Cardiovascular Proteomics

Arrell, D. Kent; Neverova, Irina; Eyk, Jennifer E. Van

doi:10.1161/hh0801.090193

Cited by 156 publications

(64 citation statements)

References 114 publications

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“…Interestingly, we were able to separate and identify several different forms of histones: H2B, H4 and H2A.z, H2A.1b and H3.1 by np-RP HPLC. Similar to membrane proteins, histones have a very basic pI (around [10][11][12] and are difficult to separate and analyze by gel electrophoresis. Proteins from the ribosomal membrane were also largely represented due to their very high abundance within the sample.…”

Section: Separation and Characterization Of Bovine Endothelial Membramentioning

confidence: 99%

Protein Separation and Characterization by np-RP−HPLC Followed by Intact MALDI-TOF Mass Spectrometry and Peptide Mass Mapping Analyses

et al. 2006

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Due to their complexity, the separation of intact proteins from complex mixtures is an important step to comparative proteomics and the identification and characterization of the proteins by mass spectrometry (MS). In the study reported, we evaluated the use of non-porous-reversed-phase (np-RP) HPLC for intact protein separation prior to MS analyses. The separation system was characterized and compared to 1D-SDS-PAGE electrophoresis in terms of resolution and sensitivity. We demonstrate that np-RP HPLC protein separation is highly reproducible and provides intact protein fractions which can be directly analyzed by MALDI-TOF MS for intact molecular weight determination. An in-well digestion protocol was developed, allowing for rapid protein identification by peptide mass fingerprinting (PMF) and resulted in comparable or improved peptide recovery compared with in-gel digestion. The np-RP sensitivity of detection by UV absorbance at 214 nm for intact proteins was at the low ng level and the sensitivity of peptide analysis by MALDI-TOF MS was in the 10-50 pg level. A membrane protein fraction was characterized to demonstrate application of this methodology. Among the identified proteins, multiple forms of vimentin were observed. Overall we demonstrate that np-RP HPLC followed by MALDI-TOF MS allows for rapid, sensitive and reproducible protein fractionation and very specific protein characterization by integration of PMF analysis with MS intact molecular weight information. Keywordsnon-porous reversed phase HPLC; protein liquid chromatography; peptide mass fingerprint; intact protein mass spectrometry

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Section: Separation and Characterization Of Bovine Endothelial Membramentioning

confidence: 99%

Protein Separation and Characterization by np-RP−HPLC Followed by Intact MALDI-TOF Mass Spectrometry and Peptide Mass Mapping Analyses

et al. 2006

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“…In terms of class (iv) proteins (energetic metabolism proteins), PBMC of CHF patients showed induction of NADH-ubiquinone oxidoreductase, and a downregulation of Nucleoside diphosphate kinase A, a protein with a major role in the synthesis of nucleotide triphosphates other than ATP. Interestingly, both these enzymes were also found to undergo changes in an "in vitro" model of hypertrophic cardiomyopathy [30]. However, in the latter study, opposite changes in the proteins were detected.…”

Section: Discussionmentioning

confidence: 68%

Using peripheral blood mononuclear cells to determine proteome profiles in human cardiac failure

Mazzola

Cianti

Bini

et al. 2008

European J of Heart Fail

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Background: In chronic heart failure (CHF), peripheral blood mononuclear cells (PBMC) might undergo structural and/or functional alterations as a consequence of the development and progression of the disease. Aims: This study was aimed at: (1) assessing the proteome profile of PBMC from Controls and CHF subjects, (2) identifying differentiallyexpressed proteins in healthy subjects and patients, and (3) analysing the expression of these proteins in patients after heart transplantation. Methods and results: Proteome changes were assessed in PBMC from 8 healthy and 11 end-stage CHF (6 Ischaemic Heart Failure [IHF], 5 Dilated CardioMyopathy [DCM]) subjects by gel electrophoresis, PD-Quest analysis and mass spectrometry. Eighteen proteins were differentially expressed in Controls and CHF patients. However, among CHF patients, these proteins were equally expressed in IHF and DCM subjects. Eleven proteins were found to belong to 4 functional classes (3 cytoskeletal, 4 cell-cycle progression, 2 stress response and DNA repair, 2 energetic metabolism proteins). Changes in three of the differentially-expressed proteins were also confirmed by Western blot and were reversed after heart transplantation. Conclusion: Results demonstrate an altered protein expression profile in PBMC of CHF patients compared to Controls, thus providing a basis for further diagnostic and prognostic tests for CHF.

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“…Proteomics: Novel technological approaches, such as highthroughput proteomics, now allow for direct evaluation of large-scale protein profiles and identification of differentially expressed proteins (ARRELL et al, 2001), contributing to our understanding of disease mechanisms and aiding the discovery of potential therapeutic targets. Our group has recently described an inventory of myocardial proteins from patients with severe CCC.…”

Section: Inflammation and The Role Of Cytokinesmentioning

confidence: 99%

Chagas disease cardiomyopathy: current concepts of an old disease

Bilate¹,

Cunha‐Neto

2008

Rev. Inst. Med. trop. S. Paulo

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SUMMARYChagas disease continues to be a significant public health problem, as ca. 10 million people are still infected with T. cruzi in Latin America. Decades after primary infection, 30% of individuals can develop a form of chronic inflammatory cardiomyopathy known as Chagas disease cardiomyopathy (CCC). Data from both murine models and human studies support the view that an autoimmune response as well as a parasite-driven immune response involving inflammatory cytokines and chemokines may both play a role in generating the heart lesions leading to CCC. This review aims to summarize recent advances in the understanding of the immunopathogenesis of Chagas disease cardiomyopathy.

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Cardiovascular Proteomics

Cited by 156 publications

References 114 publications

Protein Separation and Characterization by np-RP−HPLC Followed by Intact MALDI-TOF Mass Spectrometry and Peptide Mass Mapping Analyses

Protein Separation and Characterization by np-RP−HPLC Followed by Intact MALDI-TOF Mass Spectrometry and Peptide Mass Mapping Analyses

Using peripheral blood mononuclear cells to determine proteome profiles in human cardiac failure

Chagas disease cardiomyopathy: current concepts of an old disease

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