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1.
Mar Royuela Catherine Astier Xavier Grandier-Vazeille Yves Benyamin Benito Fraile Ricardo Paniagua Michel Duvert 《Invertebrate Biology》2003,122(1):74-82
Abstract. A light and electron immunohistochemical study was carried out on the body wall muscles of the chaetognath Sagitta friderici for the presence of a variety of contractile proteins (myosin, paramyosin, actin), regulatory proteins (tropomyosin, troponin), and structural proteins (α‐actinin, desmin, vimentin). The primary muscle (~80% of body wall volume) showed the characteristic structure of transversely striated muscles, and was comparable to that of insect asynchronous flight muscles. In addition, the body wall had a secondary muscle with a peculiar structure, displaying two sarcomere types (S1 and S2), which alternated along the myofibrils. S1 sarcomeres were similar to those in the slow striated fibers of many invertebrates. In contrast, S2 sarcomeres did not show a regular sarcomeric pattern, but instead exhibited parallel arrays of 2 filament types. The thickest filaments (~10–15 nm) were arranged to form lamellar structures, surrounded by the thinnest filaments (~6 nm). Immunoreactions to desmin and vimentin were negative in both muscle types. The primary muscle exhibited the classical distribution of muscle proteins: actin, tropomyosin, and troponin were detected along the thin filaments, whereas myosin and paramyosin were localized along the thick filaments; immunolabeling of α‐actinin was found at Z‐bands. Immunoreactions in the S1 sarcomeres of the secondary muscle were very similar to those found in the primary muscle. Interestingly, the S2 sarcomeres of this muscle were labeled with actin and tropomyosin antibodies, and presented no immunore‐actions to both myosin and paramyosin. α‐Actinin in the secondary muscle was only detected at the Z‐lines that separate S1 from S2. These findings suggest that S2 are not true sarcomeres. Although they contain actin and tropomyosin in their thinnest filaments, their thickest filaments do not show myosin or paramyosin, as the striated muscle thick myofilaments do. These peculiar S2 thick filaments might be an uncommon type of intermediate filament, which were labeled neither with desmin or vimentin antibodies. 相似文献
2.
Mar Royuela Benito Fraile Rosa García-Anchuelo Ricardo Paniagua 《Journal of morphology》1995,224(1):87-96
Muscles in the body wall, intestinal wall, and contractile hemolymphatic vessels (pseudohearts) of an oligochaete anelid (Eisenia foetida) were studied by electron microscopy. The muscle cells in all locations, except for the outer layer of the pseudohearts, are variants of obliquely striated muscle cells. Cells comprising the circular layer of the body wall possess single, peripherally located myofibrils that occupy most of the cytoplasm and surround other cytoplasmic organelles. The nuclei of the cells lie peripherally to the myofibrils. The sarcomeres consist of thin and thick myofilaments that are arranged in parallel arrays. In one plane of view, the filaments appear to be oriented obliquely to Z bands. Thin myofilaments measure 5–6 nm in diameter. Thick myofilaments are fusiform in shape and their width decreases from their centers (40–45 nm) to their tips (23–25 nm). The thin/thick filament ratio in the A bands is 10. The Z bands consist of Z bars alternating with tubules of the sarcoplasmic reticulum. Subsarcolemmal electron-dense plaques are found frequently. The cells forming the longitudinal layer of the body wall musculature are smaller than the cells in the circular layer and their thick filaments are smaller (31–33 nm centrally and 21–23 nm at the tips). Subsarcolemmal plaques are less numerous. The cells forming the heart wall inner layer, the large hemolymphatic vessels, and the intestinal wall are characterized by their large thick myofilaments (50–52 nm centrally and 27–28 nm at the tips) and abundance of mitochondria. The cells forming the outer muscular layer of the pseudohearts are smooth muscle cells. These cells are richer in thick filaments than vertebrate smooth muscle cells. They differ from obliquely striated muscle cells by possessing irregularly distributed electron-dense bodies for filament anchorage rather than sarcomeres and Z bands and by displaying tubules of smooth endoplasmic reticulum among the bundles of myofilaments. © 1995 Wiley-Liss, Inc. 相似文献
3.
4.
In Megalobulimus abbreviatus, the ultrastructural features and the contractile proteins of columellar, pharyngeal and foot retractor muscles were studied. These muscles are formed from muscular fascicles distributed in different planes that are separated by connective tissue rich in collagen fibrils. These cells contain thick and thin filaments, the latter being attached to dense bodies, lysosomes, sarcoplasmic reticulum, caveolae, mitochondria and glycogen granules. Three types of muscle cells were distinguished: T1 cells displayed the largest amount of glycogen and an intermediate number of mitochondria, suggesting the highest anaerobic metabolism; T2 cells had the largest number of mitochondria and less glycogen, which suggests an aerobic metabolism; T3 cells showed intermediate glycogen volumes, suggesting an intermediate anaerobic metabolism. The myofilaments in the pedal muscle contained paramyosin measuring between 40 and 80 nm in diameter. Western Blot muscle analysis showed a 46-kDa band that corresponds to actin and a 220-kDa band that corresponds to myosin filaments. The thick filament used in the electrophoresis showed a protein band of 100 kDa in the muscles, which may correspond to paramyosin. 相似文献
5.
R A Murphy 《Federation proceedings》1976,35(6):1302-1306
The contractile systems of vertebrate smooth and striated muscles are compared. Smooth muscles contain relatively large amounts of actin and tropomyosin organized into thin filaments, and smaller amounts of myosin in the form of thick filaments. The protein contents are consistent with observed thin:thick filament ratios of about 15-18:1 in smooth compared to 2:1 in striated muscle. The basic characteristics of both types of contractile proteins are similar; but there are a variety of quantitative differences in protein structures, enzymatic activities and filament stabilities. Biochemical and X-ray diffraction data generally support recent ultrastructural evidence concerning the organization of the myofilaments in smooth muscle, although a basic contractile unit comparable to the sarcomere in striated muscle has not been discerned. Myofilament interactions and contraction in smooth muscle are controlled by changes in the Ca2+ concentration. Recent evidence suggests the Ca2+-binding regulatory site is associated with the myosin in vertebrate smooth muscle (as in a variety of invertebrate muscles), rather than with troponin which is the regulatory protein associated with the thin filament in vertebrate striated muscle. 相似文献
6.
Summary The arrangement of myofilaments in the striated visceral muscle fibers of two arthropods (crayfish and fruitfly) and in the unstriated visceral fibers of one annelid (earthworm) was studied comparatively. Transverse sections through the A bands of arthropod visceral fibers indicate that each thick myofilament is surrounded by approximately 12 thin filaments. The myofilaments are less organized in the visceral fibers of the earthworm than in muscle fibers of the crayfish and fruitfly. The thick myofilaments of the earthworm are composed of subunits, 20–30 Å in diameter. The presence of two distinct sets of myofilaments in these slowly contracting striated and unstriated visceral muscle fibers suggests that contraction is accomplished via a sliding filament mechanism.In crayfish visceral fibers the sarcolemma invaginates at irregular intervals to form a long and unbranched tubular system at any level in the sarcomere. Dyads formed by the apposition of T and SR membranes are observed frequently. The distribution of the T and SR systems in the visceral fibers of the fruitfly and the earthworm is markedly reduced and dyads are infrequently observed. The reduced T and SR systems may be related to the slow contraction of these fibers. Transport of specific substances across the sarcolemma could initiate contraction or relaxation in these fibers.This study was supported by a training grant GM-00582-06 from the U.S. Public Health Service. 相似文献
7.
In order to evaluate the effects of specific mutations on sarcomere assembly and function in vivo, we describe the course of normal development of Drosophila indirect flight muscle (IFM) in staged pupae using electron microscopy. We find that no contractile assemblies remain in larval muscle remnants invaded by imaginal myoblasts, establishing that myofibrils in IFM assemble de novo. Stress-fiber-like structures or other template structures are not prominent before or during sarcomere assembly. By 42 hr pupation (eclosion 112 hr), thick and thin filaments have appeared simultaneously in slender, interdigitated arrays between regularly spaced Z-bodies. Each tiny, uniformly striated myofibril forms within a "sleeve" of microtubules, and both microtubules and myofibrils are attached to the cell membrane at each end of the fiber from the initial stages of assembly. Later in pupation, the microtubule "sleeves" disassemble. Sarcomere number appears to remain constant. We saw no evidence that terminal sarcomeres are sites for addition of new sarcomeres or that Z-lines split transversely, producing new, very short sarcomeres. Rather, initial thick and thin filaments and sarcomeres are much shorter than adult length. Sarcomere length increases smoothly and coordinately from 1.7 to 3.2 μm, reflecting increase in filament lengths and indicating that myosin and actin molecules must be incorporated into filaments after sarcomere formation. Myofilaments are not seen scattered in the cytoplasm at any time, nor do we detect filaments that could be in the process of being "trolleyed" along myofibrils into positions of lateral register. Myofibril diameter increases uniformly from 4-thick filaments to 36-thick filaments across, by peripheral addition of myofilaments. At each successive stage, all sarcomeres in a fiber attained similar length and diameter. Initial thick filaments are solid but within several hours these and all subsequently assembled thick filaments appear hollow. Initial Z-bodies do not show any internal lattice and are more irregularly shaped than adult Z-discs. 相似文献
8.
The fine structure of the obliquely striated muscle cells of the longitudinal muscle of an annelid was investigated. The characteristics of myofilaments and cell components, such as sarcoplasmic reticular system (S.R.), T-systems and J-rods corresponded to those previously reported, but it was noted for the first time that the cells could be classified into two types with respect to the diameters of their thick myofilaments. In one type, the thick myofilaments were about 29 nm in diameter (A-type) and in the other they were about 41 nm in diameter (B-type). Most of the obliquely striated muscles described to date have been composed of a single type of cell, but we found two types of cell mixed together in the longitudinal muscle. The A-type cells with slender thick myofilaments were distributed mainly in the inner part of the muscle and the B-type cells with broader thick myofilaments were distributed in the outer part. 相似文献
9.
R. G. Sherman 《Journal of morphology》1973,140(2):215-241
The ultrastructural features of cardiac muscle cells and their innervation were examined in the tarantula spider Eurypelma marxi Simon. The cells are transversely striated and have an A band length of about three microns. H zones are indistinct and M lines are absent. Thick and thin myofilament diameters are approximately 200 and 70 Å respectively. Eight to 12 thin filaments usually surround each thick one. Accumulations of thick and thin myofilaments occur perpendicular to the bulk of the myofilaments in some cells. The Z line is discontinuous and thick filaments may pass through the spaces in the Z line. Extensive systems of sarcoplasmic reticulum and transverse tubules are present; these form numerous dyadic junctions in both A and I band regions. Sarcolemmal invaginations form Z line tubules; lateral extensions of the plasma membrane portion of these invaginations form dyads. Nerve branches of the cardiac ganglion make multiple neuromuscular synapses with at least some of the cardiac muscle cells. Both large granular and small agranular vesicles are present in the presynaptic terminals. Intercalated discs similar to those present in other arthropod hearts occur between the ends of adjacent cardiac muscle cells. 相似文献
10.
Summary. Our immunocytochemical observations reveal that the muscle present in the tips of the arms of the Antarctic cushionstar Odontaster validus contains caldesmon and calponin but not troponin. Thus, the muscle clearly belongs to the smooth muscle category. Distributions
of contractile proteins such as actin, myosin (the latter a typical vertebrate muscle filament protein), paramyosin, and miniparamyosin
(the latter two being characteristic of thick invertebrate muscle filaments) were also determined immunocytochemically. The
results suggest that the thin filaments of the starfish smooth muscle are similar to those of the vertebrate muscle, but that
the thick filaments differ from those of vertebrates and possess traits that are also seen in the muscle organization of invertebrates.
The absence from the O. validus muscle of titin and nebulin, proteins so far known almost exclusively from the striated vertebrate muscle, comes as no surprise,
but immunoreactivity to mini-titin (a protein of the same family as titin and its replacement in invertebrates) was strong
and unambiguously recognizable between filaments. Odontaster validus' histochemical characteristics may be a reflection of the phylogenetic position of the echinoderms as deuterostome invertebrates
or they may express an adaptation of the muscle to the harsh environmental conditions under which it has to function in the
Antarctic water.
Received June 6, 2002; accepted September 17, 2002; published online March 11, 2003 相似文献
11.
Summary Myofilaments were isolated by gently homogenizing smooth muscle cells isolated from the pedal retractor muscle (PRM) of Mytilus edulis, and observed by electron microscopy. The thick filaments isolated in the presence of ATP (10–20 mM) had projections of myosin heads except near their centre (central bare zone). After extraction of myosin, the paramyosin core of the thick filaments showed a Bear-Selby net or a striated pattern with a main periodicity of 14.5 nm. Both the Bear-Selby net and the striated patterns had a polarity that reversed at the centre of the filament where the patterns were obscured. The thin filaments were attached to dense bodies. Decoration of the thin filaments with heavy meromyosin showed that they have opposite polarity on opposing sides of the dense body. The results indicate that the thick filaments are bipolar and also that the dense bodies are functionally analogous to the Z-disk of the striated muscle. 相似文献
12.
Summary The myosin filaments of the flight muscles of the locust Locusta migratoria, the cockchafer Melolontha melolontha and the femur muscles of L. migratoria have solid centers. Those of the flight muscles of the housefly Musca domestica and Drosophila melanogaster are tubular. Electron micrographs of myofibrils of the fleshfly Phormia terrae-novae contain both filament types within one sarcomere and suggest the existence of 4 cross-bridges per crown.Estimates of the ratios of myosin to paramyosin and of myosin to actin on sodium dodecyl sulphate-polyacrylamide gels yielded paramyosin contents of 9% of the thick filament mass for the solid and 2.6% for the tubular filaments (3.8% for P. terrae-novae). Based on the myosinactin ratios up to 6 myosin dimers per crown could be calculated.The molar ratio of actin to arthrin on SDS gels was found to be 3.37 for native and extracted myofibrils of flight muscles from P. terrae-novae. Arthrin is also present in isolated actin filaments suggesting that it is localized in or on the thin filaments. If we assume that it is constituent part of the helices of the thin filaments the number of myosin dimers per crown can be diminished to 4.5, considerably closer to the values obtained by evaluation of electron micrographs.Dedicated to Prof. Dr. Bernhard Rensch on his 85th birthday 相似文献
13.
The skeletal muscles of rotifers and their innervation 总被引:2,自引:2,他引:0
The skeletal muscles of rotifers are monocellular or occasionally bicellular. They display great diversity of cytological features correlated to their functional differentiation. The cross-striated fibers of some retractors are fast contracting and relaxing, with A-band lengths of 0.7 µm to 1.6 µm, abundant sarcoplasmic reticulum and dyads. Other retractors and the circular muscles are tonic fibers (A band > 3 µm), stronger (large volume of myoplasm) or with greater endurance (superior volume of mitochondria/ myoplasm). All of these retractor muscles are coupled by gap junctions and are innervated at two symmetrical points; they constitute two motor units implicated in withdrawal behaviour.The muscles inserted on the ciliary roots of the cingulum control swimming. They are multi-innervated and each of them constitute one motor unit. They have characteristics of very fast fibers; the shortest A-band length is 0.5 µm in Asplanchna.All the skeletal muscles of bdelloids are smooth or obliquely striated as are some skeletal muscles of monogononts. These muscles are well suited for maximum shortening and are either phasic or tonic fibers.All rotifer skeletal muscles originate from ectoderm and contain thin and thick myofilaments whose diameters are identical to those of actin and myosin filaments in vertebrate fast muscles or in insect flight muscles. There are no paramyosinic features in the thick myofilaments. The insertion, innervation, coupling by gap junctions and other cytological differentiations of rotifer skeletal muscles are reviewed and their phylogeny discussed. 相似文献
14.
The ultrastructure of the adductor muscle of the boring clam (Tridacna crocea) was investigated. The adductor was composed of opaque and translucent portions. The opaque portion contained smooth muscle cells; the translucent portion contained obliquely striated cells. Smooth muscle cells were classified, according to the statistically analyzed diameters of their thick myofilaments, into two types, S-1 and S-2. S-1 cells had thick myofilaments, 50–60 nm in diameter. S-2 cells had thick myofilaments of two sizes, about 55–65 nm and 85–100 nm in diameter, respectively. Obliquely striated muscle cells in the translucent portion were also classified into two types: O-1 cells, with thick myofilaments 30–35 nm in diameter, and O-2 cells, with myofilaments of 50–60 nm. 相似文献
15.
Fine structural characteristics of the cardiac muscle and its sarcomere organization in the black widow spider, Latrodectus mactans were examined using transmission electron microscopy. The arrangement of cardiac muscle fibers was quite similar to that of skeletal muscle fibers, but they branched off at the ends and formed multiple connections with adjacent cells. Each cell contained multiple myofibrils and an extensive dyadic sarcotubular system consisting of sarcoplasmic reticulum and T‐tubules. Thin and thick myofilaments were highly organized in regular repetitive arrays and formed contractile sarcomeres. Each repeating band unit of the sarcomere had three apparent striations, but the H‐zone and M‐lines were not prominent. Myofilaments were arranged into distinct sarcomeres defined by adjacent Z‐lines with relatively short lengths of 2.0 μm to 3.3 μm. Cross sections of the A‐band showed hexagon‐like arrangement of thick filaments, but the orbit of thin filaments around each thick filament was different from that seen in other vertebrates. Although each thick filament was surrounded by 12 thin filaments, the filament ratio of thin and thick myofilaments varied from 3:1 to 5:1 because thin filaments were shared by adjacent thick filaments. 相似文献
16.
The accessory muscle of the walking leg of the horseshoe crab, Tachypleus gigas, was examined electron microscopically. The muscle fibers vary in size but are small in diameter, when compared with other arthropod skeletal muscles. They are striated with A, I, Z and poorly defined H bands. The sarcomere length ranges from 3-10 μm with most sarcomeres in the range of about 6 μm. The myofilaments are arranged in lamellae in larger fibers and less well organized in the smaller ones. Each thick filament is surrounded by 9-12 thin filaments which overlap. The SR is sparse but well organized to form a fenestrated collar around the fibrils. Individual SR tubules are also seen among the myofibrils. Long transverse tubules extend inward from the sarcolemma to form dyads or triads with the SR at the A-I junction. Both dyads and triads coexist in a single muscle fiber, a feature believed to have evolutionary significance. The neuromuscular relationship is unique. In the region of synaptic contact, the sarcolemma is usually elevated to form a large club-shaped structure containing no myofilaments and few other organelles. The axons or axon terminals and glial elements penetrate deep into the club-shaped sarcoplasm and form synapses with the fiber. As many as 13 terminals have been observed within a single section. Synaptic vesicles of two types are found in the axon terminals. 相似文献
17.
OBLIQUELY STRIATED MUSCLE : IV. Sarcoplasmic Reticulum, Contractile Apparatus, and Endomysium of the Body Muscle of a Polychaete, Glycera, in Relation to Its Speed
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Jack Rosenbluth 《The Journal of cell biology》1968,36(1):245-259
Body muscle cells of the bloodworm Glycera, a polychaete annelid, were studied by electron microscopy and compared with muscle cells of the more slowly acting nematode Ascaris, which have been described previously. Both muscles are obliquely striated. The predominant type of bloodworm fiber is characterized by a prominent transversely oriented sarcoplasmic reticulum with numerous dyads at the surface of each cell. Thick myofilaments are ~3 µ long and overlap along ~60% of their length in extended fibers and ~80% in shortened fibers. There is virtually no endomysium and very little intracellular skeleton, and the cells are attached by desmosomes to one another rather than to connective tissue. Dense bodies are absent from the fibers and in their place are Z lines, which are truly linear rather than planar. Scattered among the predominant fibers are others, less orderly in arrangement, in which the SR is much less prominent and in which the thick filaments are thicker and longer and overlap to an even smaller degree. It is suggested that physiological differences between bloodworm and Ascaris muscles derive from differences in the proportion of series to parallel linkages between the contractile elements, differences in the amount and disposition of the SR, and differences in the impedance to shear within the myofibrils. 相似文献
18.
Jack Rosenbluth 《The Journal of cell biology》1965,25(3):495-515
The somatic musculature of the nematode, Ascaris, is currently thought to consist of smooth muscle fibers, which contain intracellular supporting fibrils arranged in a regular pattern. Electron microscopic examination shows that the muscle fibers are, in fact, comparable to the striated muscles of vertebrates in that they contain interdigitating arrays of thick and thin myofilaments which form H, A, and I bands. In the A bands each thick filament is surrounded by about 10 to 12 thin filaments. The earlier confusion about the classification of this muscle probably arose from the fact that in one longitudinal plane the myofilaments are markedly staggered and, as a result, the striations in that plane of section are not transverse but oblique, forming an angle of only about 6° with the filament axis. The apparent direction of the striations changes with the plane of the section and may vary all the way from radial to longitudinal. A three-dimensional model is proposed which accounts for the appearance of this muscle in various planes. Z lines as such are absent but are replaced by smaller, less orderly, counterpart "Z bundles" to which thin filaments attach. These bundles are closely associated with fibrillar dense bodies and with deep infoldings of the plasma membrane. The invaginations of the plasma membrane together with intracellular, flattened, membranous cisternae form dyads and triads. It is suggested that these complexes, which also occur at the cell surface, may constitute strategically located, low-impedance patches through which local currents are channeled selectively. 相似文献
19.
The presence of striated subumbrellar musculature in hydromedusae can be related to the development in hydrozoans of a free-swimming life stage. The detailed ultrastructure of the striated subumbrellar musculature of the anthomedusan, Pennaria tiarella is presented. The striated musculature of Pennaria resembles vertebrate striated muscle in filament arrangement (L2 lattice pattern) and M line structure. The striation pattern, out-of-register myofilaments, filament structure as determined by rotational symmetry, Z line structure, types of intercellular junctions, and sarcoplasmic reticulum are more similar to structures found in other invertebrate striated muscle. 相似文献
20.
Fine structure of the thick filament in molluscan catch muscle 总被引:4,自引:0,他引:4
Y Nonomura 《Journal of molecular biology》1974,88(2):445-455