What's news: Comprehensive computerized 2d gel protein databases offer a global approach to the study of the mammalian cell

Celis, Julio E.; Honoré, Bent; Bauw, Guy; Vandekerckhove, Joël

doi:10.1002/bies.950120209

Cited by 16 publications

(5 citation statements)

References 26 publications

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“…Initial proteomics data should be confirmed by peptide sequencing, immunoblotting and/or immunofluorescence microscopy in order to establish a new cohort of potential disease marker proteins. For comparative searches, the existence of international data banks with standardized 2-D gel patterns of all major organ and tissue systems from established animal models can greatly simplify the identification of a new disease marker [45,46]. Once interesting candidate proteins have been found by animal model proteomics, an informed decision can be made on the optimum design of subsequent clinical studies.…”

Section: Animal Model Proteomicsmentioning

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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Section: Animal Model Proteomicsmentioning

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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“…Comparative proteomics is concerned with the qualitative and quantitative comparison of entire protein complements under varying biological conditions (7). Skeletal muscle proteomics in particular involves the global biochemical analysis of protein expression patterns in contractile fibres using standard techniques to separate and characterise muscle proteins, and then identify these protein species by interlinking with 2-D gel electrophoretic databanks and/or protein sequence databanks (32,33). The skeletal muscle proteome is defined as the protein complement expressed by a given muscle fibre genome (26).…”

Section: Mass Spectrometry-based Proteomicsmentioning

confidence: 99%

“…These well-established biochemical techniques are very reliable and routinely used in the initial screening procedure of proteins or employed in the confirmation of MALDI-ToF MS-generated lists of identified protein candidates. In addition, although not as reliable as direct peptide sequencing or ESI-MS/MS analysis, the simple comparison of the relatively unique combination of the isoelectric point and relative molecular mass of a particular 2-D protein spot with existing 2-D protein databanks can be employed to identify a protein (32). If the pI-value and the molecular mass of an unknown protein result in a positive hit in a tissue-specific databank, such as the SWISS-2DPAGE database (33), it is highly recommended that these findings be confirmed by immunoblotting.…”

Section: Mass Spectrometry-based 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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“…In this way, it is possible to create 2D databases. The first for human cells included databases for transformed epithelial amnion cells, peripheral blood mononuclear cells, and embryonic lung MRC‐5 fibroblasts13–15, and 2D databases of a number of specific human tissue types and tumours have subsequently been developed. One of the best established is the SWISS‐2D database, which was begun in 199316.…”

Section: Proteomics Techniquesmentioning

confidence: 99%

Proteomics: a new approach to the study of disease

et al. 2000

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The global analysis of cellular proteins has recently been termed proteomics and is a key area of research that is developing in the post-genome era. Proteomics uses a combination of sophisticated techniques including two-dimensional (2D) gel electrophoresis, image analysis, mass spectrometry, amino acid sequencing, and bio-informatics to resolve comprehensively, to quantify, and to characterize proteins. The application of proteomics provides major opportunities to elucidate disease mechanisms and to identify new diagnostic markers and therapeutic targets. This review aims to explain briefly the background to proteomics and then to outline proteomic techniques. Applications to the study of human disease conditions ranging from cancer to infectious diseases are reviewed. Finally, possible future advances are briefly considered, especially those which may lead to faster sample throughput and increased sensitivity for the detection of individual proteins.

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What's news: Comprehensive computerized 2d gel protein databases offer a global approach to the study of the mammalian cell

Cited by 16 publications

References 26 publications

Proteomic profiling of animal models mimicking skeletal muscle disorders

Proteomic profiling of animal models mimicking skeletal muscle disorders

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

Proteomics: a new approach to the study of disease

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