Title
The use of elemental mass spectrometry in phosphoproteomic applications The use of elemental mass spectrometry in phosphoproteomic applications
Author
Faculty/Department
Faculty of Sciences. Biology
Faculty of Sciences. Chemistry
Publication type
article
Publication
Hoboken :Wiley-blackwell ,
Subject
Chemistry
Biology
Source (journal)
Mass spectrometry reviews. - New York, N.Y., 1982, currens
Volume/pages
35(2016) :3 , p. 350-360
ISSN
0277-7037
ISI
000373733800002
Carrier
E
Target language
English (eng)
Full text (Publishers DOI)
Affiliation
University of Antwerp
Abstract
Reversible phosphorylation is one of the most important post-translational modifications in mammalian cells. Because this molecular switch is an important mechanism that diversifies and regulates proteins in cellular processes, knowledge about the extent and quantity of phosphorylation is very important to understand the complex cellular interplay. Although phosphoproteomics strategies are applied worldwide, they mainly include only molecular mass spectrometry (like MALDI or ESI)-based experiments. Although identification and relative quantification of phosphopeptides is straightforward with these techniques, absolute quantification is more complex and usually requires for specific isotopically phosphopeptide standards. However, the use of elemental mass spectrometry, and in particular inductively coupled plasma mass spectrometry (ICP-MS), in phosphoproteomics-based experiments, allow one to absolutely quantify phosphopeptides. Here, these phosphoproteomic applications with ICP-MS as elemental detector are reviewed. Pioneering work and recent developments in the field are both described. Additionally, the advantage of the parallel use of molecular and elemental mass spectrometry is stressed.
E-info
https://repository.uantwerpen.be/docman/iruaauth/c28756/f50cdf4c567.pdf
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