Scientists have used two-dimensional gel electrophoresis in the quantitative analysis of phosphoproteome regulation in prion-infected neuronal cells.
A team including researchers at the Paul Ehrlich Institute in Germany, Paris-Lodron University division of microbiology in Salzburg, Austria and Dundee Cell Products in Scotland worked on the study.
Their findings, published in Cell Communication & Signaling, report the discovery of a differentially regulated phosphoproteome in neuronal cells infected with the abnormal prion protein PrPSc.
PrPSc is the converted form of the cellular prion protein PrPC which, in its abnormal expression, is associated with transmissible spongiform encephalopathies (TSEs).
During their quantitative analysis, the scientists found phosphorylation of cofilin induced in N2a neuronal cells infected with PrPSc.
They suggest this is the first discovery of a differentially regulated phosphoproteome associated with TSEs, opening avenues to further future research.
Cell Communication & Signaling is the Signal Transduction Society's official periodical, carrying research into translational and basic aspects of communications at the cellular level.
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