Gravitational unloading effects on muscle fiber size, phenotype and myonuclear number

Ohira, Yoshinobu; Yoshinaga, Tetsutaro; Nomura, Takeshi; Kawano, Fuminori; Ishihara, Akihiko; Nonaka, Ikuya; Roy, Roland R.; Edgerton, V. Reggie

doi:10.1016/s0273-1177(02)00395-2

Cited by 94 publications

(66 citation statements)

References 21 publications

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“…Consequently, resistance training, endurance training, muscle immobilization and zero-gravity conditions may trigger distinct adjustments in the skeletal muscle proteome [1,3,59]. In addition, fibre type shifting or major alterations in muscle isoform expression levels also occur in various pathophysiological situations, such as traumatic denervation, disuse atrophy and sarcopenia of old age [60][61][62].…”

Section: Discussionmentioning

confidence: 99%

Proteomic profiling of chronic low‐frequency stimulated fast muscle

et al. 2007

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Skeletal muscle fibre transitions occur in many biological processes, in response to alterations in neuromuscular activity, in muscular disorders, during age-induced muscle wasting and in myogenesis. It was therefore of interest to perform a comprehensive proteomic profiling of muscle transformation. Chronic low-frequency stimulation of the rabbit tibialis anterior muscle represents an established model system for studying the response of fast fibres to enhanced neuromuscular activity under conditions of maximum activation. We have conducted a DIGE analysis of unstimulated control specimens versus 14-and 60-day conditioned muscles. A differential expression pattern was observed for 41 protein species with 29 increased and 12 decreased muscle proteins. Identified classes of proteins that are changed during the fast-to-slow transition process belong to the contractile machinery, ion homeostasis, excitation-contraction coupling, capillarization, metabolism and stress response. Results from immunoblotting agreed with the conversion of the metabolic, regulatory and contractile molecular apparatus to support muscle fibres with slower twitch characteristics. Besides confirming established muscle elements as reliable transition markers, this proteomics-based study has established the actin-binding protein cofilin-2 and the endothelial marker transgelin as novel biomarkers for evaluating muscle transformation.

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Section: Discussionmentioning

confidence: 99%

Proteomic profiling of chronic low‐frequency stimulated fast muscle

et al. 2007

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“…Atrophy and Exercise One of the potential problems associated with cultured meat is that of atrophy or muscle wasting due to a reduction of cell size (Fox 1996) caused by lack of use, denervation, or one of a variety of diseases (Charge et al 2002;Ohira et al 2002). Regular contraction is a necessity for skeletal muscle and promotes differentiation and healthy myofiber morphology while preventing atrophy.…”

Section: Tissue Culturementioning

confidence: 99%

Prospectus of cultured meat—advancing meat alternatives

2010

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“…The proteomic profiling of fast versus slow muscles is crucial for the identification of reliable biomarkers that can differentiate between fibre type-specific disease processes. The transition of fibre types occurs during normal physiological adaptations to changed functional demands, such as extensive physical training or exposure to zero-gravity environments [74,75], and in certain neuromuscular diseases or clinical treatments such as dynamic cardiomyoplasty [76]. The proteomic cataloguing of fibre type-specific muscle markers has been carried out for four animal species of importance for biomedical research, i.e.…”

Section: Proteomic Profiling Of Muscle Fibre Typesmentioning

confidence: 99%

Proteomic profiling of animal models mimicking skeletal muscle disorders

Doran

Gannon

O’Connell

et al. 2007

Proteomics Clinical Apps

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Over the last few decades of biomedical research, animal models of neuromuscular diseases have been widely used for determining pathological mechanisms and for testing new therapeutic strategies. With the emergence of high-throughput proteomics technology, the identification of novel protein factors involved in disease processes has been decisively improved. This review outlines the usefulness of the proteomic profiling of animal disease models for the discovery of new reliable biomarkers, for the optimization of diagnostic procedures and the development of new treatment options for skeletal muscle disorders. Since inbred animal strains show genetically much less interindividual differences as compared to human patients, considerably lower experimental repeats are capable of producing meaningful proteomic data. Thus, animal model proteomics can be conveniently employed for both studying basic mechanisms of molecular pathogenesis and the effects of drugs, genetic modifications or cell-based therapies on disease progression. Based on the results from comparative animal proteomics, a more informed decision on the design of clinical proteomics studies could be reached. Since no one animal model represents a perfect pathobiochemical replica of all of the symptoms seen in complex human disorders, the proteomic screening of novel animal models can also be employed for swift and enhanced protein biochemical phenotyping.

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Gravitational unloading effects on muscle fiber size, phenotype and myonuclear number

Cited by 94 publications

References 21 publications

Proteomic profiling of chronic low‐frequency stimulated fast muscle

Proteomic profiling of chronic low‐frequency stimulated fast muscle

Prospectus of cultured meat—advancing meat alternatives

Proteomic profiling of animal models mimicking skeletal muscle disorders

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