentiated mesenchymal cell with abundant ribosomes but few other cell organelles. Usually these cells are already associated to each other in strands of 2-4 cells. Occasionally cytoplasmic areas with numerous nonspecific filaments can be observed. 2. the light rhabdomyoblast which is characterized by its conspicuous nonspecific cytoplasmic filaments and its reduction in ribosomes. Specific myofilaments can be visualized only occasionally in this cell type. 3. more differentiated rhabdomyoblasts. These cells can be identified clearly by the presence of large numbers of myofibrils and myofibrillar fragments. Higly organized myofibrils as seen in skeletal muscle are seldom found. Transitional forms between these cell types are also observed. The functions of Z-bodies and of the sarcotubular system in the process of myofibrillar differentiation are discussed.

Aged↗
PubMed1975

Myoid fibrils in epithelial cells: studies of intestine, biliary and pancreatic pathways, trachea, bronchi, and testis.

Cytoplasmic filaments have been studied extensively by electron microscopy, but the histochemical nature of such fibrils in non-keratinizing epithelia has not been systematically investigated. During studies of early arterial lesions we observed structures with the staining properties of myosins in epithelial cells of various organs. The configurational staining, polarization and fluorescence microscopic properties of these myoid structures were compared with those of myofibrils in smooth muscle and classical myoepithelial cells. The following structures showed the characteristics of myofibrils: the terminal web in columnar epithelial cells of intestine, trachea, bronchi, bile ducts, pancreatic ducts and ductus epididymidis, the pericanalicular layer of bile and pancreatic canaliculi, fibers in the caudal tube of spermatids and the flagella of spermatozoa. Cilia, e.g. of respiratory epithelium, tonofibrils in squamous epithelium and nerve axons did not react. These studies indicate significant histochemical differences between cytoplasmic filaments. Different types of intracellular fibrils can be found in the same cell, e.g. in respiratory epithelium.

Bile Ducts, Intrahepatic↗
PubMed1975

Myoepithelial cells in human thymus: staining, polarization and fluorescence microscopic studies.

Myoid cells in human thymus were studied around the turn of the century, and alterations in patients with cardiovascular disease were reported. It was therefore deemed of interest to reinvestigate these long forgotten cells. The configurational staining, polarization and fluorescence microscopic properties of smooth myofibrils in thymic epithelial cells were identical with those of classical myoepithelial cells, smooth muscle, and A bands of striated muscle. Cross-striated myoid cells could not be found in thymus of children. Myoepithelial cells formed a layer at the surface of thymic lobules; others were scattered throughout the cortex and medulla. In addition, the medulla contained seemingly hypertrophic myoepithelial cells. Hassall's corpuscles consisted of layers of myoepithelial cells. Hammar (1905) regarded epithelial cells with smooth myofibrils in human thymus as equivalents of the cross-striated myoid cells in lower vertebrates. The myoepithelial cells observed in this study are apparently identical with the smooth myoid cells of early anatomists; the hypertrophic myoepithelial cells correspond to the unicellular Hassall's corpuscles. The functions of these cells are not yet clear; the wide variations from case to case in the same age group indicate that the myoepithelial cells are affected by a variety of diseases.

Epithelial Cells↗
PubMed1976

Enzymatic changes in hypertrophied fast-twitch skeletal muscle.

Fast-twitch plantaris muscles of female rats were subjected to unilateral compensatory overload, induced by partial excision of synergistic muscles. One group of rats remained sedentary whereas another was subjected to a supplemental program of treadmill exercise consisting of walking 3 m/min, 65% grade, 2 h/day, 5 days/week. Groups of rats were sacrificed after 1, 2, 4, and 8 weeks and their muscles were weighed and analyzed for protein, citrate synthase, phosphofructokinase (PFK) and myofibril ATPase. Absolute and relative (muscle weight/body weight) muscle weights were much greater in both overloaded groups as compared to contralateral controls. However, treadmill exercise also increased the absolute and relative muscle mass of control plantaris muscles in the exercising group as compared tonormal sedentary contralateral controls. Citrate synthase activity was decreased in overloaded, sedentary muscles as compared to contralateral controls, but after 8 weeks of exercise, it returned to normal levels. PFK was decreased in both sedentary and exercised overloaded muscles throughout the 8 week period. Myofibril ATPase showed a tendency to be reduced in sedentary, overloaded muscles, and was significantly reduced in overloaded, exercising muscles. These results collectively suggest that certain fibers of overloaded fast-patterns take on similar in certain aspects to that normally seen in differentiated slow-twitch muscle fibers.

Adenosine Triphosphatases↗
PubMed1986

Light diffraction patterns and sarcomere length variation in striated muscle fibers of Limulus.

Light diffraction patterns produced by Limulus striated muscle fibers were examined. Segments of fibers were glycerinated, fixed or bathed in relaxing solution. Profiles of the intensity of a diffracted order vs. the angle of incidence of the laser beam often exhibited narrow peaks with the fiber at rest length. The incident angles at which the intensity of left and right orders is greatest are used to calculate the sarcomere length, supporting the notion that regions of the fiber are organised into Bragg reflecting planes. These profiles developed subpeaks and broadened upon stretch of the fiber. The broad angle scan profiles are suggested to result from a decrease in the regular packing of myofibrils as the fiber is lengthened. The angular width of the subpeaks is used to estimate the thickness of clusters of myofibrils. The variation in sarcomere length along the fiber, as determined by the 0th to 1st diffraction order spacing, was dependent upon the fiber preparation. Glycerinated fibers and those bathed in relaxing solution showed more variation than fixed fibers. The variation of sarcomere length is compared to the variation in thick filament lengths in Limulus reported by Dewey et al. (1982). These results are compared to those obtained from frog fiber segments.

Animals↗
PubMed1975

Ultrastructural aspects of muscle and nerve in Werdnig-Hoffmann disease.

The authors describe in biopsies from 6 cases of Werdnig-Hoffmann disease, including 2 of the more benign type, the ultrastructural typical aspects of denervation. They compare their findings with those of other workers. The striking points are the great variation in the diameter of the muscle fibres and the myofibrils, the disorganisation of the myofibrils, the sarcomeres and the filaments, with persistance of the relations between thick and thin filaments at various levels, the modifications of the Z-band and the triads in chains. The folds and the basement membrane are examined. Centrioles are present in a muscle fibre and in a satellite. Glycogen is very abundant. The nerves seem normal but some Schwann cells contain pi granules which are not observed usually at the age of the patient. The end plates and a muscle spindle are normal.

Basement Membrane↗
PubMed1994

Myofibrillar adaptations during cardiac hypertrophy.

The main purpose of this study was to determine the transmural adaptive changes that occur in cell size, myofibrils, and myosin isoforms from the endocardium (ENDO) to the epicardium (EPI) of the left ventricle (LV) of the rat heart during compensatory hypertrophy. Hypertrophy was induced by supra-renal aortic constriction for periods of 2, 7, 15 and 30 days. Percent left ventricular hypertrophy averaged 63 +/- 9.7% at 30 days following constriction. A significant (p < 0.05) transmural gradient in the V3 myosin isoform (9 +/- 0.7% ENDO vs. 5 +/- 1.8% EPI) was initially observed at 7 days and was still evident by 30 days (25 +/- 3.6% ENDO vs 15 +/- 2.0% EPI). Cell cross-sectional area was also greater (p < 0.05) in the ENDO than in the EPI at 7, 15 and 30 days. MF diameter was determined only at 30 days and was found to be similar to control values in both the hypertrophied ENDO (sham 1.24 +/- 0.05 vs hyp 1.18 +/- 0.09 microns) and EPI (sham 1.17 +/- 0.08 vs hyp 1.06 +/- 0.08 microns). The combined effects of cardiac myocyte hypertrophy with no change in MF diameter resulted in a calculated increase of approximately 70% in the number of myofibrils per myocyte both in the ENDO and EPI. It was concluded that the adaptive strategy of the left ventricular free wall to pressure overload was to initially increase myocyte cross-sectional area and then switch myosin expression from V1 to V3, both of which proceeds transmurally from the sub-endocardium towards the sub-epicardium.(ABSTRACT TRUNCATED AT 250 WORDS)

Adaptation, Physiological↗
PubMed1995

Proteolytic activity of proteasome on myofibrillar structures.

The physiologic function of proteasome remains unclear. Evidence suggests a role in degradation of ubiquitin-protein conjugates, MHC antigen presentation, and some specificity of substrate within certain cell types. To explore further the properties of proteasome we have examined its effect on a well defined structure, the myofibril. We find that despite its large size (20S) proteasome is able to degrade myofibrils and intact, permeabilized muscle fibrils. The proteins degraded showed some specificity because actin, myosin and desmin were degraded faster than alpha-actinin, troponin T and tropomyosin. Changes in ultrastructure were slow and included a general loss of structure with Z and I bands effected before the M band and costameres.

Animals↗
PubMed1995

Troponin subunits contribute to altered myosin ATPase activity in diabetic cardiomyopathy.

Our group has documented that myocardial performance is impaired in the hearts of chronically diabetic rats and rabbits. Abnormalities in the contractile proteins and regulatory proteins may be responsible for the mechanical defects in the streptozotocin (STZ)-diabetic hearts. Previously, the major focus of our research on contractile proteins in abnormal states has concentrated on myosin ATPase and its isoenzymes. Our present study is based on the overall hypothesis that regulatory proteins, in addition to contractile protein, myosin contribute to altered cardiac contractile performance in the rat model of diabetic cardiomyopathy. The purpose of our research was to define the role of cardiac regulatory proteins (troponin-tropomyosin) in the regulation of actomyosin system in diabetic cardiomyopathy. For baseline data, myofibrillar ATPase studies were conducted in the myofibrils from control and diabetic rats. To focus on the regulatory proteins (troponin and tropomyosin), individual proteins of the cardiac system were reconstituted under controlled conditions. By this approach, myosin plus actin and troponin-tropomyosin from the normal and diabetic animals could be studied enzymatically. The proteins were isolated from the cardiac muscle of control and STZ-diabetic (4 weeks) rats. Sodium dodecyl sulfate gel electrophoretic patterns demonstrate differences in the cardiac TnT and TnI regions of diabetic animals suggesting the different amounts of TnT and/or TnI or possibly different cardiac isozymes in the regulatory protein complex. Myofibrils probed with a monoclonal antibody TnI-1 (specific for adult cardiac TnI) show a downregulation of cardiac TnI in diabetics when compared to its controls. Enzymatic data confirm a diminished calcium sensitivity in the regulation of the cardiac actomyosin system when regulatory protein(s) complex was recombined from diabetic hearts. Actomyosin ATPase activity in the hearts of diabetic animals was partially reversed when myosin from diabetic rats was regulated with the regulatory protein complex isolated from control hearts. To our knowledge, this is the first study which demonstrates that the regulatory proteins from normal hearts can upregulate cardiac myosin isolated from a pathologic rat model of diabetes. This diminished calcium sensitivity along with shifts in cardiac myosin heavy chain (V1-->V3) may be partially responsible for the impaired cardiac function in the hearts of chronic diabetic rats.

Animals↗
PubMed1992

Distribution of developmental myosin isoforms in isolated A-segments.

Immunogold labelling was used to determine the distribution of myosin isoforms within the A-bands of developing chicken pectoralis muscles. Previous localization studies led to the suggestion that neonatal myosin is preferentially located in the centre of heterogeneous thick filaments that contain either embryonic or adult myosin in addition to neonatal myosin. To further explore the possibility that neonatal myosin may serve to nucleate thick filament assembly, a method was developed to isolate A-segments (arrays of myosin filaments) from myofibrils in the presence of MgATP. A-bands usually dissociate into thick and thin filaments in a relaxing buffer, but the inclusion of an antibody against M-line protein prevented separation of the thick filament array. Well-ordered A-segments, approximately 1.5 microns in length, were prepared from muscles 12, 29, 40 days, and approximately 1 year after hatching. After reaction with monoclonal antibodies specific for neonatal and adult myosins, the A-segments were labelled with gold-conjugated secondary antibodies prior to negative staining. An antibody which cross-reacts with embryonic myosin was used to localize that epitope in A-bands of myofibrils from day 1 and day 3 posthatch muscles. At ages where expression of neonatal myosin was high, extensive gold labelling of A-segments was observed in the electron microscope. However, no preferential distribution of antibodies was observed at any age, independent of whether embryonic or adult myosin was coexpressed with the neonatal myosin, suggesting that neonatal myosin is not segregated to any particular region in the A-bands of developing muscles.

Age Factors↗
PubMed1986

Accumulated strain mechanism for length determination of thick filaments in skeletal muscle. I. Experimental bases.

The kinetics of dissociation of myosin from both ends of thick filaments in glycerinated skeletal muscle fibres and myofibrils was studied in the presence of MgATP by use of an optical diffraction method and phase-contrast microscopy. The dissociation velocity, v (identical to -dL/dt where L is the length of thick filaments at time t), increased with increasing KCl concentration (0.225 to 0.5 M), or increasing pH (6.5 to 8.0) but hardly changed with temperature (5 and 25 degrees C), micromolar concentrations of Ca2+ or sarcomere length (2.4 and 2.75 micron). Over a wide range of filament length, the dissociation velocity could be expressed by v0exp(alpha L), where v0 and alpha are positive constants depending upon the dissociation condition. When the effects of crossbridge formation are minimized it was thus shown that the structural stability of thick filaments in a muscle fibre and a myofibril gradually decreases from the central part to the tips of the filaments. On the basis of these results we propose that the length of thick filaments is largely regulated by an accumulated strain mechanism in which the free energy of association of myosin molecules increases with filament length.

Animals↗
PubMed1990

Digestion of proteins associated with the Z-disc by calpain.

The Z-disc of striated muscle is degraded by the Ca2(+)-activated proteinase, calpain, during autolysis of muscle fibres. The effect of calpain on proteins in preparations of Z-discs isolated from Lethocerus flight muscle has been studied. Calpain releases alpha-actinin from the Z-disc and digests two hydrophobic proteins associated with the Z-disc, zeelin 1 (35 kD) and zeelin 2 (23 kD). The Ca2+ sensitivity of zeelin digestion is shifted to lower Ca2+ concentrations (within the physiological range) in the presence of the phospholipids phosphatidyl inositol or phosphatidyl choline and diacylglycerol. The release of alpha-actinin is not affected by phospholipid. Preparations of isolated Z-discs have five times as much associated phospholipid (w/w) as myofibrils and the composition of the lipid differs from that of myofibrils. In muscle fibres the action of calpain on zeelins may be controlled by the composition of phospholipid in the fibres as well as by Ca2+.

Actinin↗
PubMedDate not supplied

Time course of electron microscopic alterations in the hypertrophied myocardium of Goldblatt rats.

In Goldblatt rats, electron microscopic investigations of morphological changes in heart tissue during the compensatroy stage of pressure induced cardiac hypertrophy were performed. Myocardial cellular size enlarged considerably within the first 4 weeks after renal artery coarctation. An enlargement of the T-tubular system is particularly striking. The ratio of myofibril volume to total cell volume is significantly increased from the 4th-24th week and can at least partially explain a rise in developed tension which occurs in spite of a frequent disarrangement of myofibrils. In later stages severe changes in the vessel walls take place and there is an augmentation of connective tissue which impairs a correlation between myocardial cell alterations and mechanical parameters.

Animals↗
PubMedDate not supplied

A biphasic change in contractile proteins during the development of cardiac hypertrophy in pigs.

A non-failing hypertrophy of the left ventricle was produced in the pig heart by supravalvular banding of aorta for 4, 8 and 12 weeks and the myosin and myofibrillar adenosine triphosphatase activities were measured. A significant increase in myosin Ca2+-ATPase activity was seen at 4 weeks of hypertrophy, but at 8 and 12 weeks this activity was significantly decreased compared to sham control. Similar changes were also seen in actin-activated myosin ATPase activities at 4, 8 and 12 weeks of hypertrophy. There were no changes in the K+- and NH4+-EDTA-stimulated ATPAse activities of myosin. Basal ATPase activities of myofibrils were decreased at 4 and 8 weeks of hypertrophy and there was no change in this activity at 12 weeks of hypertrophy. Ca2+ stimulated ATPase activity of myofibrils was significantly increased at 4 weeks, normal at 8 weeks and significantly reduced at 12 weeks of hypertrophy. The changes in ATPase activities were not due to any alterations of proteins by high concentrations of salts during the purification of myosin. The non-hypertrophied right ventricle from the banded animals did not show any change in the basal or Ca2+ stimulated myofibrillar ATPase activities. It is suggested that hypertrophy of the myocardium is accompanied by specific changes in the enzyme activities of the contractile proteins and the biphasic responses may correlate with the functional state of the myocardium subjected to a chronic increase in pressure.

Adenosine Triphosphatases↗
PubMed1990

Activation of troponin C by Cd2+ and Pb2+.

Certain heavy metal actions such as Cd2+ and Pb2+ mimic Ca2+ effectively in stimulating calmodulin (CaM). We now show that these cations also activate skeletal muscle troponin C (TnC), a Ca2(+)-binding protein highly homologous to CaM. Like Ca2+, these cations allow TnC to alter its electrophoretic mobility on polyacrylamide gels, and to bind to phenyl-Sepharose. Moreover, they activate TnC to stimulate myofibrillar ATPase. When TnC was removed from the skeletal myofibrils by treatment with trans-1,2-cyclohexanediamine-N,N,N',N'-tetraacetic acid (CDTA), the ATPase activity was no longer stimulated by the cations. However, after reconstitution of CDTA-treated skeletal myofibril with TnC, the response of ATPase to Ca2+, Cd2+ or Pb2+ was restored. These findings suggest that the activation of myofibrillar ATPase by Cd2+ and Pb2+ is mediated through TnC. The ability of the heavy metals to stimulate TnC-supported ATPase activity correlated quite well with the ability to increase the extent of the myofibrillar superprecipitation. The activation of TnC by Cd2+ or Pb2+ could constitute a possible molecular basis for their toxicity.

Adenosine Triphosphatases↗
PubMedDate not supplied

Cooperative effects of calcium on myofibrillar ATPase of normal and hypertrophied heart.

The ATPase of myofibrils from normal and hypertrophied rat heart was studied in relation to the Ca2+-dependence of the reaction. The experimental data were fitted to theoretical curves based on the Hill equation. A positive cooperativity (n = 1.6) was found for the activation curve of the ATPase from normal heart. For hypertrophied heart no significant change in either the cooperativity or the Ca2+-sensitivity of troponin was detected. This indicates that the troponin-tropomyosin system is not altered during pressure-overload hypertrophy. However, it should be noted that no precautions were taken to control the state of phosphorylation of contractile proteins during the preparation of myofibrils.

Adenosine Triphosphatases↗