A 2D gel reference map of the basic human heart proteome
UCD Conway Institute of Biomolecular and Biomedical Research, School of Medicine and Medical Science, University College Dublin, Dublin, Ireland. Proteomics
(Impact Factor: 3.81).
09/2011; 11(17):3582-6. DOI: 10.1002/pmic.201000182
We have undertaken the identification of basic proteins (pH 6-11) of the human heart using 2-DE. Tissue from the left ventricle of human heart was lysed and proteins were separated in the first dimension on pH 6-11 IPG strips using paper-bridge loading followed by separation on 12% SDS polyacrylamide gels in the second dimension. Proteins were then identified by mass spectrometry and analysed using Proline, a proteomic data analysis platform that was developed in-house. The proteome map contains 176 identified spots with 151 unique proteins and has been made available as part of the UCD-2DPAGE database at http://proteomics-portal.ucd.ie:8082. The associated mass spectrometry data have been submitted to PRIDE (Accession number ♯10098). This reference map, and the other heart reference maps available through the UCD-2DPAGE database, will aid further proteomic studies of heart diseases such as dilated cardiomyopathy and ischaemic heart disease.
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Available from: Ashling Holland
- "Proteomic methods that involve gel electrophoresis are highly suitable for the analysis of contractile proteins, regulatory proteins, metabolic enzymes, metabolite transporters, and molecular chaperones . Two-dimensional gel electrophoresis can conveniently separate cardiac proteins in the range of approximately 10 kDa to 200 kDa and isoelectric points ranging from pH3 to pH11 [117, 118, 120]. Combinations of isoelectric focusing with narrow- or wide-range immobilised pH gradients, native gel electrophoresis, nonreducing gel electrophoresis, and reducing gel electrophoresis can be used for various two-dimensional applications [137–140]. "
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ABSTRACT: Cardiorespiratory complications are frequent symptoms of Duchenne muscular dystrophy, a neuromuscular disorder caused by primary abnormalities in the dystrophin gene. Loss of cardiac dystrophin initially leads to changes in dystrophin-associated glycoproteins and subsequently triggers secondarily sarcolemmal disintegration, fibre necrosis, fibrosis, fatty tissue replacement, and interstitial inflammation. This results in progressive cardiac disease, which is the cause of death in a considerable number of patients afflicted with X-linked muscular dystrophy. In order to better define the molecular pathogenesis of this type of cardiomyopathy, several studies have applied mass spectrometry-based proteomics to determine proteome-wide alterations in dystrophinopathy-associated cardiomyopathy. Proteomic studies included both gel-based and label-free mass spectrometric surveys of dystrophin-deficient heart muscle from the established mdx animal model of dystrophinopathy. Comparative cardiac proteomics revealed novel changes in proteins associated with mitochondrial energy metabolism, glycolysis, signaling, iron binding, antibody response, fibre contraction, basal lamina stabilisation, and cytoskeletal organisation. This review summarizes the importance of studying cardiomyopathy within the field of muscular dystrophy research, outlines key features of the mdx heart and its suitability as a model system for studying cardiac pathogenesis, and discusses the impact of recent proteomic findings for exploring molecular and cellular aspects of cardiac abnormalities in inherited muscular dystrophies.
03/2014; 2014(6):246195. DOI:10.1155/2014/246195
Available from: Yueshuai Guo
- "Recently, the Human Proteome Organization (HUPO) launched the Human Proteome Project (HPP), which generated a map of all the proteins in human tissue, both in normal and disease states . The protein map of several human tissues was characterized, including brain , heart  , kidney , pancreas  , liver  , and plasma   . Over 1000 human testicular proteins have been identified using 2DE combined with MS or 1D SDS-PAGE combined with LC   . "
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ABSTRACT: The testes are where spermatogenesis, the sperm-generating process that is unique to men, occurs. Importantly, human spermatogenesis and tumorigenesis share key similarities. Until now, only a few proteins in the human testis have been identified due to limitations of available technology. In this paper, using an advanced proteomics platform, we have identified 7346 unique proteins within the human testis with a high degree of confidence. Immunohistochemistry data from the Human Protein Atlas database show over 90% (1833/2020) of identified proteins can be detected in the human testis using specific antibodies. To make the data widely available to the scientific community, an online Human Testis Proteome Database (HTPD, http://reprod.njmu.edu.cn/htpd/) was built. Many of the identified human testicular proteins are associated with human infertility, especially human testicular predominantly expressed proteins. We characterized six novel cancer/testis genes (TMPRSS12, TPPP2, PRSS55, DMRT1, PIWIL1, HEMGN), which map to cancer-associated genetic variants positions, in both the cancer and testis tissues using genome-wide analyses. Our results provide a molecular connection between spermatogenesis and tumorigenesis and broaden the range of cancer antigen choice available for immunotherapy.
Proteomics 02/2013; 13(7). DOI:10.1002/pmic.201200489 · 3.81 Impact Factor
Available from: Donglei Du
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ABSTRACT: Most protein PageRank studies do not use signal flow direction information in protein interactions because this information was not readily available in large protein databases until recently. Therefore, four questions have yet to be answered: A) What is the general difference between signal emitting and receiving in a protein interactome? B) Which proteins are among the top ranked in directional ranking? C) Are high ranked proteins more evolutionarily conserved than low ranked ones? D) Do proteins with similar ranking tend to have similar subcellular locations? In this study, we address these questions using the forward, reverse, and non-directional PageRank approaches to rank an information-directional network of human proteins and study their evolutionary conservation. The forward ranking gives credit to information receivers, reverse ranking to information emitters, and non-directional ranking mainly to the number of interactions. The protein lists generated by the forward and non-directional rankings are highly correlated, but those by the reverse and non-directional rankings are not. The results suggest that the signal emitting/receiving system is characterized by key-emittings and relatively even receivings in the human protein interactome. Signaling pathway proteins are frequent in top ranked ones. Eight proteins are both informational top emitters and top receivers. Top ranked proteins, except a few species-related novel-function ones, are evolutionarily well conserved. Protein-subunit ranking position reflects subunit function. These results demonstrate the usefulness of different PageRank approaches in characterizing protein networks and provide insights to protein interaction in the cell.
PLoS ONE 09/2012; 7(9):e44872. DOI:10.1371/journal.pone.0044872 · 3.23 Impact Factor
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