Analysis of human plasma proteins: a focus on sample collection and separation using free-flow electrophoresis

@article{Nissum2008AnalysisOH,
  title={Analysis of human plasma proteins: a focus on sample collection and separation using free-flow electrophoresis},
  author={Mikkel Nissum and A. F. L. Foucher},
  journal={Expert Review of Proteomics},
  year={2008},
  volume={5},
  pages={571 - 587}
}
Due to ease of accessibility, plasma has become the sample of choice for proteomics studies directed towards biomarker discovery intended for use in diagnostics, prognostics and even in theranostics. The result of these extensive efforts is a long list of potential biomarkers, very few of which have led to clinical utility. Why have so many potential biomarkers failed validation? Herein, we address certain issues encountered, which complicate biomarker discovery efforts originating from plasma… 
View on Taylor & Francis
ncbi.nlm.nih.gov
34 Citations
Background Citations
4
Methods Citations
5
Results Citations
1

34 Citations

Citation Type

Citation Type

Multidimensional protein identification technology for clinical proteomic analysis
TLDR
This review discusses some of the most recent advances in multidimensional peptide separation techniques compatible with MS analysis, including gel electrophoresis, isoelectric focusing, capillary electrophoreis and liquid chromatography techniques.
Biomarkers of HIV-1 associated dementia: proteomic investigation of sera
TLDR
Validation using western-blot analysis led us to conclude that relative change of the levels of these proteins in one patient during a timeframe might be more informative, sensitive and specific than application of average level estimated based on an even larger cohort of patients.
Proteomics for quality-control processes in transfusion medicine
TLDR
Proteomic strategies have been demonstrated to be also suited to verify the effects of the production and pathogen-reduction processes of plasma derivatives and blood components on the protein fractions, or to discover particular biomarkers readily adoptable for targeted evaluation of blood-component integrity or functionality.
Free‐flow electrophoresis in proteome sample preparation
TLDR
Sample preparation by free‐flow electrophoresis mediated particle separation was preferentially performed for purification of either organelles and their subspecies or major protein complexes, where the proteins of interest are originating from, which determine the final composition of a peptide mixture.
Advancing the sensitivity of selected reaction monitoring‐based targeted quantitative proteomics
TLDR
Recent advances in methods and technologies, including front‐end immunoaffinity depletion, fractionation, selective enrichment of target proteins/peptides including posttranslational modifications, as well as advances in MS instrumentation which have significantly enhanced the overall sensitivity of SRM assays and enabled the detection of low‐abundance proteins at low‐ to sub‐ng/mL level in human blood plasma or serum are reviewed.
Use of narrow‐range peptide IEF to improve detection of lung adenocarcinoma markers in plasma and pleural effusion
TLDR
The quantitative results from IEF/LC/MS/MS showed good correlation with the results from Western blot and imunohistochemistry, showing the potential of this methodology in quantitative biomarker discovery studies.
Capture-Layer Lateral Flow Immunoassay: A New Platform Validated in the Detection and Quantification of Dengue NS1
TLDR
This method shows another form of LFIA that has the potential to be quantitative (at least semiquantitative), albeit not solving the reader cost; however, unlike the regular LFIA, this method does not use nanobeads but instead enzymes, allowing, in theory, greater sensitivity, while retaining the one-step procedure.
Proteomic applications in blood transfusion: working the jigsaw puzzle
TLDR
The technology of proteomics and its application to transfusion medicine is reviewed with specific reference to the analysis of blood products, both fractionated and fresh.
Free‐flow electrophoresis in the proteomic era: A technique in flux
TLDR
This review is intended to outline recent innovations, FFE has gained in the proteomic era, and to point out the valuable contributions it has made to the analysis of the proteome of cells, sub‐cellular organelles and functional protein networks.
The use of sigmoid pH gradients in free‐flow isoelectric focusing of human endothelial cell proteins
TLDR
Sigmoid pH gradients were applied to the prefractionation of endothelial cell proteins with the help of this advanced technology and small steps of pH incline between neighboring FFE fractions were established in pH ranges, in which the proteins of interest have their pIs.
...
1
2
3
4
...

References

SHOWING 1-10 OF 153 REFERENCES
Biomarker discovery from the plasma proteome using multidimensional fractionation proteomics.
An investigation of plasma collection, stabilization, and storage procedures for proteomic analysis of clinical samples
TLDR
Inclusion of protease inhibitor cocktail in the sample tubes, provided stable and reliable human plasma samples that yielded reproducible results by proteomic analysis.
HUPO Plasma Proteome Project specimen collection and handling: Towards the standardization of parameters for plasma proteome samples
TLDR
A compendium of observations is presented, drawing on actual results and sound clinical theories and practices, to provide guidance on sample handling issues, with the overall suggestion being to be conscious of all possible pre‐analytical variables as a prerequisite of any proteomic study.
Effects of preanalytical variables on peptide and protein measurements in human serum and plasma: implications for clinical proteomics
TLDR
Preanalytical variables are reviewed, examples for their effects on the determination of distinct peptides and proteins are provided and potential implications for clinical proteomics investigations are discussed.
Human plasma proteome analysis by multidimensional chromatography prefractionation and linear ion trap mass spectrometry identification.
TLDR
Considering the strategy allows high throughput of protein identification in serum, the prefractionation of proteins before MS analysis is a simple and effective method to facilitate human plasma proteome research.
Proteomic Analysis of Colorectal Cancer: Prefractionation Strategies Using two-Dimensional Free-Flow Electrophoresis
TLDR
A proteomics separation tool, which uses a combination of continuous FFE, a liquid-based isoelectric focusing technique, in the first dimension, followed by rapid reversed-phase HPLC in the second dimension, and optimized imaging software to present the FFE/RP-HPLC data in a virtual 2D gel-like format.
Immunoaffinity separation of plasma proteins by IgY microbeads: Meeting the needs of proteomic sample preparation and analysis
TLDR
The efficiency and effectiveness of IgY microbeads in separating 12 abundant proteins from plasma with an immunoaffinity spin column or LC column is described and the high specificity of the protein separation is demonstrated, with removal of 95–99.5% of the abundant proteins.
Utilizing human blood plasma for proteomic biomarker discovery.
TLDR
Continued development of depletion and enrichment techniques, coupled with improved pre-MS separations (both at the protein and peptide level) holds promise in extending the dynamic range of proteomic analysis.
Evaluation of Multiprotein Immunoaffinity Subtraction for Plasma Proteomics and Candidate Biomarker Discovery Using Mass Spectrometry*S
TLDR
A detailed evaluation of immunoaffinity subtraction performed applying the ProteomeLab IgY-12 system that is commonly used in human serum/plasma proteome characterization in combination with high resolution LC-MS/MS suggests that multiprotein immuno Affinity subtracted proteins can be readily integrated into quantitative strategies to enhance detection of low abundance proteins in biomarker discovery studies.
Multi‐component immunoaffinity subtraction chromatography: An innovative step towards a comprehensive survey of the human plasma proteome
TLDR
The immunoaffinity‐based protein subtraction chromatography (IASC) described here removes multiple proteins present in plasma and serum in high concentrations effectively and reproducibly and facilitates automated chromatographic processing of plasma samples in high throughput, desirable in proteomic disease marker discovery projects.
...
1
2
3
4
5
...