Skeletal Muscle最新文献

{"title":"Late-onset megaconial myopathy in mice lacking group I Paks.","authors":"Giselle A Joseph,&nbsp;Margaret Hung,&nbsp;Aviva J Goel,&nbsp;Mingi Hong,&nbsp;Marysia-Kolbe Rieder,&nbsp;Noam D Beckmann,&nbsp;Madhavika N Serasinghe,&nbsp;Jerry E Chipuk,&nbsp;Parvathi M Devarakonda,&nbsp;David J Goldhamer,&nbsp;Paulina Aldana-Hernandez,&nbsp;Jonathan Curtis,&nbsp;René L Jacobs,&nbsp;Robert S Krauss","doi":"10.1186/s13395-019-0191-4","DOIUrl":"https://doi.org/10.1186/s13395-019-0191-4","url":null,"abstract":"<p><strong>Background: </strong>Group I Paks are serine/threonine kinases that function as major effectors of the small GTPases Rac1 and Cdc42, and they regulate cytoskeletal dynamics, cell polarity, and transcription. We previously demonstrated that Pak1 and Pak2 function redundantly to promote skeletal myoblast differentiation during postnatal development and regeneration in mice. However, the roles of Pak1 and Pak2 in adult muscle homeostasis are unknown. Choline kinase β (Chk β) is important for adult muscle homeostasis, as autosomal recessive mutations in CHKβ are associated with two human muscle diseases, megaconial congenital muscular dystrophy and proximal myopathy with focal depletion of mitochondria.</p><p><strong>Methods: </strong>We analyzed mice conditionally lacking Pak1 and Pak2 in the skeletal muscle lineage (double knockout (dKO) mice) over 1 year of age. Muscle integrity in dKO mice was assessed with histological stains, immunofluorescence, electron microscopy, and western blotting. Assays for mitochondrial respiratory complex function were performed, as was mass spectrometric quantification of products of choline kinase. Mice and cultured myoblasts deficient for choline kinase β (Chk β) were analyzed for Pak1/2 phosphorylation.</p><p><strong>Results: </strong>dKO mice developed an age-related myopathy. By 10 months of age, dKO mouse muscles displayed centrally-nucleated myofibers, fibrosis, and signs of degeneration. Disease severity occurred in a rostrocaudal gradient, hindlimbs more strongly affected than forelimbs. A distinctive feature of this myopathy was elongated and branched intermyofibrillar (megaconial) mitochondria, accompanied by focal mitochondrial depletion in the central region of the fiber. dKO muscles showed reduced mitochondrial respiratory complex I and II activity. These phenotypes resemble those of rmd mice, which lack Chkβ and are a model for human diseases associated with CHKβ deficiency. Pak1/2 and Chkβ activities were not interdependent in mouse skeletal muscle, suggesting a more complex relationship in regulation of mitochondria and muscle homeostasis.</p><p><strong>Conclusions: </strong>Conditional loss of Pak1 and Pak2 in mice resulted in an age-dependent myopathy with similarity to mice and humans with CHKβ deficiency. Protein kinases are major regulators of most biological processes but few have been implicated in muscle maintenance or disease. Pak1/Pak2 dKO mice offer new insights into these processes.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"9 1","pages":"5"},"PeriodicalIF":4.9,"publicationDate":"2019-02-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-019-0191-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36988068","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dilated cardiomyopathy-mediated heart failure induces a unique skeletal muscle myopathy with inflammation.","authors":"Taejeong Song,&nbsp;Palanikumar Manoharan,&nbsp;Douglas P Millay,&nbsp;Sheryl E Koch,&nbsp;Jack Rubinstein,&nbsp;Judith A Heiny,&nbsp;Sakthivel Sadayappan","doi":"10.1186/s13395-019-0189-y","DOIUrl":"https://doi.org/10.1186/s13395-019-0189-y","url":null,"abstract":"<p><strong>Background: </strong>Skeletal muscle myopathy and exercise intolerance are diagnostic hallmarks of heart failure (HF). However, the molecular adaptations of skeletal muscles during dilated cardiomyopathy (DCM)-mediated HF are not completely understood.</p><p><strong>Methods: </strong>Skeletal muscle structure and function were compared in wild-type (WT) and cardiac myosin binding protein-C null mice (t/t), which develop DCM-induced HF. Cardiac function was examined by echocardiography. Exercise tolerance was measured using a graded maximum treadmill running test. Hindlimb muscle function was assessed in vivo from measurements of plantar flexor strength. Inflammatory status was evaluated from the expression of inflammatory markers and the presence of specific immune cell types in gastrocnemius muscles. Muscle regenerative capacityat days 3, 7, and 14 after eccentric contraction-induced injury was determined from the number of phenotypically new and adult fibers in the gastrocnemius, and functional recovery of plantar flexion torque.</p><p><strong>Results: </strong>t/t mice developed DCM-induced HF in association with profound exercise intolerance, consistent with previous reports. Compared to WT, t/t mouse hearts show significant hypertrophy of the atria and ventricles and reduced fractional shortening, both systolic and diastolic. In parallel, the skeletal muscles of t/t mice exhibit weakness and myopathy. Compared to WT, plantar flexor muscles of t/t null mice produce less peak isometric plantar torque (Po), develop torque more slowly (+ dF/dt), and relax more slowly (- dF/dt, longer half-relaxation times,1/2RT). Gastrocnemius muscles of t/t mice have a greater number of fibers with smaller diameters and central nuclei. Oxidative fibers, both type I and type IIa, show significantly smaller cross-sectional areas and more central nuclei. These fiber phenotypes suggest ongoing repair and regeneration under homeostatic conditions. In addition, the ability of muscles to recover and regenerate after acute injury is impaired in t/t mice.</p><p><strong>Conclusions: </strong>Our studies concluded that DCM-induced HF induces a unique skeletal myopathy characterized by decreased muscle strength, atrophy of oxidative fiber types, ongoing inflammation and damage under homeostasis, and impaired regeneration after acute muscle injury. Furthermore, this unique myopathy in DCM-induced HF likely contributes to and exacerbates exercise intolerance. Therefore, efforts to develop therapeutic interventions to treat skeletal myopathy during DCM-induced HF should be considered.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"9 1","pages":"4"},"PeriodicalIF":4.9,"publicationDate":"2019-01-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-019-0189-y","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36895062","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metabolic derangements of skeletal muscle from a murine model of glioma cachexia.","authors":"Pengfei Cui,&nbsp;Wei Shao,&nbsp;Caihua Huang,&nbsp;Chang-Jer Wu,&nbsp;Bin Jiang,&nbsp;Donghai Lin","doi":"10.1186/s13395-018-0188-4","DOIUrl":"https://doi.org/10.1186/s13395-018-0188-4","url":null,"abstract":"<p><strong>Background: </strong>Cachexia is a complex metabolic disorder and muscle atrophy syndrome, impacting 80% patients with advanced cancers. Malignant glioma is considered to be one of the deadliest human cancers, accounting for about 60% of all primary brain tumors. However, cachexia symptoms induced by glioma have received little attention. This work aims to explore skeletal muscle atrophy in orthotopic glioma murine models.</p><p><strong>Methods: </strong>BALB/c nude mice were orthotopicly implanted with normal glial (HEB) and glioma (WHO II CHG5 and WHO IV U87) cells. Cachexia symptoms of mice were depicted by phenotypic, histopathologic, physiological, and biochemical analyses. Muscle atrophy-related proteins were examined by western blot, and the involved signaling pathways were analyzed. NMR-based metabolomic analysis was applied to profile metabolic derangements in the skeletal muscle, including multivariate statistical analysis, characteristic metabolite identification, and metabolic pathway analysis.</p><p><strong>Results: </strong>Compared with controls, mice implanted with glioma cells exhibit typical cachexia symptoms, indicating a high correlation with the malignant grades of glioma. U87 mice develop cachexia much earlier and more severe than CHG5 mice. The glioma-bearing mice showed significantly decreased skeletal muscle mass and strength, which were associated with suppressed AKT, activated AMPK, FOXO, Atrogin1, and LC3. Interestingly, expressions of MuRF1, MyoD1, and eIF3f were not significantly changed. Consistently, metabolomic analyses elucidate pronounced metabolic derangements in cachectic gastrocnemius relative to controls. Glucose, glycerol, and 3-hydroxybutyrate were remarkably downregulated, whereas glutamate, arginine, leucine, and isoleucine were upregulated in cachectic gastrocnemius. Furthermore, U87 mice showed more characteristic metabolites and more disturbed metabolic pathways including glucose and lipid metabolism, protein catabolism, anabolism, and citric acid cycle anaplerotic.</p><p><strong>Conclusions: </strong>This study demonstrates for the first time that the orthotopic glioma murine model developed here exhibits high fidelity of cachexia manifestations in two malignant grades of glioma. Signaling pathway analysis in combination with metabolomic analysis provides significant insights into the complex pathophysiology of glioma cachexia and expands understanding of the molecular mechanisms underlying muscle atrophy.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"9 1","pages":"3"},"PeriodicalIF":4.9,"publicationDate":"2019-01-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-018-0188-4","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36899674","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Open-CSAM, a new tool for semi-automated analysis of myofiber cross-sectional area in regenerating adult skeletal muscle.","authors":"Thibaut Desgeorges,&nbsp;Sophie Liot,&nbsp;Solene Lyon,&nbsp;Jessica Bouvière,&nbsp;Alix Kemmel,&nbsp;Aurélie Trignol,&nbsp;David Rousseau,&nbsp;Bruno Chapuis,&nbsp;Julien Gondin,&nbsp;Rémi Mounier,&nbsp;Bénédicte Chazaud,&nbsp;Gaëtan Juban","doi":"10.1186/s13395-018-0186-6","DOIUrl":"https://doi.org/10.1186/s13395-018-0186-6","url":null,"abstract":"<p><p>Adult skeletal muscle is capable of complete regeneration after an acute injury. The main parameter studied to assess muscle regeneration efficacy is the cross-sectional area (CSA) of the myofibers as myofiber size correlates with muscle force. CSA analysis can be time-consuming and may trigger variability in the results when performed manually. This is why programs were developed to completely automate the analysis of the CSA, such as SMASH, MyoVision, or MuscleJ softwares. Although these softwares are efficient to measure CSA on normal or hypertrophic/atrophic muscle, they fail to efficiently measure CSA on regenerating muscles. We developed Open-CSAM, an ImageJ macro, to perform a high throughput semi-automated analysis of CSA on skeletal muscle from various experimental conditions. The macro allows the experimenter to adjust the analysis and correct the mistakes done by the automation, which is not possible with fully automated programs. We showed that Open-CSAM was more accurate to measure CSA in regenerating and dystrophic muscles as compared with SMASH, MyoVision, and MuscleJ softwares and that the inter-experimenter variability was negligible. We also showed that, to obtain a representative CSA measurement, it was necessary to analyze the whole muscle section and not randomly selected pictures, a process that was easily and accurately be performed using Open-CSAM. To conclude, we show here an easy and experimenter-controlled tool to measure CSA in muscles from any experimental condition, including regenerating muscle.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"9 1","pages":"2"},"PeriodicalIF":4.9,"publicationDate":"2019-01-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-018-0186-6","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36844824","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Defects in sarcolemma repair and skeletal muscle function after injury in a mouse model of Niemann-Pick type A/B disease.","authors":"V Michailowsky,&nbsp;H Li,&nbsp;B Mittra,&nbsp;S R Iyer,&nbsp;D A G Mazála,&nbsp;M Corrotte,&nbsp;Y Wang,&nbsp;E R Chin,&nbsp;R M Lovering,&nbsp;N W Andrews","doi":"10.1186/s13395-018-0187-5","DOIUrl":"https://doi.org/10.1186/s13395-018-0187-5","url":null,"abstract":"<p><strong>Background: </strong>Niemann-Pick disease type A (NPDA), a disease caused by mutations in acid sphingomyelinase (ASM), involves severe neurodegeneration and early death. Intracellular lipid accumulation and plasma membrane alterations are implicated in the pathology. ASM is also linked to the mechanism of plasma membrane repair, so we investigated the impact of ASM deficiency in skeletal muscle, a tissue that undergoes frequent cycles of injury and repair in vivo.</p><p><strong>Methods: </strong>Utilizing the NPDA/B mouse model ASM^-/- and wild type (WT) littermates, we performed excitation-contraction coupling/Ca²⁺ mobilization and sarcolemma injury/repair assays with isolated flexor digitorum brevis fibers, proteomic analyses with quadriceps femoris, flexor digitorum brevis, and tibialis posterior muscle and in vivo tests of the contractile force (maximal isometric torque) of the quadriceps femoris muscle before and after eccentric contraction-induced muscle injury.</p><p><strong>Results: </strong>ASM^-/- flexor digitorum brevis fibers showed impaired excitation-contraction coupling compared to WT, a defect expressed as reduced tetanic [Ca²⁺]_i in response to electrical stimulation and early failure in sustaining [Ca²⁺]_i during repeated tetanic contractions. When injured mechanically by needle passage, ASM^-/- flexor digitorum brevis fibers showed susceptibility to injury similar to WT, but a reduced ability to reseal the sarcolemma. Proteomic analyses revealed changes in a small group of skeletal muscle proteins as a consequence of ASM deficiency, with downregulation of calsequestrin occurring in the three different muscles analyzed. In vivo, the loss in maximal isometric torque of WT quadriceps femoris was similar immediately after and 2 min after injury. The loss in ASM^-/- mice immediately after injury was similar to WT, but was markedly larger at 2 min after injury.</p><p><strong>Conclusions: </strong>Skeletal muscle fibers from ASM^-/- mice have an impairment in intracellular Ca²⁺ handling that results in reduced Ca²⁺ mobilization and a more rapid decline in peak Ca²⁺ transients during repeated contraction-relaxation cycles. Isolated fibers show reduced ability to repair damage to the sarcolemma, and this is associated with an exaggerated deficit in force during recovery from an in vivo eccentric contraction-induced muscle injury. Our findings uncover the possibility that skeletal muscle functional defects may play a role in the pathology of NPDA/B disease.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"9 1","pages":"1"},"PeriodicalIF":4.9,"publicationDate":"2019-01-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-018-0187-5","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36826029","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Characterization and utilization of the flexor digitorum brevis for assessing skeletal muscle function.","authors":"Michael D Tarpey,&nbsp;Adam J Amorese,&nbsp;Nicholas P Balestrieri,&nbsp;Terence E Ryan,&nbsp;Cameron A Schmidt,&nbsp;Joseph M McClung,&nbsp;Espen E Spangenburg","doi":"10.1186/s13395-018-0160-3","DOIUrl":"https://doi.org/10.1186/s13395-018-0160-3","url":null,"abstract":"<p><strong>Background: </strong>The ability to assess skeletal muscle function and delineate regulatory mechanisms is essential to uncovering therapeutic approaches that preserve functional independence in a disease state. Skeletal muscle provides distinct experimental challenges due to inherent differences across muscle groups, including fiber type and size that may limit experimental approaches. The flexor digitorum brevis (FDB) possesses numerous properties that offer the investigator a high degree of experimental flexibility to address specific hypotheses. To date, surprisingly few studies have taken advantage of the FDB to investigate mechanisms regulating skeletal muscle function. The purpose of this study was to characterize and experimentally demonstrate the value of the FDB muscle for scientific investigations.</p><p><strong>Methods: </strong>First, we characterized the FDB phenotype and provide reference comparisons to skeletal muscles commonly used in the field. We developed approaches allowing for experimental assessment of force production, in vitro and in vivo microscopy, and mitochondrial respiration to demonstrate the versatility of the FDB. As proof-of principle, we performed experiments to alter force production or mitochondrial respiration to validate the flexibility the FDB affords the investigator.</p><p><strong>Results: </strong>The FDB is made up of small predominantly type IIa and IIx fibers that collectively produce less peak isometric force than the extensor digitorum longus (EDL) or soleus muscles, but demonstrates a greater fatigue resistance than the EDL. Unlike the other muscles, inherent properties of the FDB muscle make it amenable to multiple in vitro- and in vivo-based microscopy methods. Due to its anatomical location, the FDB can be used in cardiotoxin-induced muscle injury protocols and is amenable to electroporation of cDNA with a high degree of efficiency allowing for an effective means of genetic manipulation. Using a novel approach, we also demonstrate methods for assessing mitochondrial respiration in the FDB, which are comparable to the commonly used gastrocnemius muscle. As proof of principle, short-term overexpression of Pgc1α in the FDB increased mitochondrial respiration rates.</p><p><strong>Conclusion: </strong>The results highlight the experimental flexibility afforded the investigator by using the FDB muscle to assess mechanisms that regulate skeletal muscle function.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"8 1","pages":"14"},"PeriodicalIF":4.9,"publicationDate":"2018-04-17","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-018-0160-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10000854","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Absence of physiological Ca²⁺ transients is an initial trigger for mitochondrial dysfunction in skeletal muscle following denervation.","authors":"Chehade Karam,&nbsp;Jianxun Yi,&nbsp;Yajuan Xiao,&nbsp;Kamal Dhakal,&nbsp;Lin Zhang,&nbsp;Xuejun Li,&nbsp;Carlo Manno,&nbsp;Jiejia Xu,&nbsp;Kaitao Li,&nbsp;Heping Cheng,&nbsp;Jianjie Ma,&nbsp;Jingsong Zhou","doi":"10.1186/s13395-017-0123-0","DOIUrl":"https://doi.org/10.1186/s13395-017-0123-0","url":null,"abstract":"<p><strong>Background: </strong>Motor neurons control muscle contraction by initiating action potentials in muscle. Denervation of muscle from motor neurons leads to muscle atrophy, which is linked to mitochondrial dysfunction. It is known that denervation promotes mitochondrial reactive oxygen species (ROS) production in muscle, whereas the initial cause of mitochondrial ROS production in denervated muscle remains elusive. Since denervation isolates muscle from motor neurons and deprives it from any electric stimulation, no action potentials are initiated, and therefore, no physiological Ca²⁺ transients are generated inside denervated muscle fibers. We tested whether loss of physiological Ca²⁺ transients is an initial cause leading to mitochondrial dysfunction in denervated skeletal muscle.</p><p><strong>Methods: </strong>A transgenic mouse model expressing a mitochondrial targeted biosensor (mt-cpYFP) allowed a real-time measurement of the ROS-related mitochondrial metabolic function following denervation, termed \"mitoflash.\" Using live cell imaging, electrophysiological, pharmacological, and biochemical studies, we examined a potential molecular mechanism that initiates ROS-related mitochondrial dysfunction following denervation.</p><p><strong>Results: </strong>We found that muscle fibers showed a fourfold increase in mitoflash activity 24 h after denervation. The denervation-induced mitoflash activity was likely associated with an increased activity of mitochondrial permeability transition pore (mPTP), as the mitoflash activity was attenuated by application of cyclosporine A. Electrical stimulation rapidly reduced mitoflash activity in both sham and denervated muscle fibers. We further demonstrated that the Ca²⁺ level inside mitochondria follows the time course of the cytosolic Ca²⁺ transient and that inhibition of mitochondrial Ca²⁺ uptake by Ru360 blocks the effect of electric stimulation on mitoflash activity.</p><p><strong>Conclusions: </strong>The loss of cytosolic Ca²⁺ transients due to denervation results in the downstream absence of mitochondrial Ca²⁺ uptake. Our studies suggest that this could be an initial trigger for enhanced mPTP-related mitochondrial ROS generation in skeletal muscle.</p>","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"7 1","pages":"6"},"PeriodicalIF":4.9,"publicationDate":"2017-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-017-0123-0","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9966686","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Erratum to: Voluntary resistance wheel exercise from mid-life prevents sarcopenia and increases markers of mitochondrial function and autophagy in muscles of old male and female C57BL/6J mice","authors":"Zoe White, J. Terrill, Robert B. White, C. Mcmahon, P. Sheard, M. Grounds, T. Shavlakadze","doi":"10.1186/s13395-017-0120-3","DOIUrl":"https://doi.org/10.1186/s13395-017-0120-3","url":null,"abstract":"","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":" ","pages":""},"PeriodicalIF":4.9,"publicationDate":"2017-02-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-017-0120-3","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"44636455","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Deletion of the Ste20-like kinase SLK in skeletal muscle results in a progressive myopathy and muscle weakness","authors":"Benjamin R. Pryce, Khalid N. Al-Zahrani, S. Dufresne, N. Belkina, Cédrik Labrèche, G. Patiño-López, J. Frenette, S. Shaw, L. Sabourin","doi":"10.1186/s13395-016-0119-1","DOIUrl":"https://doi.org/10.1186/s13395-016-0119-1","url":null,"abstract":"","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"7 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2017-02-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-016-0119-1","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"65847334","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Inhibition of Stat3 signaling ameliorates atrophy of the soleus muscles in mice lacking the vitamin D receptor","authors":"S. D. Gopinath","doi":"10.1186/s13395-017-0121-2","DOIUrl":"https://doi.org/10.1186/s13395-017-0121-2","url":null,"abstract":"","PeriodicalId":21747,"journal":{"name":"Skeletal Muscle","volume":"7 1","pages":""},"PeriodicalIF":4.9,"publicationDate":"2017-01-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1186/s13395-017-0121-2","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"65847383","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"医学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}