The growth and development of skeletal muscle is an important factor affecting pork production and quality, which is elaborately regulated by many genetic and nutritional factors. MicroRNA (miRNA) is a non-coding RNA with a length of about 22 nt, which binds to the 3'UTR sequence of the mRNA of the target genes, and consequently regulates its post-transcriptional expression level. In recent years, a large number of studies have shown that miRNAs are involved in various life processes such as growth and development, reproduction, and diseases. The role of miRNAs in the regulation of porcine skeletal muscle development was reviewed, with the hope to provide a reference for the genetic improvement of pigs.
Swine ; Animals ; MicroRNAs/metabolism* ; Muscle, Skeletal/metabolism* ; Muscle Development/genetics*

Anoctamin 5 (ANO5)/TMEM16E belongs to a member of the ANO/TMEM16 family member of anion channels. However, it is a matter of debate whether ANO5 functions as a genuine plasma membrane chloride channel. It has been recognized that mutations in the ANO5 gene cause many skeletal muscle diseases such as limb girdle muscular dystrophy type 2L (LGMD2L) and Miyoshi muscular dystrophy type 3 (MMD3) in human. However, the molecular mechanisms of the skeletal myopathies caused by ANO5 defects are poorly understood. To understand the role of ANO5 in skeletal muscle development and function, we silenced the ANO5 gene in C2C12 myoblasts and evaluated whether it impairs myogenesis and myotube function. ANO5 knockdown (ANO5-KD) by shRNA resulted in clustered or aggregated nuclei at the body of myotubes without affecting differentiation or myotube formation. Nuclear positioning defect of ANO5-KD myotubes was accompanied with reduced expression of Kif5b protein, a kinesin-related motor protein that controls nuclear transport during myogenesis. ANO5-KD impaired depolarization-induced [Ca²⁺]i transient and reduced sarcoplasmic reticulum (SR) Ca²⁺ storage. ANO5-KD resulted in reduced protein expression of the dihydropyridine receptor (DHPR) and SR Ca²⁺-ATPase subtype 1. In addition, ANO5-KD compromised co-localization between DHPR and ryanodine receptor subtype 1. It is concluded that ANO5-KD causes nuclear positioning defect by reduction of Kif5b expression, and compromises Ca²⁺ signaling by downregulating the expression of DHPR and SERCA proteins.
Active Transport, Cell Nucleus ; Calcium Channels, L-Type ; Cell Membrane ; Chloride Channels ; Humans ; Muscle Development ; Muscle Fibers, Skeletal ; Muscle, Skeletal ; Muscular Diseases ; Muscular Dystrophies ; Muscular Dystrophies, Limb-Girdle ; Myoblasts ; RNA, Small Interfering ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum

PURPOSE: The purpose of this study was to provide basic data for injury prevention and rehabilitation program development of Taekwondo demonstration team by comparing lower extremity muscles function and proprioceptive senses of Taekwondo demonstration team with or without anterior cruciate ligament (ACL) injury. The subjects were ACL injured Taekwondo demonstration player group (ATD, n=13) who underwent ACL reconstruction and Kukkiwon Taekwondo demonstration player group (KTD, n=13) without injury history.METHODS: To evaluate the lower extremity muscles function, we measured the flexor-extensor muscle strength ratio and isokinetic muscle strength of the knee joint using a isokinetic muscle strength measuring device. In order to investigate the proprioceptive sensory function, position sense, and threshold to detection of passive motion was using a isokinetic muscle strength measuring device. The experiment was conducted on average 26 months after surgery.RESULTS: The results of this study are as follows. There was no significant difference between the two groups in the knee joint flexor-extensor ratio. But there was a significant difference in Knee joint flexion and extension strength between two groups at an angular velocity of 60°/sec, 180°/sec, and 300°/sec. and KTD group was higher than ATD groups (p=0.014, p=0.001, p=0.029, p=0.005, p=0.043, p=0.041, respectively). There was no significant difference between the two groups in the proprioceptive sensory test.CONCLUSION: The results of this study showed that the normal flexor to extensor ratio (50%–70%), But it was close to the injury risk level. Therefore, the training program for the improvement of the muscle strength and the imbalance of the strength of the lower extremity muscle function should be performed in both groups.
Anterior Cruciate Ligament Reconstruction ; Anterior Cruciate Ligament ; Education ; Knee Joint ; Lower Extremity ; Muscle Strength ; Muscles ; Program Development ; Proprioception ; Rehabilitation ; Sensation

PURPOSE: This study aimed to investigate effect of ankle instability on peripheral muscle activation among female ballet dancers to provide information on the development of prevention programs for ankle injury rehabilitation. METHODS: 32 female ballet dancers were randomly divided into two groups: experience ankle sprain group (n=16, age, 20.7±0.8years, BMI 18.6±1.2kg/m2) and non-experience ankle sprain group (n=16, age=21.0±0.8 years, BMI 19.6±2.0kg/m2). Activation of the peroneus longus, tibialis anterior muscle, and gastrocnemius during vertical landing, half pointe, and gait between the two groups were measured. Body composition analyzer was used to examine skeletal muscle mass and body fat mass. RESULTS: A total of 32 patients were included. In the experience ankle sprain group (n=16: left sprain 14, right sprain 2), average ankle sprain injury occurred 7.5 months before the study. The average age of the dancers in the experience ankle sprain group and non-experience ankle sprain group was 20.7±0.8 and 21.0±0.8years, major period was 64.5±23.8 and 71.6±25.8months, BMI was 18.6±1.2 and 19.5±2.0kg/m2, respectively. No significant differences were found on body composition between the two groups (p>0.05). The experience ankle sprain group showed significantly lower tibialis anterior and peroneus longus muscle activation (p<0.5), while gastrocnemius muscle activation appeared to be significantly higher (p<0.05) during landing, half pointe, and normal gait. CONCLUSION: Ankle sprain can cause a decline in peripheral muscle activation and coordination, which increased the risk for repetitive ankle sprain in the future. Moreover, ankle peripheral muscle selective strength training, coordination program development, and application need to be considered to prevent ankle sprain.
Adipose Tissue ; Ankle Injuries ; Ankle ; Body Composition ; Dancing ; Female ; Gait ; Humans ; Leg ; Muscle, Skeletal ; Muscles ; Program Development ; Rehabilitation ; Resistance Training ; Sprains and Strains

BACKGROUND: The objective of this study was to evaluate the influence of masticatory muscle injection of botulinum toxin type A (BTX-A) on the growth of the mandibular bone in vivo. METHODS: Eleven Sprague-Dawley rats were used, and BTX-A (n = 6) or saline (n = 5) was injected at 13 days of age. All injections were given to the right masseter muscle, and the BTX-A dose was 0.5 units. All of the rats were euthanized at 60 days of age. The skulls of the rats were separated and fixed with 10% formalin for micro-computed tomography (micro-CT) analysis. RESULTS: The anthropometric analysis found that the ramus heights and bigonial widths of the BTX-A-injected group were significantly smaller than those of the saline-injected group (P < 0.05), and the mandibular plane angle of the BTX-A-injected group was significantly greater than in the saline-injected group (P < 0.001). In the BTX-A-injected group, the ramus heights II and III and the mandibular plane angles I and II showed significant differences between the injected and non-injected sides (P < 0.05). The BTX-A-injected side of the mandible in the masseter group showed significantly lower mandibular bone growth compared with the non-injected side. CONCLUSION: BTX-A injection into the masseter muscle influences mandibular bone growth.
Animals ; Bone Development ; Botulinum Toxins ; Botulinum Toxins, Type A ; Formaldehyde ; Mandible ; Masseter Muscle ; Masticatory Muscles ; Rats ; Rats, Sprague-Dawley ; Skull

Sumoylation, the conjugation of a small ubiquitin-like modifier (SUMO) protein to a target, has diverse cellular effects. However, the functional roles of the SUMO modification during myogenesis have not been fully elucidated. Here, we report that basal sumoylation of histone deacetylase 1 (HDAC1) enhances the deacetylation of MyoD in undifferentiated myoblasts, whereas further sumoylation of HDAC1 contributes to switching its binding partners from MyoD to Rb to induce myocyte differentiation. Differentiation in C2C12 skeletal myoblasts induced new immunoblot bands above HDAC1 that were gradually enhanced during differentiation. Using SUMO inhibitors and sumoylation assays, we showed that the upper band was caused by sumoylation of HDAC1 during differentiation. Basal deacetylase activity was not altered in the SUMO modification-resistant mutant HDAC1 K444/476R (HDAC1 2R). Either differentiation or transfection of SUMO1 increased HDAC1 activity that was attenuated in HDAC1 2R. Furthermore, HDAC1 2R failed to deacetylate MyoD. Binding of HDAC1 to MyoD was attenuated by K444/476R. Binding of HDAC1 to MyoD was gradually reduced after 2 days of differentiation. Transfection of SUMO1 induced dissociation of HDAC1 from MyoD but potentiated its binding to Rb. SUMO1 transfection further attenuated HDAC1-induced inhibition of muscle creatine kinase luciferase activity that was reversed in HDAC1 2R. HDAC1 2R failed to inhibit myogenesis and muscle gene expression. In conclusion, HDAC1 sumoylation plays a dual role in MyoD signaling: enhancement of HDAC1 deacetylation of MyoD in the basally sumoylated state of undifferentiated myoblasts and dissociation of HDAC1 from MyoD during myogenesis.
Creatine Kinase, MM Form ; Gene Expression ; Histone Deacetylase 1 ; Histone Deacetylases ; Histones ; Luciferases ; Muscle Cells ; Muscle Development ; Myoblasts ; Myoblasts, Skeletal ; Sumoylation ; Transfection

BACKGROUND: Popeye deformity is common after rupture of the biceps muscle's long head tendon. Herein, we report on histological changes in biceps brachii muscles following tenotomy of the long head biceps tendon. METHODS: Twelve Sprague-Dawley rats (12-week-old) underwent tenotomy of the long head biceps tendon in the right shoulder. At postoperative weeks 4, 7, and 10, the operative shoulders were removed by detaching the biceps brachii muscle from the glenoid scapula and humerus; the opposite shoulders were removed as controls. H&E staining was performed to elucidate histological changes in myocytes. Oil-red O staining was performed to determine fatty infiltration. Myostatin antibody immunohistochemistry staining was performed as myostatin is expressed by skeletal muscle cells during myogenesis. RESULTS: H&E staining results revealed no changes in muscle cell nuclei. There were no adipocytes detected. Compared with that of the control biceps, the cross-sectional area of the long head biceps was significantly smaller (p=0.00). Statistical changes in the total extent of the 100 muscle cells were significant (p=0.00). Oil-red O staining revealed no fatty infiltration. Myostatin antibody immunohistochemical staining revealed no significant difference between the two sides. CONCLUSIONS: Muscular changes after tenotomy of the long head biceps included a decrease in the size of the individual muscle cells and in relative muscle mass. There were no changes observed in muscle cell nuclei and no fatty infiltration. Moreover, there were no changes detected by myostatin antibody immunohistochemistry assay.
Adipocytes ; Animals ; Congenital Abnormalities ; Head ; Humerus ; Immunohistochemistry ; Models, Animal ; Muscle Cells ; Muscle Development ; Muscle, Skeletal ; Muscles ; Myostatin ; Rats ; Rats, Sprague-Dawley ; Rupture ; Scapula ; Shoulder ; Tendons ; Tenotomy

Myoblast fusion depends on mitochondrial integrity and intracellular Ca²⁺ signaling regulated by various ion channels. In this study, we investigated the ionic currents associated with [Ca²⁺]i regulation in normal and mitochondrial DNA-depleted (ρ0) L6 myoblasts. The ρ0 myoblasts showed impaired myotube formation. The inwardly rectifying K⁺ current (I(Kir)) was largely decreased with reduced expression of KIR2.1, whereas the voltage-operated Ca²⁺ channel and Ca²⁺-activated K⁺ channel currents were intact. Sustained inhibition of mitochondrial electron transport by antimycin A treatment (24 h) also decreased the I(Kir). The ρ0 myoblasts showed depolarized resting membrane potential and higher basal [Ca²⁺]ᵢ. Our results demonstrated the specific downregulation of I(Kir) by dysfunctional mitochondria. The resultant depolarization and altered Ca²⁺ signaling might be associated with impaired myoblast fusion in ρ0 myoblasts.
Antimycin A ; Down-Regulation ; Electron Transport ; Ion Channels ; Membrane Potentials ; Mitochondria ; Muscle Development ; Muscle Fibers, Skeletal ; Myoblasts* ; Oxidative Phosphorylation*

Myofibrillogenesis regulator-1 (MR-1) is a novel protein involved in cellular proliferation, migration, inflammatory reaction and signal transduction. However, little information is available on the relationship between MR-1 expression and the progression of atherosclerosis. Here we report atheroprotective effects of silencing MR-1 in a model of Ang II-accelerated atherosclerosis, characterized by suppression focal adhesion kinase (FAK) and nuclear factor kappaB (NF-κB) signaling pathway, and atherosclerotic lesion macrophage content. In this model, administration of the siRNA-MR-1 substantially attenuated Ang II-accelerated atherosclerosis with stabilization of atherosclerotic plaques and inhibited FAK, Akt, mammalian target of rapamycin (mTOR) and NF-kB activation, which was associated with suppression of inflammatory factor and atherogenic gene expression in the artery. In vitro studies demonstrated similar changes in Ang II-treated vascular smooth muscle cells (VSMCs) and macrophages: siRNA-MR-1 inhibited the expression levels of proinflammatory factor. These studies uncover crucial proinflammatory mechanisms of Ang II and highlight actions of silencing MR-1 to inhibit Ang II signaling, which is atheroprotective.
Angiotensin II* ; Angiotensins* ; Animals ; Arteries ; Atherosclerosis* ; Cell Proliferation ; Focal Adhesion Protein-Tyrosine Kinases ; Gene Expression ; In Vitro Techniques ; Macrophages ; Mice* ; Muscle Development ; Muscle, Smooth, Vascular ; NF-kappa B ; Plaque, Atherosclerotic ; RNA, Small Interfering ; Signal Transduction ; Sirolimus

The cytokine-like hormone leptin is a classic adipokine that is secreted by adipocytes, increases with weight gain, and decreases with weight loss. Additional studies have, however, shown that leptin is also produced by skeletal muscle, and leptin receptors are abundant in both skeletal muscle and bone-derived mesenchymal (stromal) stem cells. These findings suggest that leptin may play an important role in muscle-bone crosstalk. Leptin treatment in vitro increases the expression of myogenic genes in primary myoblasts, and leptin treatment in vivo increases the expression of microRNAs involved in myogenesis. Bone marrow adipogenesis is associated with low bone mass in humans and rodents, and leptin can reduce marrow adipogenesis centrally through its receptors in the hypothalamus as well as directly via its receptors in bone marrow stem cells. Yet, central leptin resistance can increase with age, and low circulating levels of leptin have been observed among the frail elderly. Thus, aging appears to significantly alter leptin-mediated crosstalk among various organs and tissues. Aging is associated with bone loss and muscle atrophy, contributing to frailty, postural instability, and the incidence of falls. Therapeutic interventions such as protein and amino acid supplementation that can increase muscle mass and muscle-derived leptin may have multiple benefits for the elderly that can potentially reduce the incidence of falls and fractures.
Accidental Falls ; Adipocytes ; Adipogenesis ; Adipokines ; Aged ; Aging* ; Bone Marrow ; Frail Elderly ; Humans ; Hypothalamus ; In Vitro Techniques ; Incidence ; Insulin-Like Growth Factor I ; Leptin* ; Mesenchymal Stromal Cells ; MicroRNAs ; Muscle Development ; Muscle, Skeletal ; Muscular Atrophy ; Myoblasts ; Osteoporosis ; Receptors, Leptin ; Rodentia ; Sarcopenia ; Stem Cells ; Weight Gain ; Weight Loss