2001
DOI: 10.1002/1615-9861(200101)1:1<136::aid-prot136>3.3.co;2-t
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The mouse SWISS-2D PAGE database: a tool for proteomics study of diabetes and obesity

Abstract: A number of two-dimensional electrophoresis (2-DE) reference maps from mouse samples have been established and could be accessed through the internet. An up-to-date list can be found in WORLD-2D PAGE (http://www.expasy.ch/ch2d/2d- index.html), an index of 2-DE databases and services. None of them were established from mouse white and brown adipose tissues, pancreatic islets, liver nuclei and skeletal muscle. This publication describes the mouse SWISS-2D PAGE database. Proteins present in samples of mouse (C57B… Show more

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Cited by 39 publications
(74 citation statements)
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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: Introductionsupporting
confidence: 69%
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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: Introductionsupporting
confidence: 69%
“…It is therefore essential to identify reliable skeletal muscle protein markers of fast-toslow muscle transformation, which might be helpful in establishing new molecular indicators of physiological and pathological fibre alterations. Building on previously established 2D skeletal muscle reference maps [10,11], we carried out a comprehensive proteomic profiling of the chronic lowfrequency stimulated rabbit tibialis anterior muscle and determined changes in the expression pattern of key muscle protein species. DIGE analysis and ESI-MS/MS for protein identification and immunoblotting clearly confirmed established changes in representative protein species from distinct functional muscle protein groupings, and uncovered interesting new transformation biomarkers.…”
Section: Discussionmentioning
confidence: 99%
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“…The whole final diluted CSF sample corresponding to 45 g was loaded in a cup at the cathodic end of the immobilized pH gradient (IPG) strips. 2-DE was performed as described previously (10). In brief, the first dimensional protein separation was performed using a commercial 18-cm nonlinear IPG going from pH 3.5 to 10 from Amersham Biosciences (Uppsala, Sweden).…”
Section: Methodsmentioning
confidence: 99%
“…The human pancreas has been explored taking a proteomics approach and a reference map of 302 proteins has been identified. 24 The same has been done in mouse islets, 25 and both of these will provide a useful reference for future proteomics studies of the pancreas in diabetes. Cytokines released from macrophages are known to be toxic to islet β cells, and this is thought to be one of the mechanisms involved in the development of type 1 DM in genetically predisposed individuals.…”
Section: Pancreasmentioning
confidence: 99%