A human myocardial two‐dimensional electrophoresis database: Protein characterisation by microsequencing and immunoblotting

Baker, Cathy S.; Corbett, Joseph M.; May, Andrew J.; Yacoub, Magdi H.; Dünn, Michael J.

doi:10.1002/elps.11501301154

Cited by 58 publications

(21 citation statements)

References 8 publications

(4 reference statements)

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“…In this paper we have presented an update to the 2-D gel protein database of human myocardial protein originally published in 1992 [9]. The database now contains 1388 protein spots which have been characterised in terms of their apparent p l and MI values.…”

Section: Discussionmentioning

confidence: 98%

The human myocardial two‐dimensional gel protein database: Update 1994

et al. 1994

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An updated human heart protein two-dimensional electrophoresis (2-DE) database is presented. The database, which contains some 1388 protein spots characterised in terms of M(r) and pI, has been analysed further by Western immunoblotting and protein sequencing. From a total of 103 protein spots analysed, 49 have been identified by immunoblotting and 32 have been identified by protein sequencing. A further six proteins have tentatively been assigned by comparison with the human heart 2-DE protein database of Jungblut et al. (Electrophoresis) 1994, 15, 685-607). This database is being used in studies of alterations in protein expression in the diseased and transplanted human heart.

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Section: Discussionmentioning

confidence: 98%

The human myocardial two‐dimensional gel protein database: Update 1994

et al. 1994

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“…Human myocardial proteins were identified by 2-DE [102][103][104][105]. After spot identification of the variant proteins by nanospray-MS and MS/MS human heart 2-DE-databases and that of dilated cardiomyopathy were constructed [103,[106][107][108][109][110].…”

Section: Examples Of Successful Application Of Proteomicsmentioning

confidence: 99%

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

2006

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The proteome analysis by 2-DE is one of the most potent methods of analyzing the complete proteome of cells, cell lines, organs and tissues in proteomics studies. It allows a fast overview of changes in cell processes by analysis of the entire protein extracts in any biological and medical research projects. New instrumentation and advanced technologies provide proteomics studies in a wide variety of biological and biomedical questions. Proteomics work is being applied to study antibiotics-resistant strains and human tissues of various brain, lung, and heart diseases. It cumulated in the identification of antigens for the design of new vaccines. These advances in proteomics have been possible through the development of advanced high-resolution 2-DE systems allowing resolution of up to 10 000 protein spots of entire cell lysates in combination with protein identification by new highly sensitive mass spectrometric techniques. The present technological achievements are suited for a high throughput screening of different cell situations. Proteomics may be used to investigate the health effects of radiation and electromagnetic field to clarify possible dangerous alterations in human beings.

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“…Pioneering proteomic work by the laboratories of Dunn and Jungblut led to the creation of numerous online 2-D databases of human, dog, mouse, and rat myocardium. [65][66][67][68][69][70][71][72][73][74][75] They are only partially complete (with roughly 200 proteins identified), but they provide a foundation for the inventory of these particular tissues. These freely accessible works in progress are tremendously important, because they provide researchers with a basis for visualization of changes in protein patterns resulting from the conditions of their particular study.…”

Section: Traditional Proteomics: Creation Of Protein Inventoriesmentioning

confidence: 99%

Cardiovascular Proteomics

Arrell

Neverova

Eyk

2001

Circulation Research

156

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Abstract-The development of proteomics is a timely one for cardiovascular research. Analyses at the organ, subcellular, and molecular levels have revealed dynamic, complex, and subtle intracellular processes associated with heart and vascular disease. The power and flexibility of proteomic analyses, which facilitate protein separation, identification, and characterization, should hasten our understanding of these processes at the protein level. Properly applied, proteomics provides researchers with cellular protein "inventories" at specific moments in time, making it ideal for documenting protein modification due to a particular disease, condition, or treatment. This is accomplished through the establishment of species-and tissue-specific protein databases, providing a foundation for subsequent proteomic studies. Evolution of proteomic techniques has permitted more thorough investigation into molecular mechanisms underlying cardiovascular disease, facilitating identification not only of modified proteins but also of the nature of their modification. Continued development should lead to functional proteomic studies, in which identification of protein modification, in conjunction with functional data from established biochemical and physiological methods, has the ability to further our understanding of the interplay between proteome change and cardiovascular disease.

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A human myocardial two‐dimensional electrophoresis database: Protein characterisation by microsequencing and immunoblotting

Cited by 58 publications

References 8 publications

The human myocardial two‐dimensional gel protein database: Update 1994

The human myocardial two‐dimensional gel protein database: Update 1994

Two‐dimensional gel electrophoresis as tool for proteomics studies in combination with protein identification by mass spectrometry

Cardiovascular Proteomics

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