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In vitro induction and proteomics characterisation of a uranyl–protein interaction network in bovine serum

Authors :
Łukasz Szyrwiel
Ryszard Lobinski
Viktoryia Liauchuk
Laurent Chavatte
Institut des sciences analytiques et de physico-chimie pour l'environnement et les materiaux (IPREM)
Université de Pau et des Pays de l'Adour (UPPA)-Institut de Chimie du CNRS (INC)-Centre National de la Recherche Scientifique (CNRS)
Source :
Metallomics, Metallomics, Royal Society of Chemistry, 2015, 7 (12), pp.1604--1611. ⟨10.1039/c5mt00207a⟩
Publication Year :
2015
Publisher :
Oxford University Press (OUP), 2015.

Abstract

International audience; Uranyl ions (UO2 2+) were shown to interact with a number of foetal serum proteins, leading to the formation of a complex that could be isolated by ultracentrifugation. The molecular weight of the complex was estimated based on size-exclusion chromatography as 650 000 Da. Online ICP AES detection indicated that UO2 2+ in the complex co-eluted with minor amounts of calcium and phosphorous, but not with magnesium. A 1D gel electrophoresis of the U-complex produced more than 10 bands of similar intensity compared with only 2-3 intense bands corresponding to the main serum proteins in the control serum, indicative of the specific interaction of UO2 2+ with minor proteins. A proteomics approach allowed for the identification of 74 proteins in the complex. Analysis of the protein-protein interaction network in the UO2 2+ complex identified 32 proteins responsible for protein-protein complex formation and 34 with demonstrated ion-binding function, suggesting that UO2 2+ stimulates the formation of protein functional networks rather than using a particular molecule as its target. © 2015 The Royal Society of Chemistry.

Details

ISSN :
1756591X and 17565901
Volume :
7
Database :
OpenAIRE
Journal :
Metallomics
Accession number :
edsair.doi.dedup.....1506ccb42e4f63bea4f5ae314f07cc22
Full Text :
https://doi.org/10.1039/c5mt00207a