Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy

Li, Mei; Andersson-Lendahl, Monika; Sejersen, Thomas; Arner, Anders

doi:10.1085/jgp.201511452

Cited by 30 publications

(26 citation statements)

References 60 publications

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“…Structural and regulatory roles have been suggested for the MyBP-C family in both cardiac and skeletal muscles (4, 304, 322, 449, 604), although most of our knowledge stems from studies on cMyBP-C.…”

Section: Myosin Binding Protein-cmentioning

confidence: 99%

“…Moreover, Abdul-Hussain and colleagues reported that sMyBP-C is the major MyBP-C isoform expressed during early myofibrillogenesis in cultured primary human skeletal myotubes, suggesting that it may be essential for sarcomeric assembly and maintenance (4). Recently, Li and colleagues indicated that knockdown of fMyBP-C in zebrafish larvae leads to development of a myopathic phenotype, characterized by shorter sarcomeres, wider interfilament spacing, and muscle weakness (322). Muscle function was also significantly impaired, and was characterized by reduced force production, prolonged time between stimulus and onset of contraction, and slower rates of contraction and relaxation (322).…”

Section: Myosin Binding Protein-cmentioning

confidence: 99%

“…Recently, Li and colleagues indicated that knockdown of fMyBP-C in zebrafish larvae leads to development of a myopathic phenotype, characterized by shorter sarcomeres, wider interfilament spacing, and muscle weakness (322). Muscle function was also significantly impaired, and was characterized by reduced force production, prolonged time between stimulus and onset of contraction, and slower rates of contraction and relaxation (322). …”

Section: Myosin Binding Protein-cmentioning

confidence: 99%

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Thick Filament Protein Network, Functions, and Disease Association

Wang

Geist

Grogan

et al. 2018

Comprehensive Physiology

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Sarcomeres consist of highly ordered arrays of thick myosin and thin actin filaments along with accessory proteins. Thick filaments occupy the center of sarcomeres where they partially overlap with thin filaments. The sliding of thick filaments past thin filaments is a highly regulated process that occurs in an ATP-dependent manner driving muscle contraction. In addition to myosin that makes up the backbone of the thick filament, four other proteins which are intimately bound to the thick filament, myosin binding protein-C, titin, myomesin, and obscurin play important structural and regulatory roles. Consistent with this, mutations in the respective genes have been associated with idiopathic and congenital forms of skeletal and cardiac myopathies. In this review, we aim to summarize our current knowledge on the molecular structure, subcellular localization, interacting partners, function, modulation via posttranslational modifications, and disease involvement of these five major proteins that comprise the thick filament of striated muscle cells. © 2018 American Physiological Society. Compr Physiol 8:631-709, 2018.

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Section: Myosin Binding Protein-cmentioning

confidence: 99%

Section: Myosin Binding Protein-cmentioning

confidence: 99%

Section: Myosin Binding Protein-cmentioning

confidence: 99%

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Thick Filament Protein Network, Functions, and Disease Association

Wang

Geist

Grogan

et al. 2018

Comprehensive Physiology

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“…Strikingly, while motion appeared normal under baseline conditions, these mutant fish exhibited a reduced “touch-escape” response, possibly suggesting that these mutations required some form of stress to show their true function. Knockdown of fsMyBP-C in zebrafish also resulted in skeletal myopathy, albeit without the severe body curvature described in ssMyBP-C knockouts [105]. These fsMyBP-C null fish exhibited sarcomeric disorganization, reduced active force production, and an increase in markers for muscle atrophy.…”

Section: Introductionmentioning

confidence: 99%

Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology

McNamara

Sadayappan

2018

Archives of Biochemistry and Biophysics

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The Myosin Binding Protein-C (MyBP-C) family is a group of sarcomeric proteins important for striated muscle structure and function. Comprising approximately 2% of the myofilament mass, MyBP-C has important roles in both contraction and relaxation. Three paralogs of MyBP-C are encoded by separate genes with distinct expression profiles in striated muscle. In mammals, cardiac MyBP-C is limited to the heart, and it is the most extensively studied owing to its involvement in cardiomyopathies. However, the roles of two skeletal paralogs, slow and fast, in muscle biology remain poorly characterized. Nonetheless, both have been recently implicated in the development of skeletal myopathies. This calls for a better understanding of their function in the pathophysiology of distal arthrogryposis. This review characterizes MyBP-C as a whole and points out knowledge gaps that still remain with respect to skeletal MyBP-C.

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“…Lattice spacing of contractile laments at 6 dpf was determined by small angle x-ray scattering (SAXS) using synchrotron radiation. as previously described [20,26,27] at beamline PO3 at Petra III, Deutsches Elektronen-Synchrotron (DESY) synchrotron facility in Hamburg Germany [28]. Larvae muscle preparations with aluminum clips were mounted between two hooks in a Kapton cuvette in the physiological solution as described (Sect.…”

Section: Small Angle X-ray Scatteringmentioning

confidence: 99%

Relation between skeletal muscle strength and ubiquitin ligase expression in muscle atrophy models in zebrafish larvae (Danio Rerio)

Liu¹,

Le²,

Schwartzkopf³

et al. 2020

Preprint

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Background Skeletal muscle atrophy is often seen in patients with chronic diseases or muscle disuse. Upregulated expression of ubiquitin ligases such as Muscle Ring Finger 1 (MuRF-1) and Muscle Atrophy F-box (MAFbx) has been shown in different immobilization-induced atrophy models, which is believed to be responsible for the enhanced muscle protein proteolysis and thereafter results in muscle weakness. However, currently used immobilization animal models can include artefacts due to difficulty of food intake and stress. Zebrafish larvae 5-6 days after hatching do not require active movement for food intake, and it is possible to assess the muscle function of their trunk muscle. Therefore, we established two muscle atrophy models using zebrafish larvae and aimed to investigate the role of the MuRFs and MAFbx in relation with muscle function.Methods An actin-myosin interaction blocker (BTS) was used to immobilize zebrafish larvae from 3-6 days after hatching; in another series, dexamethasone was fed to larvae from 3-5 days after hatching. Maximal active force of trunk muscles was examined and the distance between adjacent filaments in sarcomeric structure was measured using small angle x-ray diffraction. MuRF and MAFbx expression was determined using real time PCR. Two-way ANOVA was used to analyze the difference between groups.Results We found a significant up-regulation of MuRF-1 and a lower active force generation in dexamethasone treated larvae. However, although the BTS immobilization induced muscle weakness, it was associated with decreased of MuRF-1 to 3 and MAFbx. After 3 days of immobilization, sarcomere became more compressed compared to the controls.Conclusions Two kinds of muscle atrophy models were successfully established in zebrafish larvae. MuRFs and MAFbx was lowered in BTS treated model whereas MuRF-1 was up-regulated in dexamethasone treated model implicating the complex role of ubiquitin ligase in different muscle atrophy models.

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Knockdown of fast skeletal myosin-binding protein C in zebrafish results in a severe skeletal myopathy

Abstract: MyBPC: A muscle protein for all seasons.

Cited by 30 publications

References 60 publications

Thick Filament Protein Network, Functions, and Disease Association

Thick Filament Protein Network, Functions, and Disease Association

Skeletal myosin binding protein-C: An increasingly important regulator of striated muscle physiology

Relation between skeletal muscle strength and ubiquitin ligase expression in muscle atrophy models in zebrafish larvae (Danio Rerio)

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