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1
Savolainen, J., and M. Vornanen. "Parvalbumin content in striated muscles of the common shrew (Sorex araneus)." Canadian Journal of Zoology 76, no. 12 (1998): 2194–99. http://dx.doi.org/10.1139/z98-160.
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The parvalbumin content of mammalian muscles correlates positively with isometric relaxation rate and fiber type IIB frequency of the muscles but negatively with animal size. Since shrews are small-bodied animals with a relatively low number of type IIB fibers, it is of some interest to know how the parvalbumin content of shrew muscle correlates with the above factors. Parvalbumin content in heart, diaphragm, and gastrocnemius muscle of the common shrew, mouse, and rat was determined electrophoretically. Parvalbumin was not found in heart muscle of any species. Shrew diaphragm (0.29 ± 0.04 g/kg) had significantly less parvalbumin than mouse (0.63 ± 0.11 g/kg) or rat (0.54 ± 0.09 g/kg) diaphragm. Similarly, the parvalbumin content of shrew gastrocnemius muscle (0.28 ± 0.04 g/kg) was significantly lower than in that of mouse (2.88 ± 0.38 g/kg) or rat (0.96 ± 0.25 g/kg) gastrocnemius muscle. The isometric twitch of the gastrocnemius muscle was somewhat faster than the twitch of the diaphragm in all three species. The isometric contractions of shrew and mouse skeletal muscles were generally very similar in duration, with the exception of the relaxation time of the gastrocnemius muscle, which was shorter in the mouse. Diaphragm and gastrocnemius muscle of the rat were clearly slower than the respective muscles in the mouse or shrew with regard to both the contraction and relaxation phases. The half-relaxation time of isometric contractions correlated relatively weakly with parvalbumin content of the muscles (r = 0.40) but more strongly with their fiber IIB content (r = 0.81). The unexpectedly low parvalbumin content and relatively slow rate of contraction in shrew skeletal muscles are attributed to the exceptional fiber type composition, i.e., a high proportion of type IID fibers.
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Cohen, Glenn M., and Margaret F. Scott. "Effects of Co60 Irradiation on Muscle Fiber Types of the Grass Frog." Microscopy and Microanalysis 6, S2 (2000): 852–53. http://dx.doi.org/10.1017/s1431927600036758.
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Striated skeletal muscle has been considered radioresistant because it is highly differentiated and post-mitotic. Striated muscle does, however, respond to irradiation with morphological and biochemical changes after short and long latency periods; vascular and/or neurological impairments might contribute to the delayed responses to irradiation.The objective of the present study was to determine the susceptibility of three amphibian muscle fiber types to Co60 irradiation. In amphibians, the three major fiber types are 1) large twitch fibers, which contain low levels of mitochondrial enzymes and lipids, but intermediate levels of glycogen; 2) small twitch fibers, which contain high levels of both glycolytic and mitochondrial enzymes (FIG. 1); and tonic fibers, which contain low levels of all three histochemical markers. Thus, the determination of susceptibility of different amphibian fiber types to irradiation might indicate whether the metabolic characteristics of the fibers, rather than morphological or electrical properties, could serve as an early indicator of radiation damage.
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Marini, Gabriela, Angélica M. Pascon Barbosa, Débora C. Damasceno, et al. "Morphological changes in the fast vs slow fiber profiles of the urethras of diabetic pregnant rats." Urogynaecologia 25, no. 1 (2011): 9. http://dx.doi.org/10.4081/uij.2011.e9.
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<em>Background</em>. This study was undertaken to test the hypothesis that diabetes and pregnancy detrimentally affect the normal function of urethral striated muscles in rats, providing a model for additional studies related to urinary incontinence. The aim of this study was to evaluate morphological alterations in the urethral striated muscles of diabetic pregnant rats. <em>Design and methods. </em>Twenty female Wistar rats were distributed into four experimental groups of five rats as follows: virgin, pregnant, diabetic virgin, and diabetic pregnant. Diabetes was induced using streptozotocin administration (40 mg/kg i.v.). The rats were lethally anesthetized, and the urethra and vagina were extracted as a unit. Cryostat sections (6 µm thick) were cut and stained with hematoxylin-eosin, and immunohistochemical procedures were performed and subjected to morphological and semi quantitative analysis. <em>Results</em>. The urethral striated muscle from the diabetic pregnant rats presented with the following variations: thinning and atrophy, disorganization and disruption associated with the colocalization of fast and slow fibers and a steady decrease in the proportion of fast <em>vs</em> slow fibers. <em>Conclusion</em>. Diabetes and pregnancy impair the urethral striated muscle and alter its fiber type distribution.
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Tavernier, Benoit M., Elie Haddad, Pascal J. Adnet, Toussaint S. Etchrivi, Dominique Lacroix, and Hugo Reyford. "Isoform-dependent Effects of Halothane in Human Skinned Striated Fibers." Anesthesiology 84, no. 5 (1996): 1138–47. http://dx.doi.org/10.1097/00000542-199605000-00016.
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Background Reports of the effects of halothane on isoform contractile proteins of striated muscles are conflicting. To determine whether halothane affects cardiac and skeletal contractile proteins differently, the authors examined the effects of two doses of halothane (0.44 and 1.26 mM, equivalent to 0.75 and 2.25 vol%, respectively) on the Ca++ sensitivity and maximal force in human skinned cardiac, type I (slow twitch), and type II (fast twitch) skeletal muscle fibers. Methods Left ventricular muscle strips and skeletal muscle biopsy specimens were obtained from eight and ten patients undergoing cardiac and orthopedic surgery, respectively. Sarcolemma and sarcoplasmic reticulum were destroyed with ethylene glycol bis (beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid plus Brij 58. Ca++ sensitivity was studied by observing the isometric tension developed by skinned fibers challenged with increasing concentrations of Ca++. Muscle fiber type was determined in each skeletal fiber by the difference in strontium-induced tension measurements. Results Halothane shifted the Ca++ tension curves toward higher Ca++ concentrations and increased the Ca++ concentrations for half-maximal activation in both cardiac and type I skeletal muscle fibers (from 1.96 microM and 1.06 microM under control conditions to 2.92 microM and 1.71 microM in presence of 0.75 vol% halothane, respectively) without changing the slope of this relationship (Hill coefficient). In contrast, no significant effect was observed in type II fibers. Halothane also decreased the maximal activated tension in the three groups of fibers with a lesser effect in type II fibers. Conclusions Halothane decreases Ca++ sensitivity and maximal force in human skinned cardiac and type I fibers at 20 degrees C. It is concluded that the negative inotropic effects of halothane depend on contractile proteins isoforms.
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Lee, Seok-Beom. "Histomorphometry on Regenerated Muscle Fiber in the Damaged Striated Muscle." Ewha Medical Journal 18, no. 1 (1995): 45. http://dx.doi.org/10.12771/emj.1995.18.1.45.
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Briggs, Margaret M., and Fred Schachat. "The superfast extraocular myosin (MYH13) is localized to the innervation zone in both the global and orbital layers of rabbit extraocular muscle." Journal of Experimental Biology 205, no. 20 (2002): 3133–42. http://dx.doi.org/10.1242/jeb.205.20.3133.
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SUMMARY Extraocular muscles (EOMs) are the most molecularly heterogeneous and physiologically diverse mammalian striated muscles. They express the entire array of striated muscle myosins, including a specialized myosin heavy chain MYH13, which is restricted to extraocular and laryngeal muscles. EOMs also exhibit a breadth of contractile activity, from superfast saccades to slow tracking and convergence movements. These movements are accomplished by the action of six ultrastructurally defined fiber types that differ from the type IIa, IIb, IIx and I fibers found in other skeletal muscles. Attempts to associate different eye movements with either the expression of different myosins or the activity of particular EOM fiber types are complicated by the molecular heterogeneity of several of the fiber types, and by electromyography studies showing that the majority of extraocular motor units participate in both fast and slow eye movements. To better understand the role of MYH13 in ocular motility, we generated MYH13-sequence-specific antibodies and used SDS-PAGE to quantify the regional distribution of myosin in EOM and to characterize its heterogeneity in single fibers. These studies demonstrate that MYH13 is preferentially expressed in the majority of orbital and global fibers in the central innervation zone of rabbit EOM. Many individual fibers express MYH13 with the fast IIb myosin and varying amounts of IIx myosin. The differential localization of MYH13, coupled with specialization of the sarcoplasmic reticulum and thin filament systems, probably explains how activation of the endplate band region enables the majority of EOM fibers to contribute to superfast contractions.
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Grove, B. K., L. Cerny, J. C. Perriard, H. M. Eppenberger, and L. E. Thornell. "Fiber type-specific distribution of M-band proteins in chicken muscle." Journal of Histochemistry & Cytochemistry 37, no. 4 (1989): 447–54. http://dx.doi.org/10.1177/37.4.2926123.
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The functions of two myofibrillar proteins, myomesin (Mr 185,000) and M-protein (Mr 165,000), associated with the M-band are as yet unknown. To extend our knowledge of these proteins, we have examined chicken striated muscles with fast and slow contractile properties, e.g., pectoralis major, PLD, ALD, medial adductor, and lateral adductor, to determine the expression and isoform composition of myomesin and M-protein in various muscles and fiber types. The high molecular weight M-band proteins were characterized and quantitated using monoclonal antibodies in immunoblotting and double-antibody sandwich ELISA. Fiber specificity was determined by immuno- and enzyme histochemistry. In addition to the previously reported Mr 195,000 and 190,000 isoforms of myomesin in heart [Grove et al. (1985): J Cell Biol 101:1431], the Mr 185,000 myomesin in skeletal muscles may represent different isoforms in fast and slow muscles on the basis of distinctive degradation patterns. M-protein has the same molecular weight in striated chicken muscles and degradation patterns indicate only one isoform. The low quantities of M-protein in slow muscles were shown to be due to the absence of M-protein in two of the generally recognized slow fiber types, types I and III. Thus, M-protein was present only in fast type II fibers, whereas myomesin was ubiquitous in all fiber types. Whatever the causal relationship, M-protein appears to function in fast motor units composed of type II fibers.
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Cooke, R. "Actomyosin interaction in striated muscle." Physiological Reviews 77, no. 3 (1997): 671–97. http://dx.doi.org/10.1152/physrev.1997.77.3.671.
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The mechanics of the actomyosin interaction have been extensively studied using the organized filament array of striated muscle. However, the extrapolation of these data to the events occurring at the level of a single actomyosin interaction has not been simple. Problems arise in part because an active fiber has an ensemble of myosin heads that are spread out through the various steps of the active cycle, and it is likely that only a small fraction of the heads are generating tension at any given time. More recently, two new approaches have greatly extended our knowledge of the actomyosin interaction. First, the three-dimensional crystal structures of both the actin monomer and the myosin head have been determined, and these structures have been fit to lower resolution images to give atomic models of the actin filament and of the actin filament decorated by myosin heads. Second, the technology to measure picoNewton forces and nanometer distances has provided direct determinations of the force and step length generated by a single myosin molecule interacting with a single actin filament. This review synthesizes the existing mechanical data obtained from the more-organized array of the muscle filament with the results obtained by these two technologies.
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Rall, Jack A. "What makes skeletal muscle striated? Discoveries in the endosarcomeric and exosarcomeric cytoskeleton." Advances in Physiology Education 42, no. 4 (2018): 672–84. http://dx.doi.org/10.1152/advan.00152.2018.
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One of the most iconic images in biology is the cross-striated appearance of a skeletal muscle fiber. The repeating band pattern shows that all of the sarcomeres are the same length. All of the A bands are the same length and are located in the middle of the sarcomeres. Furthermore, all of the myofibrils are transversely aligned across the muscle fiber. It has been known for 300 yr that skeletal muscle is striated, but only in the last 40 yr has a molecular understanding of the striations emerged. In the 1950s it was discovered that the extraction of myosin from myofibrils abolished the A bands, and the myofibrils were no longer striated. With the further extraction of actin, only the Z disks remained. Strangely, the sarcomere length did not change, and these “ghost” myofibrils still exhibited elastic behavior. The breakthrough came in the 1970s with the discovery of the gigantic protein titin. Titin, an elastic protein ~1 µm in length, runs from the Z disk to the middle of the A band and ensures that each sarcomere is the same length. Titin anchors the A band in the middle of the sarcomere and may determine thick-filament length and thus A-band length. In the 1970s it was proposed that the intermediate filament desmin, which surrounds the Z disks, connects adjacent myofibrils, resulting in the striated appearance of a skeletal muscle fiber.
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Elhanany-Tamir, Hadas, Yanxun V. Yu, Miri Shnayder, Ankit Jain, Michael Welte, and Talila Volk. "Organelle positioning in muscles requires cooperation between two KASH proteins and microtubules." Journal of Cell Biology 198, no. 5 (2012): 833–46. http://dx.doi.org/10.1083/jcb.201204102.
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Striated muscle fibers are characterized by their tightly organized cytoplasm. Here, we show that the Drosophila melanogaster KASH proteins Klarsicht (Klar) and MSP-300 cooperate in promoting even myonuclear spacing by mediating a tight link between a newly discovered MSP-300 nuclear ring and a polarized network of astral microtubules (aMTs). In either klar or msp-300ΔKASH, or in klar and msp-300 double heterozygous mutants, the MSP-300 nuclear ring and the aMTs retracted from the nuclear envelope, abrogating this even nuclear spacing. Anchoring of the myonuclei to the core acto-myosin fibrillar compartment was mediated exclusively by MSP-300. This protein was also essential for promoting even distribution of the mitochondria and ER within the muscle fiber. Larval locomotion is impaired in both msp-300 and klar mutants, and the klar mutants were rescued by muscle-specific expression of Klar. Thus, our results describe a novel mechanism of nuclear spacing in striated muscles controlled by the cooperative activity of MSP-300, Klar, and astral MTs, and demonstrate its physiological significance.
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Bennett, R. A., R. N. Pittman, and S. M. Sullivan. "Capillary spatial pattern and muscle fiber geometry in three hamster striated muscles." American Journal of Physiology-Heart and Circulatory Physiology 260, no. 2 (1991): H579—H585. http://dx.doi.org/10.1152/ajpheart.1991.260.2.h579.
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Since most oxygen exchange in muscle is thought to occur by diffusion across the walls of capillaries, it is important to determine the spatial relationship between capillaries and muscle fibers. We have extended the work of Kayar et al. (Microvasc. Res 24: 326-341, 1982) to include other statistical tests that allow one to make stronger statements regarding the spatial pattern. Data for hamsters were obtained from two sartorius, three retractor, and five soleus muscle sections. Distances between all pairs of capillaries, distances between a capillary and its first nearest neighbor for all capillaries, and distances between random tissue sample points and the closest capillary were used to test the spatial arrangement of capillaries. The null hypothesis tested of complete spatial randomness of capillary locations was rejected in favor of a regular alternative in one each of the sartorius and retractor fields and in all five soleus fields. We formulated a geometric model, composed of a space-filling array of identical hexagonal muscle fibers with capillaries placed randomly at the juncture of three fibers or between two fibers, according to the observed relative probability of those occurrences. The model simulations of muscle fibers and capillaries were then analyzed by the same statistical tests used on the histological sections. The findings were similar in both cases, providing confidence that the assumptions of the model were sufficient approximations. The results of this study provide a basis for the placement of capillaries around muscle fibers in mathematical models of oxygen transport in capillary networks.
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Volk, Talila. "Positioning nuclei within the cytoplasm of striated muscle fiber." Nucleus 4, no. 1 (2013): 18–22. http://dx.doi.org/10.4161/nucl.23086.
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D'souza, Donna, Ruanne Y. J. Lai, Michael Shuen, and David A. Hood. "mRNA stability as a function of striated muscle oxidative capacity." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 303, no. 4 (2012): R408—R417. http://dx.doi.org/10.1152/ajpregu.00085.2012.
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A change in mRNA stability alters the abundance of mRNA available for translation and is emerging as a critical pathway influencing gene expression. Variations in the stability of functional and regulatory mitochondrial proteins may contribute to the divergent mitochondrial densities observed in striated muscle. Thus we hypothesized that the stability of mRNAs encoding for regulatory nuclear and mitochondrial transcription factors would be inversely proportional to muscle oxidative capacity and would be facilitated by the activity of RNA binding proteins (RBPs). The stability of mitochondrial transcription factor A (Tfam), peroxisome proliferator-activated receptor gamma coactivator 1α (PGC-1α), and nuclear respiratory factor 2α (NRF-2α) mRNA was assessed in striated muscles with distinct oxidative capacities using in vitro decay assays. All three mitochondrial regulators were rapidly degraded in cardiac and slow-twitch red (STR) muscle, resulting in a ∼60–65% lower ( P < 0.05) mRNA half-life ( t1/2) compared with fast-twitch white (FTW) fibers. This accelerated rate of Tfam mRNA decay was matched by a 2.5-fold increase in Tfam transcription in slow- compared with fast-twitch muscle ( P = 0.05). Protein expression of four unique RBPs [AU-rich binding factor 1 (AUF1), human antigen R (HuR), KH-homology splicing regulatory protein (KSRP), and CUG binding protein 1 (CUGBP1)] believed to modulate mRNA stability was elevated in cardiac and STR muscles ( P < 0.05) and was moderately associated with the decay of Tfam, PGC-1α, and NRF-2α mRNA. Variable rates of transcript degradation were apparent when comparing all transcripts within the same muscle type. Thus the distribution of RBPs appears to follow a fiber-type specific pattern and subsequently functions to alter the stability of specific mitochondrial regulators in a transcript- and tissue-specific fashion.
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Collins, Teresa, Josephine E. Joya, Ruth M. Arkell, Vicki Ferguson та Edna C. Hardeman. "Reappearance of the minor α-sarcomeric actins in postnatal muscle". American Journal of Physiology-Cell Physiology 273, № 6 (1997): C1801—C1810. http://dx.doi.org/10.1152/ajpcell.1997.273.6.c1801.
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The postnatal expression profiles of α-sarcomeric actin transcripts and protein are quantified in mouse striated muscles from birth to postnatal day 56 by Northern and Western blot analyses. α-Cardiac actin (α-CA) transcripts transiently increase between 12 and 21 days after birth in the quadriceps muscle, reaching ∼90% that found in the adult mouse heart. Although α-CA is the α-sarcomeric actin isoform expressed in the immature fiber, the expression profiles of other contractile protein isoforms indicate that this postnatal period is not reflective of an immature phenotype. α-Skeletal actin (α-SA) transcripts accumulate to ∼32% of the total α-sarcomeric actin transcripts in the adult heart. Our study shows that 1) there is a simultaneous reappearance of α-CA and α-SA in postnatal skeletal and heart muscles, respectively, and 2) the contractile protein gene expression profile characteristic of adult skeletal muscle is not achieved until after 42 days postnatal in the mouse. We propose there is a previously uncharacterized period of postnatal striated muscle maturation marked by the reappearance of the minor α-sarcomeric actins.
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Krafsur, G., E. J. Ehrhart, J. Ramos-Vara, et al. "Histomorphologic and Immunohistochemical Characterization of a Cardiac Purkinjeoma in a Bearded Seal (Erignathus barbatus)." Case Reports in Veterinary Medicine 2014 (2014): 1–4. http://dx.doi.org/10.1155/2014/103279.
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The most common cardiac tumors of heart muscle are rhabdomyomas, solitary or multiple benign tumors of striated muscle origin. While cardiac rhabdomyomas are well described in human medical literature, limited information depicting the occurrence of cardiac rhabdomyomas in veterinary species exists. A case of multiple firm white nonencapsulated nodules in the heart of a bearded seal is described. Microscopic findings included cytoplasmic vacuolization with formation of spider cells, glycogen vacuoles, and striated myofibrils. These cells expressed immunoreactivity for neuron-specific enolase and protein gene product 9.5, a marker for neuronal tissue and Purkinje fiber cells. Immunoreactivity for protein gene product 9.5 along with other microscopic findings substantiates Purkinje fiber cell origin of the cardiac rhabdomyoma in the bearded seal and use of the termpurkinjeomato describe this lesion.
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Schulze, Stacey L., Susan K. Danielson, John S. Rhee, Robert J. Toohill, Judith I. Kulpa, and Safwan S. Jaradeh. "Morphology of the Cricopharyngeal Muscle in Zenker and Control Specimens." Annals of Otology, Rhinology & Laryngology 111, no. 7 (2002): 573–78. http://dx.doi.org/10.1177/000348940211100702.
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The cricopharyngeal muscle (CPM) is essential for normal deglutition. Pharyngeal dysphagia commonly results from impaired or uncoordinated CPM dilation. Dysfunction of the CPM has also been implicated in the genesis of Zenker's (pharyngoesophageal) diverticulum. Despite the CPM's significance, little is understood about its morphology. We studied CPM biopsy specimens from 20 patients with Zenker's diverticulum and from 5 fresh cadaver patients with detailed histologic techniques to include fiber size and shape and adenosine triphosphatase, reduced nicotinamide adenine dinucleotide, trichrome, succinate dehydrogenase, cytochrome C oxidase, periodic acid-Schiff reaction, oil red O, acid phosphatase, Congo red, crystal violet, and monoadenylate deaminase stains. The normal CPM has unique morphological characteristics, with some myofibers having staining properties that are a hybrid between striated muscle and muscle spindle. The variable orientation of the muscle fibers is also different from that of most other striated musculature. Of the 20 Zenker CPM specimens, 4 specimens did not reveal any significant differences from controls (2 of which had insufficient amounts of tissue for complete analysis). In the remaining 16 specimens, several abnormalities existed, including excessive size variation (16/16), grouping of atrophic fibers (9/16), target or targetoid formations (4/16), cores (2/16), and ragged red fibers (2/16). The final pathological pattern of the 16 specimens was neurogenic in 7, myopathic in 4, and mixed (with neurogenic predominance) in the remaining 5. Two specimens contained significant lymphocytic inflammatory infiltrates. We conclude that the unique neuromuscular function of the CPM in deglutition is likely due to its fiber orientation and the hybrid nature of some of the myofibers. Morphological disturbances of the CPM impair its dilation and may account for the development of Zenker's diverticulum. This disturbance is most often due to progressive denervation of the CPM.
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Leary, S. C., C. N. Lyons, A. G. Rosenberger, J. S. Ballantyne, J. Stillman, and C. D. Moyes. "Fiber-type differences in muscle mitochondrial profiles." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 285, no. 4 (2003): R817—R826. http://dx.doi.org/10.1152/ajpregu.00058.2003.
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Although striated muscles differ in mitochondrial content, the extent of fiber-type specific mitochondrial specializations is not well known. To address this issue, we compared mitochondrial structural and functional properties in red muscle (RM), white muscle (WM), and cardiac muscle of rainbow trout. Overall preservation of the basic relationships between oxidative phosphorylation complexes among fiber types was confirmed by kinetic analyses, immunoblotting of native holoproteins, and spectroscopic measurements of cytochrome content. Fiber-type differences in mitochondrial properties were apparent when parameters were expressed per milligram mitochondrial protein. However, the differences diminished when expressed relative to cytochrome oxidase (COX), possibly a more meaningful denominator than mitochondrial protein. Expressed relative to COX, there were no differences in oxidative phosphorylation enzyme activities, pyruvate-based respiratory rates, H2O2 production, or state 4 proton leak respiration. These data suggest most mitochondrial qualitative properties are conserved across fiber types. However, there remained modest differences (∼50%) in stoichiometries of selected enzymes of the Krebs cycle, β-oxidation, and antioxidant enzymes. There were clear differences in membrane fluidity (RM > cardiac, WM) and proton conductance (H+/min/mV/U COX: WM > RM > cardiac). The pronounced differences in mitochondrial content between fiber types could be attributed to a combination of differences in myonuclear domain and modest effects on the expression of nuclear- and mitochondrially encoded respiratory genes. Collectively, these studies suggest constitutive pathways that transcend fiber types are primarily responsible for determining most quantitative and qualitative properties of mitochondria.
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Krier, J., T. Adams, and R. A. Meyer. "Physiological, morphological, and histochemical properties of cat external anal sphincter." American Journal of Physiology-Gastrointestinal and Liver Physiology 255, no. 6 (1988): G772—G778. http://dx.doi.org/10.1152/ajpgi.1988.255.6.g772.
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The contractile properties, morphology, and the distribution of striated muscle fiber types of the external and sphincter (EAS) were determined using axial force measurements, fiber size cross-sectional area measurements, and histochemistry. Electrical stimulation of motor axons in pudendal nerve at supramaximal intensities (10 V, 0.05 ms duration) elicited twitch contractions of EAS. The time to peak force after a single pulse ranged from 37 to 42 ms. The time for relaxation to half-maximal twitch force ranged from 20 to 29 ms. Repetitive stimulation of motor axons (0.1-3.0 Hz) produced potentiation and fatigue of single twitch contractile force, suggesting that the EAS of the cat is comprised predominantly of fast-twitch muscle fibers. Confirmation of skeletal muscle fiber types was determined by histochemistry. Frozen serial cross sections of EAS were incubated to demonstrate succinic dehydrogenase (SDH) and myosin adenosine triphosphatase after alkaline preincubation (pH 10.4). Based on these reactions, muscle fibers were classified as fast glycolytic (FG) (high ATPase, low SDH), fast oxidative-glycolytic (FOG) (high ATPase, high SDH), and slow oxidative (SO) (low ATPase, high SDH). The mean percentage +/- SE of each histochemical type was the following: FG, 73.5 +/- 3.9; FOG, 22.8 +/- 3.7; and SO, 3.7 +/- 0.6. These results indicate that the predominant fiber type for the EAS is FG. The EAS of the cat is considered a nominally fast-twitch muscle.
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O'Connell, Brett, Ronnie Blazev, and Gabriela M. M. Stephenson. "Electrophoretic and functional identification of two troponin C isoforms in toad skeletal muscle fibers." American Journal of Physiology-Cell Physiology 290, no. 2 (2006): C515—C523. http://dx.doi.org/10.1152/ajpcell.00307.2005.
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The differential sensitivity of frog twitch and slow-tonic fibers to Ca2+ and Sr2+ suggests that these two fiber types express different troponin C (TnC) isoforms. To date, only one TnC isoform from anurans (resembling the mammalian fast-twitch isoform) has been isolated and characterized. In this study, we examined the possibility that anuran striated muscle contains more than one TnC isoform. Toward this end, we determined the TnC isoform composition of 198 single fibers from the rectus abdominis of the cane toad (a mixed slow-tonic and twitch muscle) and of toad cardiac muscle using a method that enables the identification of TnC isoforms on the basis of the effect of Ca2+ on their electrophoretic mobility. The fibers were typed according to their myosin heavy chain (MHC) isoform composition. The data indicate that striated muscle of the cane toad contains two TnC isoforms, one of which (TnC-t) is present in all fibers displaying only twitch MHC isoforms and the other of which (TnC-T/c) is present in fibers displaying the tonic MHC isoform and in cardiac muscle. For a subpopulation of 15 fibers, the TnC isoform composition was also compared with Ca2+ and Sr2+ activation characteristics. Fibers containing the TnC-T/c isoform were ∼3-fold more sensitive to Ca2+, ∼40-fold more sensitive to Sr2+, and responded to a ∼4.6-fold broader range of [Ca2+] than did fibers containing the TnC-t isoform. The Ca2+ activation properties of toad fibers containing the TnC-T/c isoform appear to be consistent with the previously reported physiological characteristics of amphibian slow-tonic muscle fibers.
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Brown, Lisa D., George G. Rodney, Erick Hernández-Ochoa, Chris W. Ward, and Martin F. Schneider. "Ca2+ sparks and T tubule reorganization in dedifferentiating adult mouse skeletal muscle fibers." American Journal of Physiology-Cell Physiology 292, no. 3 (2007): C1156—C1166. http://dx.doi.org/10.1152/ajpcell.00397.2006.
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Ca+ sparks are rare in healthy adult mammalian skeletal muscle but may appear when adult fiber integrity is compromised, and occur in embryonic muscle but decline as the animal develops. Here we used cultured adult mouse flexor digitorum brevis muscle fibers to monitor occurrence of Ca2+ sparks during maintenance of adult fiber morphology and during eventual fiber morphological dedifferentiation after various times in culture. Fibers cultured for up to 3 days retain normal morphology and striated appearance. Ca2+ sparks were rare in these fibers. At 5–7 days in culture, many of the original muscle fibers exhibit sprouting and loss of striations, as well as the occurrence of spontaneous Ca2+ sparks. The average rate of occurrence of Ca2+ sparks is >10-fold higher after 5–7 days in culture than in days 1–3. With the use of fibers cultured for 7 days, application of the Ca2+ channel blockers Co2+ or nifedipine almost completely suppressed the occurrence of Ca2+ sparks, as previously shown in embryonic fibers, suggesting that Ca2+ sparks may be generated by similar mechanisms in dedifferentiating cultured adult fibers and in embryonic fibers before final differentiation. The sarcomeric disruption observed under transmitted light microscopy in dedifferentiating fibers was accompanied by morphological changes in the transverse (T) tubular system, as observed by fluorescence confocal imaging of both an extracellular marker dye and membrane staining dyes. Changes in T tubule morphology coincided with the appearance of Ca2+ sparks, suggesting that Ca2+ sparks may either be a signal for, or the result of, disruption of DHPR-ryanodine receptor 1 coupling.
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Lehti, T. Maarit, Mika Silvennoinen, Riikka Kivelä, Heikki Kainulainen, and Jyrki Komulainen. "Effects of streptozotocin-induced diabetes and physical training on gene expression of titin-based stretch-sensing complexes in mouse striated muscle." American Journal of Physiology-Endocrinology and Metabolism 292, no. 2 (2007): E533—E542. http://dx.doi.org/10.1152/ajpendo.00229.2006.
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In striated muscle, a sarcomeric noncontractile protein, titin, is proposed to form the backbone of the stress- and strain-sensing structures. We investigated the effects of diabetes, physical training, and their combination on the gene expression of proteins of putative titin stretch-sensing complexes in skeletal and cardiac muscle. Mice were divided into control (C), training (T), streptozotocin-induced diabetic (D), and diabetic training (DT) groups. Training groups performed for 1, 3, or 5 wk of endurance training on a motor-driven treadmill. Muscle samples from T and DT groups together with respective controls were collected 24 h after the last training session. Gene expression of calf muscles (soleus, gastrocnemius, and plantaris) and cardiac muscle were analyzed using microarray and quantitative PCR. Diabetes induced changes in mRNA expression of the proteins of titin stretch-sensing complexes in Z-disc (MLP, myostatin), I-band (CARP, Ankrd2), and M-line (titin kinase signaling). Training alleviated diabetes-induced changes in most affected mRNA levels in skeletal muscle but only one change in cardiac muscle. In conclusion, we showed diabetes-induced changes in mRNA levels of several fiber-type-biased proteins (MLP, myostatin, Ankrd2) in skeletal muscle. These results are consistent with previous observations of diabetes-induced atrophy leading to slower fiber type composition. The ability of exercise to alleviate diabetes-induced changes may indicate slower transition of fiber type.
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Connaughton, M. A., M. L. Fine, and M. H. Taylor. "The effects of seasonal hypertrophy and atrophy on fiber morphology, metabolic substrate concentration and sound characteristics of the weakfish sonic muscle." Journal of Experimental Biology 200, no. 18 (1997): 2449–57. http://dx.doi.org/10.1242/jeb.200.18.2449.
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Male weakfish Cynoscion regalis possess highly specialized, bilateral, striated sonic muscles used in sound production associated with courtship. Androgen-driven hypertrophy of the muscles during the late spring spawning period results in a tripling of sonic muscle mass followed by post-spawning atrophy. This study examined the morphological and biochemical changes underlying seasonal changes in sonic muscle mass and the functional effects of these on contraction as measured by sound production. Sonic muscle fiber cross-sectional area (CSA) increased significantly during the period of hypertrophy and then decreased by nearly 60%. Both the CSA of the contractile cylinder and that of the peripheral sarcoplasm decreased significantly by late summer, with the peripheral ring of sarcoplasm virtually disappearing. Muscle protein content followed a similar trend, suggesting a major loss of structural elements during atrophy. Muscle glycogen and lipid content decreased precipitously in early June during the period of maximal sound production. Sound pressure level increased and sound pulse duration decreased with increasing sonic muscle mass, indicating that sonic muscle fibers contract with greater force and shorter duration during the spawning season. Neither the pulse repetition rate nor the number of pulses varied seasonally or with muscle mass, suggesting that the effects of steroids on the acoustic variables are more pronounced peripherally than in the central nervous system. Seasonal sonic muscle hypertrophy, therefore, functions as a secondary sexual characteristic that maximizes vocalization amplitude during the spawning period.
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Petchey, Louisa K., Catherine A. Risebro, Joaquim M. Vieira, et al. "Loss ofProx1in striated muscle causes slow to fast skeletal muscle fiber conversion and dilated cardiomyopathy." Proceedings of the National Academy of Sciences 111, no. 26 (2014): 9515–20. http://dx.doi.org/10.1073/pnas.1406191111.
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Duncan, Diane, and Ivan Dinev. "Noninvasive Induction of Muscle Fiber Hypertrophy and Hyperplasia: Effects of High-Intensity Focused Electromagnetic Field Evaluated in an In-Vivo Porcine Model: A Pilot Study." Aesthetic Surgery Journal 40, no. 5 (2019): 568–74. http://dx.doi.org/10.1093/asj/sjz244.
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Abstract Background High-intensity focused electromagnetic (HIFEM) field technology has been reported to increase muscle thickness and hypertrophy. However, this process has not yet been confirmed on a histologic level. Objectives The aim of this study was to evaluate in-vivo structural changes in striated porcine muscle tissue following HIFEM treatment. Methods Three Yorkshire pigs received four 30-minute HIFEM treatments applied to the biceps femoris muscle on 1 side only. The fourth pig served as a control subject. At baseline and 2 weeks after the last treatment, biopsy specimens of the muscle tissue were collected from the treatment site. The control pig underwent muscle biopsy from a similar but untreated site. Twenty-five histology slides were evaluated from each pig. A certified histopathologist analyzed sliced biopsy samples for structural changes in the tissue. Results Histologic analysis showed hypertrophic changes 2 weeks posttreatment. The muscle mass density increased by 20.56% (to a mean of 17,053.4 [5617.9] µm2) compared with baseline. Similarly, muscle fiber density (hyperplasia) increased: the average change in the number of fibers in a slice area of 136,533.3 µm2 was +8.0%. The mean size of an individual muscle fiber increased by 12.15% (to 332.23 [280.2] µm2) 2 weeks posttreatment. Control samples did not show any significant change in fiber density or hyperplasia. Conclusions Histopathologic quantification showed significant structural muscle changes through a combination of fiber hypertrophy and hyperplasia. Control biopsies showed a lack of similar changes. The data correlate with findings of other HIFEM research and suggest that HIFEM could be used for noninvasive induction of muscle growth.
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Chun, Lois G., Christopher W. Ward, and Martin F. Schneider. "Ca2+ sparks are initiated by Ca2+ entry in embryonic mouse skeletal muscle and decrease in frequency postnatally." American Journal of Physiology-Cell Physiology 285, no. 3 (2003): C686—C697. http://dx.doi.org/10.1152/ajpcell.00072.2003.
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“Spontaneous” Ca2+ sparks and ryanodine receptor type 3 (RyR3) expression are readily detected in embryonic mammalian skeletal muscle but not in adult mammalian muscle, which rarely exhibits Ca2+ sparks and expresses predominantly RyR1. We have used confocal fluorescence imaging and systematic sampling of enzymatically dissociated single striated muscle fibers containing the Ca2+ indicator dye fluo 4 to show that the frequency of spontaneous Ca2+ sparks decreases dramatically from embryonic day 18 (E18) to postnatal day 14 (P14) in mouse diaphragm and from P1 to P14 in mouse extensor digitorum longus fibers. In contrast, the relative levels of RyR3 to RyR1 protein remained constant in diaphragm muscles from E18 to P14, indicating that changes in relative levels of RyR isoform expression did not cause the decline in Ca2+ spark frequency. E18 diaphragm fibers were used to investigate possible mechanisms underlying spark initiation in embryonic fibers. Spark frequency increased or decreased, respectively, when E18 diaphragm fibers were exposed to 8 or 0 mM Ca2+ in the extracellular Ringer solution, with no change in either the average resting fiber fluo 4 fluorescence or the average properties of the sparks. Either CoCl2 (5 mM) or nifedipine (30 μM) markedly decreased spark frequency in E18 diaphragm fibers. These results indicate that Ca2+ sparks may be triggered by locally elevated [Ca2+] due to Ca2+ influx via dihydropyridine receptor L-type Ca2+ channels in embryonic mammalian skeletal muscle.
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Kiss, András A., Nikoletta Somlyai-Popovics, Márton Kiss, Zsolt Boldogkői, Katalin Csiszár, and Mátyás Mink. "Type IV Collagen Is Essential for Proper Function of Integrin-Mediated Adhesion in Drosophila Muscle Fibers." International Journal of Molecular Sciences 20, no. 20 (2019): 5124. http://dx.doi.org/10.3390/ijms20205124.
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Congenital muscular dystrophy (CMD), a subgroup of myopathies is a genetically and clinically heterogeneous group of inherited muscle disorders and is characterized by progressive muscle weakness, fiber size variability, fibrosis, clustered necrotic fibers, and central myonuclei present in regenerating muscle. Type IV collagen (COL4A1) mutations have recently been identified in patients with intracerebral, vascular, renal, ophthalmologic pathologies and congenital muscular dystrophy, consistent with diagnoses of Walker–Warburg Syndrome or Muscle–Eye–Brain disease. Morphological characteristics of muscular dystrophy have also been demonstrated Col4a1 mutant mice. Yet, several aspects of the pathomechanism of COL4A1-associated muscle defects remained largely uncharacterized. Based on the results of genetic, histological, molecular, and biochemical analyses in an allelic series of Drosophila col4a1 mutants, we provide evidence that col4a1 mutations arise by transitions in glycine triplets, associate with severely compromised muscle fibers within the single-layer striated muscle of the common oviduct, characterized by loss of sarcomere structure, disintegration and streaming of Z-discs, indicating an essential role for the COL4A1 protein. Features of altered cytoskeletal phenotype include actin bundles traversing over sarcomere units, amorphous actin aggregates, atrophy, and aberrant fiber size. The mutant COL4A1-associated defects appear to recapitulate integrin-mediated adhesion phenotypes observed in RNA-inhibitory Drosophila. Our results provide insight into the mechanistic details of COL4A1-associated muscle disorders and suggest a role for integrin-collagen interaction in the maintenance of sarcomeres.
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Bee, G., V. G. Pursel, A. D. Mitchell, et al. "Carcass composition and skeletal muscle morphology of swine expressing an insulin-like growth factor I transgene." Archives Animal Breeding 50, no. 5 (2007): 501–19. http://dx.doi.org/10.5194/aab-50-501-2007.
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Abstract. Research was conducted to determine if directing expression of insulin-like growth factor I (IGF1) specifically to striated muscle would enhance lean muscle growth in swine. At 120 kg BW, 25 transgenic (T) and 26 control (C) pigs were sacrificed to evaluate carcass composition. T-pigs had lower percentages of fat and higher percentages of lean tissues than C-pigs for the overall carcass and each carcass region (P ≤ 0.002 for each). Expression of the IGF1 transgene did not alter the percentages of the three fiber types in the five skeletal muscles, however, fiber areas of longissimus dorsi muscle (LM) and serratus ventralis were larger (P ≤ 0.031) in T- than in C-pigs. In Tpigs the relative abundance of IGF1 mRNA in gastrocnemius, gluteus medius, LM, and the average for all five skeletal muscles (ASM) was positively (P ≤ 0.011) correlated with percentage of carcass lean (r = +0.597 to 0.804), whereas the relative abundance of IGF1 mRNA in the LM and the ASM was negatively (P ≤ 0.047) correlated with average backfat (r = −0.546 and −0.488, respectively). Based on these results we conclude that expression of IGF1 specifically in skeletal muscle had a positive effect on carcass composition of swine.
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Sumino, Yasuhiro, Fuminori Sato, Toshihide Kumamoto, and Hiromitsu Mimata. "Striated Muscle Fiber Compositions of Human Male Urethral Rhabdosphincter and Levator Ani." Journal of Urology 175, no. 4 (2006): 1417–21. http://dx.doi.org/10.1016/s0022-5347(05)00697-x.
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Palumbo, Carla, Claudio Rovesta, and Marzia Ferretti. "Striated muscle fiber apoptosis after experimental tendon lesion in a rat model." Journal of Anatomy 221, no. 4 (2012): 358–63. http://dx.doi.org/10.1111/j.1469-7580.2012.01554.x.
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Lucas, C. M., M. G. Havenith, F. H. van der Veen, et al. "Changes in canine latissimus dorsi muscle during 24 wk of continuous electrical stimulation." Journal of Applied Physiology 72, no. 3 (1992): 828–35. http://dx.doi.org/10.1152/jappl.1992.72.3.828.
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To study functional, structural, and biochemical adaptations to electrical stimulation of striated muscle in a large animal, the canine latissimus dorsi (LD) muscle was conditioned continuously for 24 wk with an increasing number of pulse bursts (burst duration 250 ms, burst frequency 30 Hz). Force measurements in vivo after 12 wk showed a significant decrease in the ripple, the ratio of interstimulus to peak force amplitude, from 0.94 +/- 0.03 to 0.13 +/- 0.08 (SE; n = 8, P less than 0.05), indicating reduction in contractile speed. Also the steep part of the force-frequency relation shifted to lower frequencies. A significant change in fiber-type composition was seen with both enzyme- and immunohistochemistry, manifested by an increase of type I fibers from 29.5 +/- 2.9 to 83 +/- 8% (SE; n = 8, P less than 0.05). During this period a transient rise in the number of type IIc/Ic fibers (from 3 to 10%) was seen. In the stimulated muscle, capillary-to-fiber ratio increased from 1.9 +/- 0.4 to 2.7 +/- 0.1 (P less than 0.05). A significant increase in mitochondrial volume was also seen, especially in the peripheral part of the fiber. Both creatine kinase and lactate dehydrogenase revealed a significant decline in activity within 12 wk. At the same time a shift in lactate dehydrogenase-isozyme pattern was observed toward the cardiac composition. No additional changes occurred after 12 wk of stimulation, indicating that conversion of the canine LD muscle was complete within this period.
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García-Pelagio, Karla P., Joaquin Muriel, Andrea O'Neill, et al. "Myopathic changes in murine skeletal muscle lacking synemin." American Journal of Physiology-Cell Physiology 308, no. 6 (2015): C448—C462. http://dx.doi.org/10.1152/ajpcell.00331.2014.
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Diseases of striated muscle linked to intermediate filament (IF) proteins are associated with defects in the organization of the contractile apparatus and its links to costameres, which connect the sarcomeres to the cell membrane. Here we study the role in skeletal muscle of synemin, a type IV IF protein, by examining mice null for synemin (synm-null). Synm-null mice have a mild skeletal muscle phenotype. Tibialis anterior (TA) muscles show a significant decrease in mean fiber diameter, a decrease in twitch and tetanic force, and an increase in susceptibility to injury caused by lengthening contractions. Organization of proteins associated with the contractile apparatus and costameres is not significantly altered in the synm-null. Elastimetry of the sarcolemma and associated contractile apparatus in extensor digitorum longus myofibers reveals a reduction in tension consistent with an increase in sarcolemmal deformability. Although fatigue after repeated isometric contractions is more marked in TA muscles of synm-null mice, the ability of the mice to run uphill on a treadmill is similar to controls. Our results suggest that synemin contributes to linkage between costameres and the contractile apparatus and that the absence of synemin results in decreased fiber size and increased sarcolemmal deformability and susceptibility to injury. Thus synemin plays a moderate but distinct role in fast twitch skeletal muscle.
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Mckoy, G., Y. Hou, S. Y. Yang, et al. "Expression of Ankrd2 in fast and slow muscles and its response to stretch are consistent with a role in slow muscle function." Journal of Applied Physiology 98, no. 6 (2005): 2337–43. http://dx.doi.org/10.1152/japplphysiol.01046.2004.
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In striated muscle, the structural genes associated with muscle fiber phenotype determination as well as muscle mass accretion are regulated largely by mechanical stimuli. Passive stretch of skeletal muscle stimulates muscle growth/hypertrophy and an increased expression of slow muscle genes. We previously identified Ankyrin repeat-domain protein ( Ankrd2) as a novel transcript expressed in fast tibialis anterior muscles after 7 days of passive stretch immobilization in vivo. Here, we test the hypothesis that the expression of Ankrd2 in stretched fast muscle is associated with the stretch-induced expression of slow muscle phenotype rather than the hypertrophic response. Our results show that, in 4- and 7-day stretched tibialis anterior muscle, the expression of Ankrd2 mRNA and protein was significantly upregulated ( P > 0.001). However, in fast muscles of kyphoscoliotic mutant mice, which lack the hypertrophic response to overload but have a slower muscle phenotype than wild-type, Ankrd2 expression was significantly upregulated. The distribution pattern of Ankrd2 in fast and slow muscle is also in accord with their slow fiber composition. Furthermore, it was markedly downregulated in denervated rat soleus muscle, which produces a pronounced shift toward the fast muscle phenotype. Using a sensitive proteomics approach (Ciphergen Technology), we observed that Ankrd2 protein was undetectable in soleus after 4 wk of denervation. We suggest that Ankrd2, which is also a titin binding protein, is a stretch-response gene associated with slow muscle function and that it is part of a separate mechanotransduction system to the one that regulates muscle mass.
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Wahr, Philip A., and Joseph M. Metzger. "Peak power output is maintained in rabbit psoas and rat soleus single muscle fibers when CTP replaces ATP." Journal of Applied Physiology 85, no. 1 (1998): 76–83. http://dx.doi.org/10.1152/jappl.1998.85.1.76.
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The chemomechanical coupling mechanism in striated muscle contraction was examined by changing the nucleotide substrate from ATP to CTP. Maximum shortening velocity [extrapolation to zero force from force-velocity relation ( V max) and slope of slack test plots ( V 0)], maximum isometric force (Po), power, and the curvature of the force-velocity curve [ a/Po(dimensionless parameter inversely related to the curvature)] were determined during maximum Ca2+-activated isotonic contractions of fibers from fast rabbit psoas and slow rat soleus muscles by using 0.2 mM MgATP, 4 mM MgATP, 4 mM MgCTP, or 10 mM MgCTP as the nucleotide substrate. In addition to a decrease in the maximum Ca2+-activated force in both fiber types, a change from 4 mM ATP to 10 mM CTP resulted in a decrease in V max in psoas fibers from 3.26 to 1.87 muscle length/s. In soleus fibers, V max was reduced from 1.94 to 0.90 muscle length/s by this change in nucleotide. Surprisingly, peak power was unaffected in either fiber type by the change in nucleotide as the result of a three- to fourfold decrease in the curvature of the force-velocity relationship. The results are interpreted in terms of the Huxley model of muscle contraction as an increase in f 1and g 1 coupled to a decrease in g 2(where f 1 is the rate of cross-bridge attachment and g 1 and g 2 are rates of detachment) when CTP replaces ATP. This adequately accounts for the observed changes in Po, a/Po, and V max. However, the two-state Huxley model does not explicitly reveal the cross-bridge transitions that determine curvature of the force-velocity relationship. We hypothesize that a nucleotide-sensitive transition among strong-binding cross-bridge states following Pi release, but before the release of the nucleotide diphosphate, underlies the alterations in a/Poreported here.
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Sweitzer, N. K., and R. L. Moss. "The effect of altered temperature on Ca2(+)-sensitive force in permeabilized myocardium and skeletal muscle. Evidence for force dependence of thin filament activation." Journal of General Physiology 96, no. 6 (1990): 1221–45. http://dx.doi.org/10.1085/jgp.96.6.1221.
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The effect of changes in temperature on the calcium sensitivity of tension development was examined in permeabilized cellular preparations of rat ventricle and rabbit psoas muscle. Maximum force and Ca2+ sensitivity of force development increased with temperature in both muscle types. Cardiac muscle was more sensitive to changes in temperature than skeletal muscle in the range 10-15 degrees C. It was postulated that the level of thin filament activation may be decreased by cooling. To investigate this possibility, troponin C (TnC) was partially extracted from both muscle types, thus decreasing the level of thin filament activation independent of temperature and, at least in skeletal muscle fibers, decreasing cooperative activation of the thin filament as well. TnC extraction from cardiac muscle reduced the calcium sensitivity of tension less than did extraction of TnC from skeletal muscle. In skeletal muscle the midpoint shift of the tension-pCa curve with altered temperature was greater after TnC extraction than in control fibers. Calcium sensitivity of tension development was proportional to the maximum tension generated in cardiac or skeletal muscle under all conditions studied. Based on these results, we conclude that (a) maximum tension-generating capability and calcium sensitivity of tension development are related, perhaps causally, in fast skeletal and cardiac muscles, and (b) thin filament activation is less cooperative in cardiac muscle than in skeletal muscle, which explains the differential sensitivity of the two fiber types to temperature and TnC extraction. Reducing thin filament cooperativity in skeletal muscle by TnC extraction results in a response to temperature similar to that of control cardiac cells. This study provides evidence that force levels in striated muscle influence the calcium binding affinity of TnC.
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Mikłosz, Agnieszka, Bartłomiej Łukaszuk, Adrian Chabowski, and Jan Górski. "Treadmill Running Changes Endothelial Lipase Expression: Insights from Gene and Protein Analysis in Various Striated Muscle Tissues and Serum." Biomolecules 11, no. 6 (2021): 906. http://dx.doi.org/10.3390/biom11060906.
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Endothelial lipase (EL) is an enzyme capable of HDL phospholipids hydrolysis. Its action leads to a reduction in the serum high-density lipoprotein concentration, and thus, it exerts a pro-atherogenic effect. This study examines the impact of a single bout exercise on the gene and protein expression of the EL in skeletal muscles composed of different fiber types (the soleus—mainly type I, the red gastrocnemius—mostly IIA, and the white gastrocnemius—predominantly IIX fibers), as well as the diaphragm, and the heart. Wistar rats were subjected to a treadmill run: 1) t = 30 [min], V = 18 [m/min]; 2) t = 30 [min], V = 28 [m/min]; 3) t = 120 [min], V = 18 [m/min] (designated: M30, F30, and M120, respectively). We established EL expression in the total muscle homogenates in sedentary animals. Resting values could be ordered with the decreasing EL protein expression as follows: endothelium of left ventricle > diaphragm > red gastrocnemius > right ventricle > soleus > white gastrocnemius. Furthermore, we observed that even a single bout of exercise was capable of inducing changes in the mRNA and protein level of EL, with a clearer pattern observed for the former. After 30 min of running at either exercise intensity, the expression of EL transcript in all the cardiovascular components of muscles tested, except the soleus, was reduced in comparison to the respective sedentary control. The protein content of EL varied with the intensity and/or duration of the run in the studied whole tissue homogenates. The observed differences between EL expression in vascular beds of muscles may indicate the muscle-specific role of the lipase.
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Krivoi, Igor, and Alexey Petrov. "Cholesterol and the Safety Factor for Neuromuscular Transmission." International Journal of Molecular Sciences 20, no. 5 (2019): 1046. http://dx.doi.org/10.3390/ijms20051046.
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A present review is devoted to the analysis of literature data and results of own research. Skeletal muscle neuromuscular junction is specialized to trigger the striated muscle fiber contraction in response to motor neuron activity. The safety factor at the neuromuscular junction strongly depends on a variety of pre- and postsynaptic factors. The review focuses on the crucial role of membrane cholesterol to maintain a high efficiency of neuromuscular transmission. Cholesterol metabolism in the neuromuscular junction, its role in the synaptic vesicle cycle and neurotransmitter release, endplate electrogenesis, as well as contribution of cholesterol to the synaptogenesis, synaptic integrity, and motor disorders are discussed.
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Derkacs, Amanda D. Felder, Samuel R. Ward, and Richard L. Lieber. "The Use of Neural Networks and Texture Analysis for Rapid Objective Selection of Regions of Interest in Cytoskeletal Images." Microscopy and Microanalysis 18, no. 1 (2012): 115–22. http://dx.doi.org/10.1017/s1431927611012670.
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AbstractUnderstanding cytoskeletal dynamics in living tissue is prerequisite to understanding mechanisms of injury, mechanotransduction, and mechanical signaling. Real-time visualization is now possible using transfection with plasmids that encode fluorescent cytoskeletal proteins. Using this approach with the muscle-specific intermediate filament protein desmin, we found that a green fluorescent protein–desmin chimeric protein was unevenly distributed throughout the muscle fiber, resulting in some image areas that were saturated as well as others that lacked any signal. Our goal was to analyze the muscle fiber cytoskeletal network quantitatively in an unbiased fashion. To objectively select areas of the muscle fiber that are suitable for analysis, we devised a method that provides objective classification of regions of images of striated cytoskeletal structures into “usable” and “unusable” categories. This method consists of a combination of spatial analysis of the image using Fourier methods along with a boosted neural network that “decides” on the quality of the image based on previous training. We trained the neural network using the expert opinion of three scientists familiar with these types of images. We found that this method was over 300 times faster than manual classification and that it permitted objective and accurate classification of image regions.
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Gokhin, David S., Raymond A. Lewis, Caroline R. McKeown, et al. "Tropomodulin isoforms regulate thin filament pointed-end capping and skeletal muscle physiology." Journal of Cell Biology 189, no. 1 (2010): 95–109. http://dx.doi.org/10.1083/jcb.201001125.
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During myofibril assembly, thin filament lengths are precisely specified to optimize skeletal muscle function. Tropomodulins (Tmods) are capping proteins that specify thin filament lengths by controlling actin dynamics at pointed ends. In this study, we use a genetic targeting approach to explore the effects of deleting Tmod1 from skeletal muscle. Myofibril assembly, skeletal muscle structure, and thin filament lengths are normal in the absence of Tmod1. Tmod4 localizes to thin filament pointed ends in Tmod1-null embryonic muscle, whereas both Tmod3 and -4 localize to pointed ends in Tmod1-null adult muscle. Substitution by Tmod3 and -4 occurs despite their weaker interactions with striated muscle tropomyosins. However, the absence of Tmod1 results in depressed isometric stress production during muscle contraction, systemic locomotor deficits, and a shift to a faster fiber type distribution. Thus, Tmod3 and -4 compensate for the absence of Tmod1 structurally but not functionally. We conclude that Tmod1 is a novel regulator of skeletal muscle physiology.
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Ikonomov, Ognian C., Diego Sbrissa, Khortnal Delvecchio, et al. "Muscle-specific Pikfyve gene disruption causes glucose intolerance, insulin resistance, adiposity, and hyperinsulinemia but not muscle fiber-type switching." American Journal of Physiology-Endocrinology and Metabolism 305, no. 1 (2013): E119—E131. http://dx.doi.org/10.1152/ajpendo.00030.2013.
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The evolutionarily conserved kinase PIKfyve that synthesizes PtdIns5P and PtdIns(3,5)P2 has been implicated in insulin-regulated GLUT4 translocation/glucose entry in 3T3-L1 adipocytes. To decipher PIKfyve's role in muscle and systemic glucose metabolism, here we have developed a novel mouse model with Pikfyve gene disruption in striated muscle (MPIfKO). These mice exhibited systemic glucose intolerance and insulin resistance at an early age but had unaltered muscle mass or proportion of slow/fast-twitch muscle fibers. Insulin stimulation of in vivo or ex vivo glucose uptake and GLUT4 surface translocation was severely blunted in skeletal muscle. These changes were associated with premature attenuation of Akt phosphorylation in response to in vivo insulin, as tested in young mice. Starting at 10–11 wk of age, MPIfKO mice progressively accumulated greater body weight and fat mass. Despite increased adiposity, serum free fatty acid and triglyceride levels were normal until adulthood. Together with the undetectable lipid accumulation in liver, these data suggest that lipotoxicity and muscle fiber switching do not contribute to muscle insulin resistance in MPIfKO mice. Furthermore, the 80% increase in total fat mass resulted from increased fat cell size rather than altered fat cell number. The observed profound hyperinsulinemia combined with the documented increases in constitutive Akt activation, in vivo glucose uptake, and gene expression of key enzymes for fatty acid biosynthesis in MPIfKO fat tissue suggest that the latter is being sensitized for de novo lipid anabolism. Our data provide the first in vivo evidence that PIKfyve is essential for systemic glucose homeostasis and insulin-regulated glucose uptake/GLUT4 translocation in skeletal muscle.
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Moreira Neto, Antonio Augusto, Sylvio Sebastião de Souza Júnior, Vera Luíza Capelozzi, et al. "Effects of cilostazol in kidney and skeletal striated muscle of Wistar rats submitted to acute ischemia and reperfusion of hind limbs." Acta Cirurgica Brasileira 27, no. 11 (2012): 783–88. http://dx.doi.org/10.1590/s0102-86502012001100007.
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PURPOSE: To investigate the effect of cilostazol, in kidney and skeletal muscle of rats submitted to acute ischemia and reperfusion. METHODS: Fourty three animals were randomized and divided into two groups. Group I received a solution of cilostazol (10 mg/Kg) and group II received saline solution 0.9% (SS) by orogastric tube after ligature of the abdominal aorta. After four hours of ischemia the animals were divided into four subgroups: group IA (Cilostazol): two hours of reperfusion. Group IIA (SS): two hours of reperfusion. Group IB (Cilostazol): six hours of reperfusion. Group IIB (SS) six hours of reperfusion. After reperfusion, a left nephrectomy was performed and removal of the muscles of the hind limb. The histological parameters were studied. In kidney cylinders of myoglobin, vacuolar degeneration and acute tubular necrosis. In muscle interstitial edema, inflammatory infiltrate, hypereosinophilia fiber, cariopicnose and necrosis. Apoptosis was assessed by immunohistochemistry for cleaved caspase-3 and TUNEL. RESULTS: There was no statistically significant difference between groups. CONCLUSION: Cilostazol had no protective effect on the kidney and the skeletal striated muscle in rats submitted to acute ischemia and reperfusion in this model.
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Mijailovich, Srboljub M., Momcilo Prodanovic, and Thomas C. Irving. "Estimation of Forces on Actin Filaments in Living Muscle from X-ray Diffraction Patterns and Mechanical Data." International Journal of Molecular Sciences 20, no. 23 (2019): 6044. http://dx.doi.org/10.3390/ijms20236044.
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Many biological processes are triggered or driven by mechanical forces in the cytoskeletal network, but these transducing forces have rarely been assessed. Striated muscle, with its well-organized structure provides an opportunity to assess intracellular forces using small-angle X-ray fiber diffraction. We present a new methodology using Monte Carlo simulations of muscle contraction in an explicit 3D sarcomere lattice to predict the fiber deformations and length changes along thin filaments during contraction. Comparison of predicted diffraction patterns to experimental meridional X-ray reflection profiles allows assessment of the stepwise changes in intermonomer spacings and forces in the myofilaments within living muscle cells. These changes along the filament length reflect the effect of forces from randomly attached crossbridges. This approach enables correlation of the molecular events, such as the current number of attached crossbridges and the distributions of crossbridge forces to macroscopic measurements of force and length changes during muscle contraction. In addition, assessments of fluctuations in local forces in the myofilaments may reveal how variations in the filament forces acting on signaling proteins in the sarcomere M-bands and Z-discs modulate gene expression, protein synthesis and degradation, and as well to mechanisms of adaptation of muscle in response to changes in mechanical loading.
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Stiber, Jonathan A., Zhu-Shan Zhang, Jarrett Burch, et al. "Mice Lacking Homer 1 Exhibit a Skeletal Myopathy Characterized by Abnormal Transient Receptor Potential Channel Activity." Molecular and Cellular Biology 28, no. 8 (2008): 2637–47. http://dx.doi.org/10.1128/mcb.01601-07.
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ABSTRACT Transient receptor potential (TRP) channels are nonselective cation channels, several of which are expressed in striated muscle. Because the scaffolding protein Homer 1 has been implicated in TRP channel regulation, we hypothesized that Homer proteins play a significant role in skeletal muscle function. Mice lacking Homer 1 exhibited a myopathy characterized by decreased muscle fiber cross-sectional area and decreased skeletal muscle force generation. Homer 1 knockout myotubes displayed increased basal current density and spontaneous cation influx. This spontaneous cation influx in Homer 1 knockout myotubes was blocked by reexpression of Homer 1b, but not Homer 1a, and by gene silencing of TRPC1. Moreover, diminished Homer 1 expression in mouse models of Duchenne's muscular dystrophy suggests that loss of Homer 1 scaffolding of TRP channels may contribute to the increased stretch-activated channel activity observed in mdx myofibers. These findings provide direct evidence that Homer 1 functions as an important scaffold for TRP channels and regulates mechanotransduction in skeletal muscle.
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Zhang, Jianlin, Marie-Louise Bang, David S. Gokhin, et al. "Syncoilin is required for generating maximum isometric stress in skeletal muscle but dispensable for muscle cytoarchitecture." American Journal of Physiology-Cell Physiology 294, no. 5 (2008): C1175—C1182. http://dx.doi.org/10.1152/ajpcell.00049.2008.
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Syncoilin is a striated muscle-specific intermediate filament-like protein, which is part of the dystrophin-associated protein complex (DPC) at the sarcolemma and provides a link between the extracellular matrix and the cytoskeleton through its interaction with α-dystrobrevin and desmin. Its upregulation in various neuromuscular diseases suggests that syncoilin may play a role in human myopathies. To study the functional role of syncoilin in cardiac and skeletal muscle in vivo, we generated syncoilin-deficient ( syncoilin−/−) mice. Our detailed analysis of these mice up to 2 yr of age revealed that syncoilin is entirely dispensable for cardiac and skeletal muscle development and maintenance of cellular structure but is required for efficient lateral force transmission during skeletal muscle contraction. Notably, syncoilin−/− skeletal muscle generates less maximal isometric stress than wild-type (WT) muscle but is as equally susceptible to eccentric contraction-induced injury as WT muscle. This suggests that syncoilin may play a supportive role for desmin in the efficient coupling of mechanical stress between the myofibril and fiber exterior. It is possible that the reduction in isometric stress production may predispose the syncoilin skeletal muscle to a dystrophic condition.
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Lu, MH, C. DiLullo, T. Schultheiss, et al. "The vinculin/sarcomeric-alpha-actinin/alpha-actin nexus in cultured cardiac myocytes." Journal of Cell Biology 117, no. 5 (1992): 1007–22. http://dx.doi.org/10.1083/jcb.117.5.1007.
Full textAbstract:
Experiments are described supporting the proposition that the assembly of stress fibers in non-muscle cells and the assembly of myofibrils in cardiac cells share conserved mechanisms. Double staining with a battery of labeled antibodies against membrane-associated proteins, myofibrillar proteins, and stress fiber proteins reveals the following: (a) dissociated, cultured cardiac myocytes reconstitute intercalated discs consisting of adherens junctions (AJs) and desmosomes at sites of cell-cell contact and sub-sarcolemmal adhesion plaques (SAPs) at sites of cell-substrate contact; (b) each AJ or SAP associates proximally with a striated myofibril, and conversely every striated myofibril is capped at either end by an AJ or a SAP; (C) the invariant association between a given myofibril and its SAP is especially prominent at the earliest stages of myofibrillogenesis; nascent myofibrils are capped by oppositely oriented SAPs; (d) the insertion of nascent myofibrils into AJs or into SAPs invariably involves vinculin, alpha-actin, and sarcomeric alpha-actinin (s-alpha-actinin); (e) AJs are positive for A-CAM but negative for talin and integrin; SAPs lack A-CAM but are positive for talin and integrin; (f) in cardiac cells all alpha-actinin-containing structures invariably are positive for the sarcomeric isoform, alpha-actin and related sarcomeric proteins; they lack non-s-alpha-actinin, gamma-actin, and caldesmon; (g) in fibroblasts all alpha-actinin-containing structures are positive for the non-sarcomeric isoform, gamma-actin, and related non-sarcomeric proteins, including caldesmon; and (h) myocytes differ from all other types of adherent cultured cells in that they do not assemble authentic stress fibers; instead they assemble stress fiber-like structures of linearly aligned I-Z-I-like complexes consisting exclusively of sarcomeric proteins.
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Pieples, Kathy, Grace Arteaga, R. John Solaro, et al. "Tropomyosin 3 expression leads to hypercontractility and attenuates myofilament length-dependent Ca2+activation." American Journal of Physiology-Heart and Circulatory Physiology 283, no. 4 (2002): H1344—H1353. http://dx.doi.org/10.1152/ajpheart.00351.2002.
Full textAbstract:
Tropomyosin (TM), an integral component of the thin filament, is encoded by three striated muscle isoforms: α-TM, β-TM, and TPM 3. Although the α-TM and β-TM isoforms are well characterized, less is known about the function of the TPM 3 isoform, which is predominantly found in the slow-twitch musculature of mammals. To determine its functional significance, we ectopically expressed this isoform in the hearts of transgenic mice. We generated six transgenic mouse lines that produce varying levels of TPM 3 message with ectopic TPM 3 protein accounting for 40–60% of the total striated muscle tropomyosin. The transgenic mice have normal life spans and exhibit no morphological abnormalities in their sarcomeres or hearts. However, there are significant functional alterations in cardiac performance. Physiological assessment of these mice by using closed-chest analyses and a work-performing model reveals a hyperdynamic effect on systolic and diastolic function. Analysis of detergent-extracted fiber bundles demonstrates a decreased sensitivity to Ca2+ in force generation and a decrease in length-dependent Ca2+activation with no detectable change in interfilament spacing as determined by using X-ray diffraction. Our data are the first to demonstrate that TM isoforms can affect sarcomeric performance by decreasing sensitivity to Ca2+ and influencing the length-dependent Ca2+ activation.
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Goldspink, G., A. Scutt, P. T. Loughna, D. J. Wells, T. Jaenicke, and G. F. Gerlach. "Gene expression in skeletal muscle in response to stretch and force generation." American Journal of Physiology-Regulatory, Integrative and Comparative Physiology 262, no. 3 (1992): R356—R363. http://dx.doi.org/10.1152/ajpregu.1992.262.3.r356.
Full textAbstract:
Striated muscle is a tissue in which gene expression is influenced to a large extent by mechanical signals. This includes the regulation of gene expression-associated muscle fiber phenotype determination, which depends on which protein isoform genes are transcribed, as well as muscle fiber mass accretion, which appears to involve some translational regulation. Although muscle synthesizes a set of highly specialized proteins it has a remarkable ability to adapt by expressing different isoforms of the same protein so that it acquires the appropriate contractile characteristics. Our work has focused on the myosin heavy chain (HC) genes as these encode the myosin cross bridge, which is responsible for muscle intrinsic velocity of contraction and economy of force development. RNA analyses after cast immobilization of the limb with the muscle in the lengthened or shortened position and/or with electrical stimulation were used to determine the effects of altered mechanical signals on gene transcription. When the soleus muscle was immobilized in the shortened position in the young animal it did not fully differentiate into a slow postural-type muscle. Even in the adult, the soleus muscle if deprived of stretch and contractile activity switches back to transcribing the fast myosin HC gene. The converse was true when the fast rabbit tibialis anterior was subjected to immobilization in the lengthened position and/or electrical stimulation. Both stretch alone and stimulation alone caused repression of the fast type and activation of the slow myosin genes. The reprogramming of the fast muscle was more complete when the stretch was combined with stimulation.(ABSTRACT TRUNCATED AT 250 WORDS)
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Nissar, Aliyah A., Bart Zemanek, Rita Labatia, et al. "Skeletal muscle regeneration is delayed by reduction in Xin expression: consequence of impaired satellite cell activation?" American Journal of Physiology-Cell Physiology 302, no. 1 (2012): C220—C227. http://dx.doi.org/10.1152/ajpcell.00298.2011.
Full textAbstract:
Xin is a striated muscle-specific actin-binding protein whose mRNA expression has been observed in damaged skeletal muscle. Here we demonstrate increased Xin protein expression early postinjury (≤12 h) and localization primarily to the periphery of damaged myofibers. At 1 day postinjury, Xin is colocalized with MyoD, confirming expression in activated satellite cells (SCs). By 5 days postinjury, Xin is evident in newly regenerated myofibers, with a return to preinjury levels by 14 days of regeneration. To determine whether the increased Xin expression is functionally relevant, tibialis anterior muscles of wild-type mice were infected with Xin-short hairpin RNA (shRNA) adenovirus, whereas the contralateral tibialis anterior received control adenovirus (Control). Four days postinfection, muscles were harvested or injured with cardiotoxin and collected at 3, 5, or 14 days thereafter. When compared with Control, Xin-shRNA infection attenuated muscle regeneration as demonstrated by Myh3 expression and fiber areas. Given the colocalization of Xin and MyoD, we isolated single myofibers from infected muscles to investigate the effect of silencing Xin on SC function. Relative to Control, SC activation, but not proliferation, was significantly impaired in Xin-shRNA-infected muscles. To determine whether Xin affects the G0-G1 transition, cell cycle reentry was assessed on infected C2C12 myoblasts using a methylcellulose assay. No difference in reentry was noted between groups, suggesting that Xin contributes to SC activation by means other than affecting G0-G1 transition. Together these data demonstrate a critical role for Xin in SC activation and reduction in Xin expression results in attenuated skeletal muscle repair.
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Maricelli, Joseph W., Denali R. Kagel, Yemeserach M. Bishaw, O. Lynne Nelson, David C. Lin, and Buel D. Rodgers. "Sexually dimorphic skeletal muscle and cardiac dysfunction in a mouse model of limb girdle muscular dystrophy 2i." Journal of Applied Physiology 123, no. 5 (2017): 1126–38. http://dx.doi.org/10.1152/japplphysiol.00287.2017.
Full textAbstract:
The fukutin-related protein P448L mutant mouse replicates many pathologies common to limb girdle muscular dystrophy 2i (LGMD2i) and is a potentially strong candidate for relevant drug screening studies. Because striated muscle function remains relatively uncharacterized in this mouse, we sought to identify metabolic, functional and histological metrics of exercise and cardiac performance. This was accomplished by quantifying voluntary exercise on running wheels, forced exercise on respiratory treadmills and cardiac output with echocardiography and isoproterenol stress tests. Voluntary exercise revealed few differences between wild-type and P448L mice. By contrast, peak oxygen consumption (VO2peak) was either lower in P448L mice or reduced with repeated low intensity treadmill exercise while it increased in wild-type mice. P448L mice fatigued quicker and ran shorter distances while expending 2-fold more calories/meter. They also received over 6-fold more motivational shocks with repeated exercise. Differences in VO2peak and resting metabolic rate were consistent with left ventricle dysfunction, which often develops in human LGMD2i patients and was more evident in female P448L mice, as indicated by lower fractional shortening and ejection fraction values and higher left ventricle systolic volumes. Several traditional markers of dystrophinopathies were expressed in P448L mice and were exacerbated by exercise, some in a muscle-dependent manner. These include elevated serum creatine kinase and muscle central nucleation, smaller muscle fiber cross-sectional area and more striated muscle fibrosis. These studies together identified several markers of disease pathology that are shared between P448L mice and human subjects with LGMD2i. They also identified novel metrics of exercise and cardiac performance that could prove invaluable in preclinical drug trials.NEW & NOTEWORTHY Limb-girdle muscular dystrophy 2i is a rare dystroglycanopathy that until recently lacked an appropriate animal model. Studies with the FKRP P448L mutant mouse began assessing muscle structure and function as well as running gait. Our studies further characterize systemic muscle function using exercise and cardiac performance. They identified many markers of respiratory, cardiac and skeletal muscle function that could prove invaluable to better understanding the disease and more importantly, to preclinical drug trials.
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van der Ven, P. F., G. Schaart, H. J. Croes, P. H. Jap, L. A. Ginsel, and F. C. Ramaekers. "Titin aggregates associated with intermediate filaments align along stress fiber-like structures during human skeletal muscle cell differentiation." Journal of Cell Science 106, no. 3 (1993): 749–59. http://dx.doi.org/10.1242/jcs.106.3.749.
Full textAbstract:
Differentiating human skeletal muscle cell cultures were used to study the association of titin with other sarcomeric and cytoskeletal proteins during myofibrillogenesis. Several developmental stages of these cultures were double stained with antibodies to titin in combination with antibodies to alpha-actin, alpha-actinin, myosin heavy chain (MHC), nebulin, desmin, and beta-tubulin. The first indications of titin expression were found in postmitotic mononuclear myoblasts where it is located in a random, punctate fashion. At the light microscope level no evidence was found for an association of these titin spots with any of the other proteins studied, with the exception of MHC, which colocalized with titin in a small minority of the titin expressing cells. Subsequently the titin spots were found to be linked to longitudinally oriented stress fiber-like structures (SFLS), containing alpha-actinin and sarcomeric alpha-actin, but not MHC, nebulin or desmin. Upon further maturation titin antibodies seemed to stain SFLS in a rather homogeneous fashion together with MHC, alpha-actin and alpha-actinin. Thereafter a more periodic localization of titin, MHC, alpha-actin and alpha-actinin on SFLS became obvious. From these structures myofibrils developed as a result of further differentiation. Initially only short stretches with a striated titin, MHC, F-actin and alpha-actinin organization were found. Nebulin was integrated in these young myofibrils at a later developmental stage. Desmin was not found to be incorporated in these myofibrils until complete alignment of the sarcomeres in mature myotubes had occurred. At the ultrastructural level titin antibodies recognized aggregates that were associated with intermediate filaments (IF) in postmitotic mononuclear myoblasts. At a later maturational stage, prior to the development of cross-striated myofibrils, the IF-associated titin aggregates were found in close association with subsarcolemmally located SFLS. We conclude that IF and SFLS play an important role in the very early stages of in vitro human myofibrillogenesis. On the basis of our results we assume that titin aggregates are targeted to SFLS through IF. The association of titin with SFLS might be crucial for the unwinding of titin necessary for the assembly of sarcomeres and the first association of titin with other sarcomeric proteins.
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Jagatheesan, Ganapathy, Sudarsan Rajan, Emily M. Schulz та ін. "An internal domain of β-tropomyosin increases myofilament Ca2+ sensitivity". American Journal of Physiology-Heart and Circulatory Physiology 297, № 1 (2009): H181—H190. http://dx.doi.org/10.1152/ajpheart.00329.2008.
Full textAbstract:
Tropomyosin (TM) is involved in Ca2+-mediated muscle contraction and relaxation in the heart. Striated muscle α-TM is the major isoform expressed in the heart. The expression of striated muscle β-TM in the murine myocardium results in a decreased rate of relaxation and increased myofilament Ca2+ sensitivity. Replacing the carboxyl terminus (amino acids 258–284) of α-TM with β-TM (a troponin T-binding region) results in decreased rates of contraction and relaxation in the heart and decreased myofilament Ca2+ sensitivity. We hypothesized that the putative internal troponin T-binding domain (amino acids 175–190) of β-TM may be responsible for the increased myofilament Ca2+ sensitivity observed when the entire β-TM is expressed in the heart. To test this hypothesis, we generated transgenic mice that expressed chimeric TM containing β-TM amino acids 175–190 in the backbone of α-TM (amino acids 1–174 and 191–284). These mice expressed 16–57% chimeric TM and did not develop cardiac hypertrophy or any other morphological changes. Physiological analysis showed that these hearts exhibited decreased rates of contraction and relaxation and a positive response to isoproterenol. Skinned fiber bundle analyses showed a significant increase in myofilament Ca2+ sensitivity. Biophysical experiments demonstrated that the exchanged amino acids did not influence the flexibility of the TM. This is the first study to demonstrate that a specific domain within TM can increase the Ca2+ sensitivity of the thin filament and affect sarcomeric performance. Furthermore, these results enhance the understanding of why TM mutations associated with familial hypertrophic cardiomyopathy demonstrate increased myofilament sensitivity to Ca2+.