Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs.

Détails

ID Serval
serval:BIB_7430159478AC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Quantitative proteomics of heat-treated human cells show an across-the-board mild depletion of housekeeping proteins to massively accumulate few HSPs.
Périodique
Cell Stress and Chaperones
Auteur(s)
Finka A., Sood V., Quadroni M., Rios Pde L, Goloubinoff P.
ISSN
1466-1268 (Electronic)
ISSN-L
1355-8145
Statut éditorial
Publié
Date de publication
2015
Peer-reviewed
Oui
Volume
20
Numéro
4
Pages
605-620
Langue
anglais
Notes
Publication types: Journal Article
Publication Status: ppublish
Résumé
Classic semiquantitative proteomic methods have shown that all organisms respond to a mild heat shock by an apparent massive accumulation of a small set of proteins, named heat-shock proteins (HSPs) and a concomitant slowing down in the synthesis of the other proteins. Yet unexplained, the increased levels of HSP messenger RNAs (mRNAs) may exceed 100 times the ensuing relative levels of HSP proteins. We used here high-throughput quantitative proteomics and targeted mRNA quantification to estimate in human cell cultures the mass and copy numbers of the most abundant proteins that become significantly accumulated, depleted, or unchanged during and following 4 h at 41 °C, which we define as mild heat shock. This treatment caused a minor across-the-board mass loss in many housekeeping proteins, which was matched by a mass gain in a few HSPs, predominantly cytosolic HSPCs (HSP90s) and HSPA8 (HSC70). As the mRNAs of the heat-depleted proteins were not significantly degraded and less ribosomes were recruited by excess new HSP mRNAs, the mild depletion of the many housekeeping proteins during heat shock was attributed to their slower replenishment. This differential protein expression pattern was reproduced by isothermal treatments with Hsp90 inhibitors. Unexpectedly, heat-treated cells accumulated 55 times more new molecules of HSPA8 (HSC70) than of the acknowledged heat-inducible isoform HSPA1A (HSP70), implying that when expressed as net copy number differences, rather than as mere "fold change" ratios, new biologically relevant information can be extracted from quantitative proteomic data. Raw data are available via ProteomeXchange with identifier PXD001666.
Mots-clé
hsp70, Hsc70, Hsp90, Molecular chaperone, Heat shock, Jurkat cells
Pubmed
Web of science
Open Access
Oui
Création de la notice
29/06/2015 11:16
Dernière modification de la notice
20/08/2019 15:31
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