Human stem cell proteome extensively mined

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  • Published: Dec 30, 2014
  • Author: Steve Down
  • Channels: Laboratory Informatics / UV/Vis Spectroscopy / Proteomics / Base Peak / Infrared Spectroscopy / MRI Spectroscopy / X-ray Spectrometry / Chemometrics & Informatics / Atomic / NMR Knowledge Base / Raman

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The most detailed proteomics study to date of the human embryonic stem cell proteome has identified 3184 proteins, including post-translationally modified proteins and known stem cell markers.

The extensive study by scientists in the US, reported in Proteomics, was so successful due to the in-depth pre-fractionation of proteins before the peptide digestion procedure, then the double fractionation of peptides before the mass spectrometric analysis. The fractionation steps increase the number of proteins identified as well as the peptide coverage to increase the confidence in the result.

The identified proteins included 102 secreted proteins. In addition, 491 phosphorylation sites and 68 sites of O-GlcNAc modification were revealed. The results will go some way to help "discover proteomic candidates that are responsible for the maintenance of the undifferentiated cell state and the initial loss of pluripotency."

However, the molecular changes involved in stem cell differentiation can only be discerned by comparing the proteomes of undifferentiated stem cells and those that have transformed into other cell types. This will rely on the ability to quantify the proteins but the scientists proved that this was possible by spectral counting.

Image: Niels Geijsen, Massachusetts General Hospital/National Science Foundation

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