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PubMed1979

[Ultrastructural-morphometric study of cardiac myocytes in the cell culture].

Ultrastructural-morphometric studies of the right and left heart ventricles of 4-day young rat were carried out during 7-day cultivation to examine morphologic and sterologic parameters of mitochondria and myofibrils. The morphometric data demonstrated a recurrent character of mitochondria and myofibril structural changes. The changes occurred should not be regarded as structural cell differentiations but rather as adaptation to the cultivation conditions.

Animals↗
PubMed1979

Electron microscopic study of light muscle degeneration in queens of Atta sexdens (Hymenoptera: Formicidae.

The reabsorption of the flight muscles of A. sexdens queens was studied just after the autotomy of the wings, and 1,10,15,25 and 45 days thereafter. The muscle cells degenerate slowly, the first alterations taking place in the mitochondria and sarcoplasm. Signs of degeneration appear in the myofibrils after only 10 days and alterations increase with time. After 45 days the myofibrils have completely disintegrated.

Animals↗
PubMed1979

Morphological changes in the right ventricular septomarginal trabecula (false tendon) during maturation and ageing in the dog heart.

Right ventricular septomarginal trabeculae ('false-tendons') from puppies, young adult, and older adult dogs were examined by light and electron microscopy. The connective tissue of the trabeculae obtained from the puppies and the young adult dogs had few elastic fibres, but this component was well developed in the connective tissue of the adult dogs. The trabeculae of older dogs also showed scattered foci of extracellular fat droplets, and their junctional regions nearest to the ventricular wall were often heavily laden with fat. The Purkinje cells were uniform in each group, but differed from one group to another: in the puppies they resembled typical conducting cells, being predominantly cuboidal with few, poorly developed myofibrils, whilst in the adults the Purkinje cells resembled working myocytes, being elongated with a well developed complement of longitudinally arranged myofibrils. The cells of all age groups showed a complete absence of T-tubules, simply arranged interculated discs, and frequent dilatations of the sarcoplasmic reticulum. The cells of older dogs showed separations of the undifferentiated regions of most discs. Membrane degenerations and the presence of numerous fat droplets also were common. The fine structural cytology of Purkinje cells therefore appears to change considerable with age in the right ventricular septomarginal trabeculae ('false-tendons') of the dog heart.

Aging↗
PubMed1977

Dynamic characteristics of F-actin and thin filaments in vivo and in vitro.

Measurements of birefringence, ultraviolet dichorism and quasielastic light scattering were carried out on F-actin in solution and on the thin filaments of glycerinated myofibrils. The birefringence of the I-bands of myofibrils was of the same order of magnitude as that of F-actin or the F-actin-tropomyosin-troponin complex oriented in vitro at the same concentration. The ultraviolet dichroism spectrum of the I-bands was very similar to that of F-actin or the F-actin complex in vitro, which is due to orientation of bound ADP and tryptophan residues in F-actin. Quasielastic light scattering measurements, electronmicroscopic observations and the analyses of the electro-optic effect of the I-bands suggested approximately the same flexibility for F-actin in vitro and for the thin filaments in vivo. These optical measurements which were made under various conditions provide evidence for a conformational change induced by calcium ions in F-actin both in vivo and in vitro. This conformational change was found to be amplified by the interaction of F-actin with myosin. This is a brief review of our investigation on the dynamics of F-actin and the thin filament in vivo and in vitro by optical methods.

Actins↗
PubMed1976

Effect of Ca++ on Vmax measured in absence of external or internal load.

Myofibrils 1 sarcomere wide (single myofibrils) were prepared from rat heart. Mean initial sarcomere length was 2.68 mu. Contraction was initiated with 20, 25 or 100 muM MgATP and terminated with EGTA and EDTA. Single fibrils shortened at the theoretical Vmax for the in vitro conditions until sarcomere length reached 2.05 mu. At this length they encountered a significant internal afterload. Reaction time, substrate, and temperature were adjusted so that final sarcomere length was greater than or equal to 2.05 mu in most experiments. Ca++ increased Vmax of single fibrils 2- 4-fold. Results were similar at 20 and 100 muM MgATP, and in reaction mixture containing 100 or 140 mM KCI. We conclude that Ca++ controls not only the number of cross-bridges, but also the rate at which the cross-bridges turn over.

Animals↗
PubMed1980

[Quantitative morphologic studies on the myocardium in early stages of ontogenesis and after application of various cardioactive agents].

The authors have morphometrically studied the differentiation of the myocardium in dynamic phases of the embryonic and postnatal development in chickens and Syrian Hamsters. Moreover, they investigated the action of the beta-adrenalytic substances Practolol and Trimepranol on ultrastructure of the cardiac muscle in adult animals. The volume of mitochondria in myocardial cells in 6-day old chicken embryos amounts to 5.65% of the total cell volume, in 12-day old embryos 14.35%, in 18-day old embryos 19.60%, in 1-day old chickens 23.24% which is nearly as much as in adult animals. The volume of myofibrils in 6-day old embryos is about 3.2%, in 12-day old embryos about 7.4%, in 18-day old embryos about 16.4% and in 1-day old chickens about 21.2%. The differences between individual groups are statistically significant. The dynamics of differentiation of the myocardium in Syrian Hamsters was studied in 5 phases, namely in 14-day old embryos and in postnatal phases on the 2nd, 5th, 14th and 21st days after birth. Most cells in 14-day old embryos are rather immature. Participation of the volume of mitochondria, myofibrils, equipment of mitochondria with cristae etc. considerably increase in postnatal phases. These findings suggest that the heart of mammals is rather immature at birth and will differentiate mainly in the postnatal developmental phases. Many morphometric findings, as regards the action of beta-adrenalytic drugs on the ultrastructure of the myocardium in adult rabbits, point to the fact that application of these substances will give rise to degenerative alterations in approximately 10% of myocardial cells. Theoretical explantation of these mechanisms is being discussed.

Animals↗
PubMed1984

Function of M-line-bound creatine kinase as intramyofibrillar ATP regenerator at the receiving end of the phosphorylcreatine shuttle in muscle.

After 10 wash cycles, 0.8 u.e. of creatine kinase activity remained bound per mg of chicken pectoralis myofibrils which had been freed of soluble creatine kinase, mitochondria, and membranes. The bound creatine kinase is located at the M-band and contributes to the electron density of this sarcomeric structure (Wallimann, T., Pelloni, G.W., Turner, D.C., and Eppenberger, H. M. (1978) Proc. Natl. Acad. Sci. U. S. A. 75, 4296-4300). By measuring the combined actin-activated Mg2+-ATPase and creatine kinase reactions of myofibrils by pH-stat, it was shown that the amount of M-line-bound creatine kinase activity was sufficient to rephosphorylate the ATP hydrolyzed in vitro by the actin-activated Mg2+-ATPase. The amount of M-line-bound creatine kinase and thus the ATP regeneration potential depended on the muscle type. It was higher in fast muscles and lower in slow muscles. Inhibition of myofibrillar creatine kinase or extraction of the M-line-bound enzyme abolished the ATP regeneration potential without affecting ATPase activity. Inhibitors of myokinase, mitochondrial ADP/ATP translocase, and respiration did not affect the ATP regeneration potential or the ATPase. M-line-bound creatine kinase, sufficient to support an ATP turnover rate of 6s-1 per myosin head, seems to have the capacity for the intramyofibrillar regeneration of most or all of the ATP hydrolyzed by the myofibrillar ATPase during muscle contraction. Thus, M-line-bound creatine kinase at the myofibrillar receiving end of the phosphorylcreatine shuttle is of physiological significance.

Actins↗
PubMed1982

Immunofluorescence comparisons of anti-actin specificity.

The abilities of antibody populations against brain actin and two immunogenic forms of cardiac actin to react with sarcomeric muscle actin and cytoplasmic non-muscle actin were tested by indirect immunofluorescence, by using isolated skeletal muscle myofibrils and cultured non-neuronal dorsal root ganglion cells as the test systems. All three antibody preparations stained the I-bands of myofibrils, a result that demonstrated the presence of antigenic determinants shared among skeletal, cardiac, and brain actins. However, although antibodies against cytoplasmic brain actin stained the stress fibers of cultured cells, those against glutaraldehyde cross-linked cardiac actin did not, a result that implies that cardiac actin possesses determinants common to sarcomeric actins but not present on cytoplasmic actin. Finally, antibodies against SDS-treated cardiac actin readily stained the stress fibers of cultured cells, in contrast to those against glutaraldehyde cross-linked cardiac actin, a result that suggests that the state of the original immunogen can affect the actin type specificity of the resulting antibody population.

Actins↗
PubMed1983

[Modification of the affinity of actomyosin calcium sites by anions].

ATP hydrolysis-pCa and isometric tension-pCa relationships were determined for isolated myofibrils under a variety of ionic conditions i.e. in presence of Cl- ions (normal conditions), in presence of CH3COO- or CH3OSO3- (ions replacing all or a part of Cl- ions). In all ionic conditions, these relationships have a S-shape. For each ionic condition, the relationships between isometric tension or ATP hydrolysis and pCa were parallel, but the isometric tension-pCa was shifted towards a smaller value of pCa. The relation between ATP hydrolysis and pCa has been analysed by means of the enzymatic reaction described by Michaelis-Menten. The analysis of isometric tension-pCa relationship can be also described by using the consecutive scheme of reaction for the co-operative action of two Ca2+ ions in the process of tension activation given by Ashley & Moisescu (1977) for barnacle myofibrils. The dissociation constant (k1) equal to the one that we determined for the ATP hydrolysis probably corresponds to the Ca2+ binding site of troponin (M1). This association (M1-Ca) would lead to the phosphorylation of the second site (M2) localized on myosin, which can bind a Ca2+ ion. In presence of CH3COO-, ATP hydrolysis (V) was increased with no change of the affinity of the first site for the Ca2+ ion. At the opposite, V did not change but the affinity of M1 site was decreased in presence of CH3OSO3-. CH3OSO3- must be considered as a competitive inhibitor whereas CH3COO- must be considered as an activator ion of the ATP hydrolysis reaction. In all cases, the relationship between isometric tension and ATP hydrolysis was hyperbolic.

Acetates↗
PubMed1984

6-Tridecylresorcylic acid, a novel ATPase inhibitor that blocks the contractile apparatus of skeletal muscle proteins.

6-Tridecylresorcylic acid (TRA) isolated from a primula Lysimachia japonica Thunb. inhibited contraction of myofibrils, superprecipitation of myosin B, and ATPase activities of myosin and actomyosin prepared from rabbit skeletal muscle in a dose-dependent manner. The IC50 values in molarity of TRA were as follows: myosin (K+,EDTA)-ATPase, 3.5 X 10(-6); myosin Ca2+-ATPase, 3.5 X 10(-5); and actomyosin Mg2+-ATPase, 1.6 X 10(-5). The inhibition of ATPase activity of myofibrils by TRA was virtually reversed by washing with the fresh saline solution. Kinetic analysis of inhibitory effects of TRA suggests that the inhibition of (K+,EDTA)-ATPase activity of myosin or subfragment-1 is parabolic noncompetitive. TRA had no effect on alkaline phosphatase and choline acetyltransferase activities. TRA may provide a useful chemical tool for the study of the molecular mechanisms of actin-myosin contractile systems.

Actomyosin↗
PubMed1976

Studies on the specificity of smooth-muscle antibodies.

Purified contractile proteins from smooth and striated muscles have been used to test the specificity of human smooth muscle antibodies (SMA) from patients with chronic liver disease (IgG-SMA) and acute hepatitis (IgM-SMA). The reactions, as detected by indirect immunofluorescence, of IgG-SMA with renal vessel walls, renal glomeruli, peritubular fibrils and the luminal part of the tubular cells could be completely abolished by absorption with either smooth muscle or skeletal muscle F-actin, while absorption with myosin and tropomyosin had no effect. The specificity of IgG-SMA for actin was confirmed by their staining of the actin-rich I-bands of skeletal muscle myofibrils and by the blocking of this reaction by pretreatment of myofibrils and isolated smooth muscle cells with smooth muscle myosin subfragment 1 (S-1). IgM-SMA from patients with acute hepatitis-stained renal vessel walls and some sera also stained renal glomeruli. The IgM-SMA titres decreased after absorption both with myosin and F-actin but not with tropomyosin. The reactivity of some IgM-SMA could be blocked by S-1 while others could not. Thus the specificity of IgM-SMA seemed to be variable, and apparently differed from IgG-SMA in some cases.

Absorption↗
PubMed1978

Fine structure of the homologous tergo-coxal muscles of flying and flightless beetles.

The flight-related tergo-coxal muscles of flying and flightless beetles are compared. In the flying beetle, Pachynoda sinuata, the myofibrils and cylindrical and the myofilaments packed in double hexagonal arrays. The sarcomeres are short (2.8 micrometer) and wide with many large, closely packed adjacent mitochondria but the sarcoplasmic reticulum is poorly developed in this fibrillar (asynchronous) muscle. Sarcoplasmic glycogen in rosette form is abundant. In the flightless beetle, Anthia thoracica, the myofibrils are lamellar-like with sarcomeres of 5.3 micrometer. The myosin filaments form a single hexagonal array each thick filament having an orbital of 11 to 12 thin filaments. The width of the Z-line (120 nm) of A. thoracia muscle was twice that of the Z-line of P. sinuata muscle. The sarcoplasmic reticulum and T-system are well-developed in this afibrillar (synchronous) muscle. Few glycogen granules are present. Triangular projections of the sarcolemma occur regularly opposite the Z-lines in A. thoracica and they appear to extend into the Z-lines. Membranous connections joint adjacent Z-lines in A. thoracica and occasionally in P. sinuata.

Animals↗
PubMed1983

Regeneration of adult newt skeletal muscle tissue in vitro.

Explants and cells of forelimb muscle from adult Notophthalmus viridescens were cultured for periods up to 160 days in MEM-based medium supplemented with serum, hormones, and antibiotics. Explants which were not minced prior to culture contained muscle fibres with healthy myonuclei and no evidence of dedifferentiation after four weeks. Explants which were minced prior to culture contained degenerated muscle fibres after 1 day and no evidence of dedifferentiation after four weeks. Mononucleated cells from both minced and non-minced explants proliferated. Cell proliferation and myotube formation was greater in the minced muscle cultures. Proliferation and fusion of myoblasts and subsequent formation of myofibrils were observed on the plate in primary cultures. Secondarily transferred cells proliferated and fused into myotubes. Although adult newt muscle does not contain satellite cells, myogenesis in this amphibian followed the same course as all other vertebrate skeletal muscle: proliferation of mononucleated myogenic cells, fusion of the myoblasts to form syncytia, and eventual accumulation of myofibrils. The ultimate source of the myogenic cells was not identified; however, the absence of dedifferentiation of the mature fibres and the occurrence of myogenesis in cultures of minced muscle explants demonstrated that the regenerated muscle developed from a population of mononucleated cells whose origin did not depend upon dedifferentiation of intact fibres.

Animals↗
PubMed1984

[Changes in the ultrastructure and electrolyte composition of the muscles of rats during embryogenesis. I. Electron microscopic study of the structure of skeletal and heart muscle].

The ultrastructure of rat skeletal and cardiac muscles during embryogenesis was studied. Uninucleated skeletal muscle myoblasts of 13 day old embryos contain no myofibrils or discrete sarcomers, although intermediate filaments (8-13 nm) are observed. In cardiomyocytes of this stage, a formation of myofibrils from thick (15-16 nm) and thin (5-7 nm) filaments takes place. In 18-19 day old embryos, the ultrastructure of myofibrillar material is similar in skeletal and cardiac muscle cells. In cardiac muscle of 19 day old embryos, mitochondria with unusual structure were discovered: their membranes form invaginations filled up with glycogen.

Animals↗
PubMedDate not supplied

[X-ray diffraction study of the rabbit psoas muscle with extracted H-zone].

Fibre bundles of glycerinated rabbit psoas muscle about 0.5-1.0 mm thick were incubated in 5 mM tris-(hydroxymethyl)-aminomethane (Tris), pH 8.0 for 5-20 hours at 4 degrees C. This treatment leads to selective removal of some proteins in the M-bands and H-zones of sarcomeres. Effects of extraction were analyzed on the basis of electron micrographs of longitudinal sections of muscle specimens, gel electrophoresis patterns of myofibrils and of the extracts, and measurements of the creatine kinase activity of myofibrils. In the X-ray diffraction patterns of the fibre bundles subjected to prolonged extraction a drastic decrease in the intensity of "442 A" and "223 A" meridional reflections and a considerably smaller decrease in the intensity of "212 A" meridional reflections were observed. The "147 A" meridional reflection remains practically unchanged. It was concluded that: (1) The reflections "442 A" and "223 A" were contributed mainly by diffraction on the minor proteins located in the central part of the thick filaments in between the C-zones. This is contrary to the widely accepted viewpoint according to which the appearance of "442 A" reflection is caused only by the C-protein component of the thick filaments. (2) The "147 A" meridional reflection is contributed mainly by C-protein and light meromyosin of the thick filaments.

Animals↗
PubMed1981

Proteolysis of myofibrillar proteins at neutral pH.

Myofibrils that had been exposed to rat pancreatic trypsin-like serine proteinase and to beef heart Ca2+-activated thiol proteinase were examined in the electron microscope and by SDS-gel electrophoresis. The former enzyme caused more extensive disruption of the ultrastructure and degraded more of the myofibril proteins than the CA2+-activated proteinase. The susceptibilities of individual purified proteins to the two enzymes were also compared. Myosin was virtually resistant to the Ca2+-activated enzyme but with smooth muscle myosin/rat serine proteinase at a ratio of 20000/1, heavy chain degradation took place very rapidly and the ability of the degraded myosin to have its ATPase activity activated by actin in the presence of Ca2+ was lost at a similar rate. G-actin, troponins T and I and alpha-actinin were also degraded readily by the trypsin-like proteinase whereas tropomyosin, a negatively charged rodlike protein, was more resistant. The cellular location of both proteinases remains to be established but from these results obtained in vitro, consideration is given to whether these types of proteinase might work cooperatively in vivo to bring about the disassembly and turnover of myofibrillar proteins that is known to take place outside the lysosomes in muscle.

Actins↗
PubMed1981

[Ultrastructure of rat skeletal muscle fibers during prolonged static loading].

Ultrastructural characteristics of the rat skeletal muscle fibers was studied under a prolonged static loading. Disruption of the mitochondrial membranes, desintegration and lysis of myofibrils, desorganization of the T-system and Z-bands were revealed. Destructive processes were accompanied with the physiological reparative regeneration evidenced by a large number of polysomes and accumulation of myofibrils at the peripheral zone of the muscle fibre. The satellite cells with poorly developed organells were revealed in cytoplasm. Mitotic figures were present in the satellite cells. Clusters of the satellite cells were revealed in the interstitial connective tissue with their successive differentiation into mature muscle fibres. Possible mechanisms of the skeletal muscle fibre formation were discussed.

Animals↗
PubMed1980

[Quantitative comparison of the ultrastructures of the blood capillaries and muscle fibers in all stages of obliterating endarteritis].

The time course of quantitative changes in the ultrastructure of capillaries and muscle fibrers was studied by the totality of morphological signs in 33 patients with obliterating endarteritis of the lower extremities. As the disease develops, the area of luminal surface and the volume of basal membrane of the capillaries and mitochondria of muscle fibers increase progressively; the volume and number of micropinocytotic vesicles, the volume of myofibrills and the ratio of myofibrill to the mitochondria volume decrease. In early stages of the disease the size of capillary lumen decreases and subsequently increases along with a decrease in the volume of endothelial cells. An increase in the number of mitochondria in a unit of area of muscle fiber at early stages with subsequent decrease was noted. All the values of observed changes are statistically significant. None of the examined features of the structure can be considered pathognomonic separately, but the totality of the quantitative alterations gives a whole picture of the progressive disease.

Adult↗