Histochemical characteristics of a tonic smooth muscle (original) (raw)
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Journal of Fish Biology, 1983
In myotomes of the stickleback three main complexes of muscle fibres were present. They comprised dwarf, intermediate and white fibres, which differed in regard to histochemical, immunohistochemical and ultrastructural features. In addition, dwarf fibres were divided into two categories on the basis of myofibrillar ATPase activity and cross-reactions with specific antisera. Among intermediate muscle fibres it was possible to observe some ' aberrant fibres ', which were characterized by low reactivity with anti P-myosin serum. 303 0022-1 I12/83/030303+ I4 $03.00/0 0 1983 The Fisheries Society of the British Isles
The Journal of experimental zoology, 1992
The superficial flexor muscle in the abdomen of the Norway lobster Nephrops norvegicus (L.), comprises medial and lateral bundles with distinct fiber type composition. Fibers of the medial bundle have long sarcomeres (> 9 microns) and a thick fringe of subsarcolemmal mitochondria. In histochemical tests they have a low total myofibrillar ATPase activity, a pH-stable isoform of myosin ATPase, and a high level of oxidative enzyme activity. A few fibers of the lateral bundle also display these morphological and histochemical properties. However, the majority of lateral fibers have shorter sarcomeres (< 8 microns), no subsarcolemmal mitochondria, but a well-developed tubular system. They also have a higher total myofibrillar ATPase activity, a pH-labile isoform of myosin ATPase, and a low level of oxidative enzyme activity. The heterogeneous pattern of different fiber types in the lateral bundle of this muscle is similar but not identical in the different abdominal segments and in...
The Histochemical Journal, 1989
Intensities of histochemical and immunohistochemical reactions in muscle fibres of Rana and Xenopus have been estimated microphotometrically, and the data from serial sections statistically analysed. Quantitative validities of reactions and measurements have also been assessed against independent published evidence. It is concluded that NADH-tetrazolium reductase overestimates tonic-fibre aerobic capacities and the actomyosin ATPase reaction overestimates their contraction speeds. However, it appears that succinate dehydrogenase, despite being a near-equilibrium enzyme of particulate distribution, indicates the relative aerobic capacities of fibres with acceptable accuracy when lightly reacted. Capacities for aerobic and anaerobic metabolism are positively correlated over all types of fibre (r typically-0.6 for 200 fibres), perhaps as an adaptation to environmental hypoxia. Multivariate clusters (indicating fibre types) have been sought, using Ward's method with optimizing procedures (iterative relocation and multivariate-normal modelling). Cluster analysis confirms the subjective identifications of two 'slow/tonic' types in Xenopus (labelled T5 and $4) but of only one (T5) in Rana. Division of the 'fast family' twitch fibres into three types (F1 F3) in both genera, with metabolic capacity related inversely to apparent shortening velocity, is highly supportable by objective criteria. However, statistically significant subdivisions also present themselves. Rana F2 and Xenopus F1 clusters can be bisected according to metabolic capacity; and Xenopus F2 fibres fall into three subtypes reflecting different isomyosin contents. In the different types of twitch fibre, ratios of myofibrillar ATP consumption rate to aerobic capacity increase up to 30-fold with contraction speed, but anaerobic/aerobic ratios do so only 5-fold.
Tissue and Cell, 2008
The aim of this work was to gain insights into the mechanism of muscle differentiation and growth in Pagellus bogaraveo, by studying muscle fibre phenotypes identified by immunohistochemistry. At hatching, several layers of deep fast-white fibres were covered by a superficial fibre monolayer. At 5 days, slow-red fibres appeared near the lateral line nerve. At 40 days, the intermediate-pink muscle became visible, and in the slow-red and fast-white muscle layers transitions from larval myosin isoforms to the isoforms typical of adult muscle occurred. Between 70 and 100 days, small fibres with a distinct ATPase profile appeared throughout the fast-white muscle, marking the onset of "mosaic" hyperplasia. The myosin of the original superficial monolayer fibres underwent two myosin transformations, before being slowly replaced by an adult slow-red isoform. In juveniles and adults, the slow-red muscle layer could be resolved into two distinct types. The analysis of fibre phenotypes indicated that post-larval muscle growth occurred by two distinct stages of hyperplasia. This study offers a basis for further comparative and experimental studies with this economically relevant species, namely for identifying factors influencing its muscle growth dynamics and disclosing underlying mechanisms.
The Comparative Study of Myofibrillar Proteins of Skeletal Muscles of Some Deep-Sea Fish Species
Journal of FisheriesSciences.com, 2017
Comparative characteristics, common and distinctive features of qualitative and quantitative composition of myofibril proteins of skeletal muscles of some deep-sea fish species (Podonema longipes, Coryphaenoides cinereus, Coryphaenoides pectoralis) have been determined. Myofibrillar proteins were extracted from the skeletal muscle of three species deep-sea fish and their relative molecular mass was estimated by SDS/polyacrylamide gel electrophoresis. Subunit and quantitative compositions of deep-sea fish proteins were determined. The molecular weight of predominant contractile proteins, myosin (with heavy chains and two light chains), actin, troponin and tropomyosin was about 492, 47, 38 and 35 kDa, respectively for all fish species. The myosin/actin ratios were determined to be 2.85, 2.76 and 2.56 respectively for C. cinereus, P. longipes, and C. pectoralis. The Ca 2+-ATPase activity of C. cinereus and P. longipes actomyosins was significantly higher at low ionic strengths (0.317 and 0.324 µМ P i mg-1 min-1 accordingly) than at high ionic strengths (0.257 and 0.221 µМ P i mg-1 min-1 accordingly). At the same time the Mg 2+-ATPase activity value remained almost constant at both high and low ionic strengths (0.169-0.178 µМ P i mg-1 min-1). The Ca 2+-ATPase activity of C. cinereus, P. longipes and C. pectoralis myosins was 0.534, 0.641 and 0.376 µМ P i mg-1 min-1 respectively.
The Anatomical Record, 1984
The muscle fibers of the cranial slip of M. pectoralis pars thoracica of an emu @romaius novaehollandiae) were studied histochemically for intracellular lipid, succinic dehydrogenase, myofibrillar adenosine triphosphatase, and acetylcholinesterase. It was concluded that the muscle consisted of approximately 28% slow-tonic and 72% fast-twitch glycolytic fibers. The tonic fibers were considered to be characteristic of a postural muscle, and the fasttwitch glycolytic fibers to reflect the inability of the muscle to engage in sustained activity. The general absence of slow-tonic fibers from the pectoralis of other avian species so far studied may be attributed to inadequate sampling of the deeper regions of the muscle.
A histochemical and enzymatic study of the muscle fiber types in the water monitor, Varanus salvator
Journal of Experimental Zoology, 1983
Histochemical analysis of five muscles from the water monitor, Varanus saluator, identified three major classes of fibers based on histochemical activities of the enzymes myosin ATPase (mATPase), succinic dehydrogenase (SDH), and a-glycerophosphate dehydrogenase (aGPDH). Fasttwitch, glycolytic (FG) fibers were the most abundant fiber type and exhibited the following reaction product intensities: mATPase, dark; SDH, light; aGPDH, moderate to dark. Fast-twitch, oxidative, glycolytic (FOG) fibers were characteristically mATPase, dark; SDH, light; aGPDH, moderate to dark. The third class of fibers had the following histochemical characteristics: mATPase, light; SDH, moderate to dark; aGPDH, light. These fibers were considered to be either slow twitch, or tonic, and oxidative (S/O). Pyruvate kinase (PK), aGPDH, and citrate synthase (CS) activities were measured in homogenates of the same muscles studied histochemically. There was a positive relationship between both PK and aGPDH activities and the percentage of glycolytic fiber types within a muscle. Likewise, CS activities were greater in muscles high in FOG and S/O content. Based on CS activities, Varanus S/O fibers were eight-fold more oxidative than FG fibers within the same muscle. PWCS ratios suggested that FG fibers possess high anaerobic capacity, similar to the iguanid lizard Dipsosaurus. The fiber type composition of the gastrocnemius muscle, relative to that of other lizard species, suggests that varanid lizards may possess a greater proportion of FOG and S/O fibers than other lizards. 0 1983 ALAN R. LISS, INC.
Journal of Fish Biology, 1991
Myofibrillar proteins in the myotomal muscle fibre types of two freshwater teleosts, Heferopneusfes fossilis (Bloch) and Labeo rohita (Hamilton), were investigated. The fibre types were identified histochemically based on the reactivities of the enzymes SDH and m-ATPase. Electrophoretic analysis revealed distribution patterns of myosin light chains, tropomyosin, troponin, c-and m-protein; specific to the muscle fibre types. The results correlate well with the general pattern of myofibrillar protein distribution found in the skeletal muscles of higher vertebrates. The significance of the present findings are discussed with regard to histochemical, biochemical as well as functional properties of the muscle fibre types.
Proceedings of the National Academy of Sciences, 1982
The giant smooth muscle fibers of a ctenophore were isolated by enzymatic digestion. These fibers are multinucleated cells, up to 50 ,um in diameter and 2 cm in length. Their ultrastructure and membrane electrical properties are similar to those of in situ fibers. Relaxed, coiled (partially contracted), and fully shortened states were distinguished in isolated cells and studied by scanning and transmission electron microscopy. Calciumcontaining mitochondrial granules were found in the coiled cells but not in either the relaxed or the fully shortened cells. The relaxed cell is characterized in cross section by the density of myosin filaments (457 ± 15 per jpm2) and the thin-to-thick filament ratio (5.2 ± 0.2). In the coiled cell, the muscle lattice does not expand uniformly, as shown by the variability of myosin spacing, and the thin-to-thick filament ratio decreases. Both clockwise and counterclockwise coiling occur along the same fiber. The implications of these findings with respect to the structure of the contractile apparatus are discussed.
Electrophoretic analyses of myofibrillar proteins from the body wall muscle of Ascaris suum
Molecular and Biochemical …, 1981
A myofibrillax protein extract has been isolated from the muscle ofAscaris suum. Two-dimensional electrophoresis of this extract revealed that the myosin light chain 1 (ALC !) migrates as 3 components with approximate isocieetfic points in the range of 5.3-5.6. The most acidic component of ALCI appeared to be phosphorylated when the myofibrillar extract was incubated for 10 s with catalytic subunit of cAMP-dependent protein kinase and [-r-32PIATP. The myosin light chain 2 (ALC 2) migrated as a single component in isoeleetric focusing with an approximate isoelectrie point of 5.5. Actin was resolved into 2 components with identical molecular weights but isoeleetric points differing by approximately 0.2 pH units. A protein was tentatively identified in the myofibriUar extract as tropomyosin. It migrated as a single band with an approximate isoelectfic point of 5.0 and a molecular weight of 39 000. None of the troponin components could be identified in the myofibrillar extract. It is postulated that muscle contraction in A. suum muscle could be controlled by phosphorylation of myosin.