Assembly of transverse tubule architecture in the middle and myotendinous junctional regions in developing rat skeletal muscle fibers
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Sarcolemma
Tubule
Skeletal Muscle Fibers
Maintaining viability in cardiac myocytes isolated from adult rats using collagenase is difficult in Ca-containing media due to cell damage that occurs on reintroduction of Ca after perfusing the heart with the Ca-free medium needed to isolate myocytes with collagenase. Recently it has been proposed that Ca-free perfusion of isolated rabbit interventricular septa leads to cellular Na overload which, on reintroducing Ca, produces influx of toxic concentrations of Ca due to the Na/Ca exchange mechanism in the sarcolemma. We have found that replacing a portion of the 118 mM NaCl in the Ca-free perfusion medium with 69 mM LiCl dramatically increased the proportion of Ca-tolerant cardiac myocytes isolated from adult male rats with collagenase. Myocyte viability was maintained over a four hour period of incubation at 37 degrees C in 1 mM Ca.
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Cardiac myocyte
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The membrane systems of hamster general atrial and ventricular myocytes were studied and their reactivity with the sterol probes, filipin and tomatine, compared with that of atrioventricular nodal myocytes. The sarcolemma of atrial and atrioventricular nodal myocytes was considerably more reactive to sterol probes than the sarcolemma of general ventricular myocytes. Atrial myocyte sarcolemma was also more reactive than previously reported in rat atrial myocytes. Particle-free regions of annular nexuses were consistently unreactive with all combinations of sterol probes whereas much smaller particle-free regions of macular nexuses and desmosomes were reactive with the same probes. Intracellular membrane systems of all three types of cardiac myocyte reacted in a similar manner with sterol probes. These results indicate variation in comparable sarcolemma composition of cardiac myocytes between the rat and hamster and between cardiac regions within the same species.
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Filipin
Mesocricetus
Atrial myocytes
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Myofilament
Sarcolemma
Myofibril
Embryonic heart
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Skeletal Muscle Fibers
Calcium in biology
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A new method has been developed for mechanically disrupting the sarcolemma of mammalian sketletal muscle fibers (sarcolemma nonfunctional). Single fibers were produced from small pieces of the soleus muscle of the rabbit by gentle homogenization in a relaxing solution in a tissue homogenizer. These fibers were found to be longitudinally intact, with a sarcomere spacing of approximately 2.1 mum, permeable to large molecules of 10,000 MW, sensitive to the chemical stimuli that cause Ca2+ to be released from the sarcoplasmic reticulum, and responsive to Ca2+ in the same manner as frog fibers skinned in the traditional manner. The single fibers were mounted in a tension transducer and steady-state tensions were recorded in test solutions of different Ca2+ concentrations. The data did not differ statistically from data similarly obtained in identically prepared fibers that, in addition, we had longitudinally split in half to ensure disruption of the sarcolemmal barrier to the diffusion of ions.
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Skeletal Muscle Fibers
Homogenization
Myofibril
Cardiac muscle
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Sarcolemma
Skeletal Muscle Fibers
Line (geometry)
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Sarcolemma
Skeletal Muscle Fibers
Muscle fibre
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Abstract Human muscle is a hierarchically organised tissue with its contractile cells called myofibers packed into large myofiber bundles. Each myofiber contains periodic myofibrils built by hundreds of contractile sarcomeres that generate large mechanical forces. To better understand the mechanisms that coordinate human muscle morphogenesis from tissue to molecular scales, we adopted a simple in vitro system using induced pluripotent stem cell-derived human myogenic precursors. When grown on an unrestricted two-dimensional substrate, developing myofibers spontaneously align and self-organise into higher-order myofiber bundles, which grow and consolidate to stable sizes. Following a transcriptional boost of sarcomeric components, myofibrils assemble into chains of periodic sarcomeres that emerge across the entire myofiber. By directly probing tension we found that tension build-up precedes sarcomere assembly and increases within each assembling myofibril. Furthermore, we found that myofiber ends stably attach to other myofibers using integrin-based attachments and thus myofiber bundling coincides with stable myofiber bundle attachment in vitro . A failure in stable myofiber attachment results in a collapse of the myofibrils. Overall, our results strongly suggest that mechanical tension across sarcomeric components as well as between differentiating myofibers is key to coordinate the multi-scale self-organisation of muscle morphogenesis.
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Myofibril
Cardiac muscle
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Antibodies previously described to inhibit specifically nucleotide transport (ADP-ATP carrier) of the inner mitochondrial membrane were found to bind specifically to the sarcolemma of the enzymatically isolated rat ventricular myocytes. In this communication, we report for the first time that a component of these antibodies enhanced the Ca2+ current in isolated cardiac myocytes and potentiated twitch tension in ventricular strips. Prolonged exposure of rat myocytes to large concentrations of antibodies caused spontaneous contractions, progressive cell deterioration, and death. Our results thus show that a component of antibodies against ADP-ATP carrier cross-reacts with cardiac sarcolemmal proteins enhancing the Ca2+ channel.
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Cardiac myocyte
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