An Electrical Stimulation Method to Control Deep Muscle Contraction using Surface Electrodes

Conventional EMS technology cannot stimulate deep muscles to induce muscle contraction using surface electrodes. Several treatments use electrical stimulation for various neurological conditions, including stroke and spinal cord injury. One such treatment is functional electrical stimulation (FES), a form of rehabilitation in which electrical muscle stimulation (EMS) is provided while the muscles are being moved. Here, we show whether two interfering electrical stimulation pulses could stimulate the deep muscles of the forearm to control muscle contraction. The results showed that the strongest torques were generated across the subjects when the reference frequency was mid-frequency (4,000 Hz) and the beat frequencies were low (20 Hz, 40 Hz, 80 Hz, 160 Hz and 320 Hz). This study is the first counterexample to demonstrate that it is possible to control muscle contraction in the deep muscles of the forearm using surface electrodes, which was previously thought to be impossible.

Absence of Desmin Results in Impaired Adaptive Response to Mechanical Overloading of Skeletal Muscle

Background: Desmin is a muscle-specific protein belonging to the intermediate filament family. Desmin mutations are linked to skeletal muscle defects, including inherited myopathies with severe clinical manifestations. The aim of this study was to examine the role of desmin in skeletal muscle remodeling and performance gain induced by muscle mechanical overloading which mimics resistance training.Methods: Plantaris muscles were overloaded by surgical ablation of gastrocnemius and soleus muscles. The functional response of plantaris muscle to mechanical overloading in desmin-deficient mice (DesKO, n = 32) was compared to that of control mice (n = 36) after 7-days or 1-month overloading. To elucidate the molecular mechanisms implicated in the observed partial adaptive response of DesKO muscle, we examined the expression levels of genes involved in muscle growth, myogenesis, inflammation and oxidative energetic metabolism. Moreover, ultrastructure and the proteolysis pathway were explored.Results: Contrary to control, absolute maximal force did not increase in DesKO muscle following 1-month mechanical overloading. Fatigue resistance was also less increased in DesKO as compared to control muscle. Despite impaired functional adaptive response of DesKO mice to mechanical overloading, muscle weight and the number of oxidative MHC2a-positive fibers per cross-section similarly increased in both genotypes after 1-month overloading. However, mechanical overloading-elicited remodeling failed to activate a normal myogenic program after 7-days overloading, resulting in proportionally reduced activation and differentiation of muscle stem cells. Ultrastructural analysis of the plantaris muscle after 1-month overloading revealed muscle fiber damage in DesKO, as indicated by the loss of sarcomere integrity and mitochondrial abnormalities. Moreover, the observed accumulation of autophagosomes and lysosomes in DesKO muscle fibers could indicate a blockage of autophagy. To address this issue, two main proteolysis pathways, the ubiquitin-proteasome system and autophagy, were explored in DesKO and control muscle. Our results suggested an alteration of proteolysis pathways in DesKO muscle in response to mechanical overloading.Conclusion: Taken together, our results show that mechanical overloading increases the negative impact of the lack of desmin on myofibril organization and mitochondria. Furthermore, our results suggest that under these conditions, the repairing activity of autophagy is disturbed. Consequently, force generation is not improved despite muscle growth, suggesting that desmin is required for a complete response to resistance training in skeletal muscle.

Signaling Pathways That Control Muscle Mass

The loss of skeletal muscle mass under a wide range of acute and chronic maladies is associated with poor prognosis, reduced quality of life, and increased mortality. Decades of research indicate the importance of skeletal muscle for whole body metabolism, glucose homeostasis, as well as overall health and wellbeing. This tissue’s remarkable ability to rapidly and effectively adapt to changing environmental cues is a double-edged sword. Physiological adaptations that are beneficial throughout life become maladaptive during atrophic conditions. The atrophic program can be activated by mechanical, oxidative, and energetic distress, and is influenced by the availability of nutrients, growth factors, and cytokines. Largely governed by a transcription-dependent mechanism, this program impinges on multiple protein networks including various organelles as well as biosynthetic and quality control systems. Although modulating muscle function to prevent and treat disease is an enticing concept that has intrigued research teams for decades, a lack of thorough understanding of the molecular mechanisms and signaling pathways that control muscle mass, in addition to poor transferability of findings from rodents to humans, has obstructed efforts to develop effective treatments. Here, we review the progress made in unraveling the molecular mechanisms responsible for the regulation of muscle mass, as this continues to be an intensive area of research.

Magnesium Sulphate For Tetanus, review of two cases

<div class="WordSection1"><p><strong>Introduction</strong><strong>: </strong>Tetanus is critically ill disease with long term hospitalization period. It need to be carefully monitored, usually in intensive care unit and involves critical care physicians. Benzodiazepine is preferred by World Health Organization (WHO) for muscle spasm control in tetanus, but it will be less costly if magnesium sulphate can be used alone to control spasm and autonomic dysfunction in tetanus. We report a series of 2 tetanus cases that were treated using magnesium sulphate to provide a brief clinical description about the use of magnesium sulphate in tetanus. We also give a brief review on epidemiology, pathophysiology, clinical findings, diagnosis, and treatment of tetanus to provide implications for intensive care physicians. Methods : Case series report</p><p><strong>Results : </strong>Two patients with tetanus was given magnesium sulphate infusion to control muscle spasm and autonomic dysfunction with good results as expected. Both of them were survive and discharged home in healthy condition.</p><p><strong>Conclusions :</strong></p><p>Magnesium sulphate can also be used to control muscle spasm and autonomic dysfunction although WHO recommend benzodiazepines for controlling muscle spasm. Intensive care physicians should have enough knowledge about tetanus and how it should be managed adequately to ensure survival from tetanus.</p></div>

Proteome and transcriptome profiling of equine myofibrillar myopathy identifies diminished peroxiredoxin 6 and altered cysteine metabolic pathways

Equine myofibrillar myopathy (MFM) causes exertional muscle pain and is characterized by myofibrillar disarray and ectopic desmin aggregates of unknown origin. To investigate the pathophysiology of MFM, we compared resting and 3 h postexercise transcriptomes of gluteal muscle and the resting skeletal muscle proteome of MFM and control Arabian horses with RNA sequencing and isobaric tags for relative and absolute quantitation analyses. Three hours after exercise, 191 genes were identified as differentially expressed (DE) in MFM vs. control muscle with >1 log2 fold change (FC) in genes involved in sulfur compound/cysteine metabolism such as cystathionine-beta-synthase ( CBS, ↓4.51), a cysteine and neutral amino acid membrane transporter ( SLC7A10, ↓1.80 MFM), and a cationic transporter (SLC24A1, ↓1.11 MFM). In MFM vs. control at rest, 284 genes were DE with >1 log2 FC in pathways for structure morphogenesis, fiber organization, tissue development, and cell differentiation including > 1 log2 FC in cardiac alpha actin ( ACTC1 ↑2.5 MFM), cytoskeletal desmoplakin ( DSP ↑2.4 MFM), and basement membrane usherin ( USH2A ↓2.9 MFM). Proteome analysis revealed significantly lower antioxidant peroxiredoxin 6 content (PRDX6, ↓4.14 log2 FC MFM), higher fatty acid transport enzyme carnitine palmitoyl transferase (CPT1B, ↑3.49 MFM), and lower sarcomere protein tropomyosin (TPM2, ↓3.24 MFM) in MFM vs. control muscle at rest. We propose that in MFM horses, altered cysteine metabolism and a deficiency of cysteine-containing antioxidants combined with a high capacity to oxidize fatty acids and generate ROS during aerobic exercise causes chronic oxidation and aggregation of key proteins such as desmin.