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РИС. 3. Раковины Зрелых глохидиев Beringiana beringiana в раЗных ракурсах: А–С – Закрытые раковины, вид со стороны створки (А), вентрального угла (В) и лигамента (С); D–F – полностью открытые раковины, вид иЗнутри (D), снаруЖи (E) и боковых краев створок (F); G, H – приоткрытые раковины, стрелка укаЗывает на остатки волокон мускулаЗамыкателЯ. МасштабнаЯ линейка 100 мкм. СканируюЩаЯ ЭлектроннаЯ микроскопиЯ. FIG. 3. Mature glochidial shells of Beringiana beringiana from different angles of view: A–C – closed shells, view from the valve side (A), ventral angle (B), and ligament (C); D–F – open shells, interior view (D), exterior view (E), and from lateral margins of valves (F); G, H – ajar shells, the arrows indicate the remains of the adductor muscle fibers. Scale bar 100 µm. Scanning electron microscopy. in Первые данные о морфологии глохидиев двустворчатых моллюсков Beringiana beringiana (Bivalvia, Unionidae) оЗера Дальнее, Камчатка
РИС. 3. Раковины Зрелых глохидиев Beringiana beringiana в раЗных ракурсах: А–С – Закрытые раковины, вид со стороны створки (А), вентрального угла (В) и лигамента (С); D–F – полностью открытые раковины, вид иЗнутри (D), снаруЖи (E) и боковых краев створок (F); G, H – приоткрытые раковины, стрелка укаЗывает на остатки волокон мускулаЗамыкателЯ. МасштабнаЯ линейка 100 мкм. СканируюЩаЯ ЭлектроннаЯ микроскопиЯ. FIG. 3. Mature glochidial shells of Beringiana beringiana from different angles of view: A–C – closed shells, view from the valve side (A), ventral angle (B), and ligament (C); D–F – open shells, interior view (D), exterior view (E), and from lateral margins of valves (F); G, H – ajar shells, the arrows indicate the remains of the adductor muscle fibers. Scale bar 100 µm. Scanning electron microscopy.
Dataset for "Quantification of Muscle Fiber Malformations Using Edge Detection to Investigate Chronic Wound Healing"
<p>Primary images, spreadsheets and files for "Quantification of Muscle Fiber Malformations Using Edge Detection to Investigate Chronic Wound Healing"</p>
Harmonization of experimental procedures to assess mitochondrial respiration in human permeabilized skeletal muscle fibers
<p>DatLab files of the experiments included in the "Harmonization of experimental procedures to assess mitochondrial respiration in human permeabilized skeletal muscle fibers" manuscript (<a href="https://doi.org/10.1016/j.freeradbiomed.2024.07.039" target="_blank" rel="noopener">https://doi.org/10.1016/j.freeradbiomed.2024.07.039</a>).</p>
Residual force enhancement is reduced in permeabilized fiber bundles from mdm muscles
<p>Residual force enhancement (RFE) is the increase in steady-state force after active stretch relative to the force after isometric contraction at the same final length. The mdm mutation in mice, characterized by a small deletion in N2A titin, has been proposed to prevent N2A titin-actin interactions so that active mdm muscles are more compliant than WT. This decrease in active muscle stiffness should be associated with reduced RFE. We investigated RFE in permeabilized soleus (SOL) and extensor digitorum longus (EDL) fiber bundles from wild type and mdm mice. On each fiber bundle, we performed active and passive stretch from an average sarcomere length of 2.6 - 3.0 &[mu]m at a slow rate of 0.04 &[mu]m/s, as well as isometric contractions at the initial and final lengths. One-way ANOVA showed that SOL and EDL fiber bundles from mdm mice exhibited significantly lower RFE than WT (P < 0.0001). This result is consistent with previous observations in single myofibrils and intact muscles. However, it contradicts the results from a previous study which appeared to show that compensatory mechanisms could restore titin force enhancement in single fibers from mdm psoas. We suggest that force enhancement measured previously in mdm single fibers was an artifact of the high variability in passive tension found in degenerating fibers, which begins after ~24 days of age. The results are consistent with the hypothesis that RFE is reduced in mdm skeletal muscles due to impaired Ca2+ dependent titin-actin interactions resulting from the small deletion in N2A titin.</p>
Residual force enhancement is reduced in permeabilized fiber bundles from mdm muscles
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Type I fiber decrease and ectopic fat accumulation in skeletal muscle from women with PCOS
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Mechanical loading induces the longitudinal growth of muscle fibers via a rapamycin-insensitive mechanism
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Fig. 5. Correlation between the fibers diameters and body weight from 300 in Morphological and morphometric analysis of skeletal muscle between male and female young adult Colossoma macropomum (Characiformes: Serrasalmidae)
Fig. 5. Correlation between the fibers diameters and body weight from 300 days old Colossoma macropomum. The fibers diameters are showed by class: circle (<20 µm), triangle (20 to 50 µm) and square (>50 µm).
Data from: Cold-acclimation increases depolarization resistance and tolerance in muscle fibers from a chill-susceptible insect, Locusta migratoria
<p>Cold exposure depolarizes cells in insects due to a reduced electrogenic ion transport and a gradual increase in extracellular [K<sup>+</sup>]. Cold-induced depolarization is linked to cold injury in chill-susceptible insects, and the locust, <i>Locusta migratoria</i>, has shown improved cold tolerance following cold-acclimation through depolarization resistance. Here we investigate how cold-acclimation influences depolarization resistance and how this resistance relates to improved cold tolerance. To address this question, we investigated if cold-acclimation affects the electrogenic transport capacity and/or the relative K<sup>+</sup> permeability during cold exposure by measuring membrane potentials of warm- and cold-acclimated locusts in the presence/absence of ouabain (Na<sup>+</sup>/K<sup>+</sup> pump blocker) or 4-aminopyridine (4-AP, voltage-gated K<sup>+</sup> channel blocker). In addition, we compared the membrane lipid composition of muscle tissue from warm- and cold-acclimated locust, and the abundance of a range transcripts related to ion transport and cell injury accumulation. We found that cold-acclimated locusts are depolarization resistant due to an elevated K<sup>+</sup> permeability, facilitated by opening of 4-AP sensitive K<sup>+</sup> channels. In accordance, cold-acclimation was associated with an increased abundance of <i>shaker</i> transcripts (gene encoding 4-AP sensitive voltage-gated K<sup>+</sup> channels). Furthermore, we found that cold-acclimation improved muscle cell viability following exposure to cold and hyperkalemia even when muscles were depolarized substantially. Thus, cold-acclimation confers resistance to depolarization by altering the relative ion permeability, but cold-acclimated locusts are also more tolerant to depolarization.</p>
Data from: A functional regulatory variant of MYH3 influences muscle fiber-type composition and intramuscular fat content in pigs
Muscle development and lipid accumulation in muscle critically affect meat quality in livestock. Yet, the underlying genetic factors for myofiber-type specification and intramuscular fat (IMF) accumulation remain to be elucidated. Using two independent intercrosses between Western breeds and Korean native pigs (KNPs) and a joint linkage-linkage disequilibrium analysis, we here identified a 488.1-kb region on porcine chromosome 12 that affects both reddish meat color (a*) and IMF. In this critical region, only the MYH3 gene, encoding myosin heavy chain 3, was found to be preferentially overexpressed in the skeletal muscle in KNPs. Subsequently, MYH3-transgenic mice demonstrated that this gene controls both myofiber-type specification and adipogenesis in skeletal muscle. We discovered a structural variant in the promotor/regulatory region of MYH3 for which Q allele carriers exhibited significantly higher values of a* and IMF than q allele carriers. Furthermore, chromatin immunoprecipitation and co-transfection assays showed the structural variant in the 5'-UTR of MYH3 abrogated binding of the myogenic regulatory factors (MYF5, MYOD, MYOG, and MRF4). The allele distribution of the MYH3 among worldwide pig populations indicated that the MYH3 Q allele is of Asian origin and likely predates domestication. In conclusion, we identified a functional regulatory sequence variant in the porcine MYH3 that provides novel insights into the genetic basis of the regulation of myofiber type ratios and associated changes in IMF in pigs. The MYH3 variant can play an important role to improve pork quality in current breeding programs.
3D rendering (left) and 2D orthoslice (rigth) of a virtual longitudinal section in the chorda tendinea insertion into the papillary muscle allowing to visualize the transition from collagen to muscle fibers
<p>The white square on the 3D rendering indicates the region-of-interest shown on the right. At the beginning of the video, the yellow and<br> blue arrows indicated the presence of adipocytes and a vessel filled with blood.</p>
Variability of the Unique Fiber Potentials of a Spastic Muscle Treated With Botulinum Toxin
ClinicalTrials.gov study NCT04002843. IPD Sharing: Not stated. Countries: 1. Publications: 1.
Muscle Fiber Fragments for Improved Function of Rotator Cuff Musculature Following Rotator Cuff Repair
ClinicalTrials.gov study NCT03752034. IPD Sharing: NO. Countries: 1. Publications: 12.
Data from: Cold-acclimation increases depolarization resistance and tolerance in muscle fibers from a chill-susceptible insect, Locusta migratoria
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Data from: A functional regulatory variant of MYH3 influences muscle fiber-type composition and intramuscular fat content in pigs
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Data from: Preserved single muscle fiber specific force in facioscapulohumeral muscular dystrophy
Objective: To investigate single muscle fiber contractile performance in muscle biopsies from patients with facioscapulohumeral muscular dystrophy, one of the most common hereditary muscle disorders. Methods: we collected 26 vastus lateralis and 24 tibialis anterior muscle biopsies from 14 genetically confirmed FSHD patients and 12 healthy controls. Single muscle fibers (N = 547) were isolated for contractile measurements. Titin content and PEVK phosphorylation were examined in vastus lateralis muscle biopsies. Results: Single muscle fiber specific force is intact at saturating and physiological calcium concentrations in all FSHD biopsies, with (FSHDFAT) and without (FSHDNORMAL) fatty infiltration. Myofilament calcium sensitivity of force is increased in single muscle fibers obtained from FSHD muscle biopsies with increased fatty infiltration, but not in FSHD muscle biopsies without fatty infiltration (pCa50: 5.77-5.80 in healthy control, 5.74-5.83 in FSHDNORMAL and 5.86-5.90 in FSHDFAT single muscle fibers). Cross-bridge cycling kinetics at saturating calcium concentrations and myofilament cooperativity did not differ from healthy controls. Passive force was increased in all FSHD muscle fibers, resulting in increased fiber stiffness. Titin content was increased in FSHD biopsies, however titin phosphorylation did not differ from healthy controls. Conclusion: Muscle weakness in patients with FSHD is not caused by reduced specific force of individual muscle fibers, even in severely affected tissue. Muscle fiber calcium sensitivity of force was increased in severely affected tissue and probably is a compensatory mechanism to maintain specific force. Fiber stiffness was increased in FSHD muscle with and without fatty infiltration, suggesting an early event in disease pathology.
Polyamine Metabolism Dysregulation Contributes to Muscle Fiber Vulnerability in ALS
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Muscle Fibers
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Data from: Preserved single muscle fiber specific force in facioscapulohumeral muscular dystrophy
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Muscle fiber size, myonuclear domain, and fat mass phenotypes in pre-migratory snow buntings
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Allen Brain Atlas
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Annotated Behaviour and Observability Dataset (ABODe)
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