Analysis of the plasma proteome using iTRAQ and TMT‐based Isobaric labeling

Over the past decade, chemical labeling with isobaric tandem mass tags, such as isobaric tags for relative and absolute quantification reagents (iTRAQ) and tandem mass tag (TMT) reagents, has been employed in a wide range of different clinically orientated serum and plasma proteomics studies. In thi...

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Bibliographic Details
Published in:Mass spectrometry reviews 2018-09, Vol.37 (5), p.583-606
Main Authors: Moulder, Robert, Bhosale, Santosh D., Goodlett, David R., Lahesmaa, Riitta
Format: Article
Language:English
Subjects:
Autoimmune Diseases - blood
Blood Proteins - analysis
Blood Proteins - chemistry
Blood Proteins - metabolism
Cardiovascular Diseases - blood
Chemical Fractionation - methods
Chromatography, Ion Exchange - methods
disease research
Female
Humans
immunodepletion
Indicators and Reagents
isobaric labeling
Isotope Labeling - methods
Neoplasms - blood
peptide fractionation
plasma
Pregnancy
protein biomarkers
Protein Carbonylation
Protein Processing, Post-Translational
Proteome - analysis
Proteomics
Proteomics - methods
Reproducibility of Results
Tandem Mass Spectrometry - methods
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Summary:Over the past decade, chemical labeling with isobaric tandem mass tags, such as isobaric tags for relative and absolute quantification reagents (iTRAQ) and tandem mass tag (TMT) reagents, has been employed in a wide range of different clinically orientated serum and plasma proteomics studies. In this review the scope of these works is presented with attention to the areas of research, methods employed and performance limitations. These applications have covered a wide range of diseases, disorders and infections, and have implemented a variety of different preparative and mass spectrometric approaches. In contrast to earlier works, which struggled to quantify more than a few hundred proteins, increasingly these studies have provided deeper insight into the plasma proteome extending the numbers of quantified proteins to over a thousand.
ISSN:0277-7037
1098-2787
DOI:10.1002/mas.21550