Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization

Isfort, Robert J.; Wang, Feng; Greis, Kenneth D.; Sun, Yiping; Keough, T.; Bodine, Sue C.; Anderson, N. Leigh

doi:10.1016/s1570-0232(02)00021-1

Cited by 35 publications

(30 citation statements)

References 17 publications

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“…The effects of immobilization was also investigated in the rat by differential proteomic analysis after varying duration of hindlimb suspension [92][93][94][95]. As observed in humans after prolonged bed rest, remodeling of a postural muscle (the soleus) phenotype, results in a fiber type shift from slow oxidative to fast glycolytic which is paralleled by an increase in muscle fatiguability.…”

Section: Effects Of Immobilizationmentioning

confidence: 99%

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Gelfi

Vasso

Cerretelli

2011

Journal of Proteomics

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Section: Effects Of Immobilizationmentioning

confidence: 99%

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Gelfi

Vasso

Cerretelli

2011

Journal of Proteomics

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“…Another important area of comparative muscle proteomics is the study of diseased human tissue and animal models. The focus has been on immobilizationinduced muscular atrophy (79,80), muscular dystrophy (34,35,56,81,82), dysferlinopathy (83), mitochondrial muscle disease (15) and sarcopenia (16,(84)(85)(86)(87)(88).…”

Section: Skeletal Muscle Proteomicsmentioning

confidence: 99%

Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (Review)

Doran

Donoghue²,

O’Connell³

et al. 2007

Int J Mol Med

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Abstract. In contrast to the traditional biochemical study of single proteins or isolated pathways in health and disease, technical advances in the high-throughput screening of peptides by mass spectrometry have established new ways of identifying entire cellular protein populations in one swift analytical approach. This review discusses the recent progress in the biochemical analysis of skeletal muscle extracts and outlines the mass spectrometry-based proteomics approach for studying muscle tissues in normal and pathobiochemical processes using peptide mass fingerprinting. Individual topics covered include the most commonly inherited muscle disease, X-linked muscular dystrophy, the physiological process of fast-to-slow fibre transformation, and the role of fibre degeneration in age-related muscle wasting. Recent proteomic profiling studies of dystrophic muscles have revealed new disease markers in dystrophin-deficient fibres, such as adenylate kinase, the Ca 2+ -binding protein regucalcin and the small heat shock protein cvHSP. Since these muscle proteins are of low abundance, they have not previously been identified as biomarkers of muscular dystrophy, illustrating the increased sensitivity of modern mass spectrometric techniques. This review outlines comparative proteomic techniques that employ conventional labeling methods, such as Coomassie-or silver-staining. In addition, the most advanced proteomic screening approach currently available, fluorescence difference in-gel electrophoresis, is described and its potential for studying muscle proteomes is critically examined. As an alternative suggestion, the two-dimensional analysis of different protein samples separated in parallel on a single second dimension gel is introduced and the usefulness of this technique for direct comparative investigations is explained. The potential of studying protein complex formation by intraproteomics, estimating the composition of subcellular fraction by subproteomics, and analyzing total muscle protein extracts by mass spectrometry-based proteomics, is enormous. Proteomics is one of the most promising new analytical ways of comparing large muscle protein complements and has the potential to decisively improve modern biochemical and biomedical research into neuromuscular disorders.

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“…Due to its more heterogeneous nature, the proteomic profiling of skeletal muscle fibres is still in its infancy, but has already made sub-stantial contributions to our general understanding of basic and applied myology. Recent studies have successfully cataloged the skeletal muscle proteome from various animal species [9][10][11][12][13][14], determined global differences in protein expression between predominantly slow-versus fast-twitching fibres [15][16][17][18], and have identified novel marker proteins of muscle growth [19], myoblast differentiation [20], neonatal fibre necrosis [18], hypertrophy [21], muscular dystrophy [22][23][24][25][26], dysferlinopathy [27], immobilization-induced atrophy [28,29] and ageing-induced sarcopenia [30][31][32][33][34]. In analogy, based on the findings of an initial proteomic analysis of the fast-to-slow fibre transformation process using a conventional nonfluorescent method [35], this report describes the detailed DIGE analysis of the differential expression of the fast skeletal muscle proteome following chronic low-frequency stimulation.…”

Section: Introductionmentioning

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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Proteomic analysis of rat soleus and tibialis anterior muscle following immobilization

Cited by 35 publications

References 17 publications

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Diversity of human skeletal muscle in health and disease: Contribution of proteomics

Proteomic profiling of pathological and aged skeletal muscle fibres by peptide mass fingerprinting (Review)

Proteomic profiling of chronic low‐frequency stimulated fast muscle

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