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Proteomic analysis of oxidative stress after nanoparticle treatment in cell culture to study cytotoxicity mechanisms

Project

Food and consumer protection

This project contributes to the research aim 'Food and consumer protection'. Which funding institutions are active for this aim? What are the sub-aims? Take a look:
Food and consumer protection


Project code: BfR-PRS-08-1322-421
Contract period: 01.01.2009 - 31.12.2010
Purpose of research: Applied research

Increasing numbers of products furnished with nanoparticles require careful analysis of possible adverse health effects in humans (consumers and workers). By reducing particle size toward nanoscale ranges novel and partially unexpected physicochemical properties appear. Sometimes such properties are of advantage and favor, thus explaining the increasing abundance of nanoparticels in products at the market. Such new features also hamper toxicological assessment though. It is not possible to predict the behavior of nanoparticles based on properties of the corresponding bulk material. In addition nanoparticles might interfere with standard toxicological tests which represents another major drawback. Currently there are many data gaps and thus reliable risk assessments are impossible.In cell culture experiments with several cell lines it could be shown that nanoparticles cause cytotoxic effects. To explain the cytotoxicity of different kinds of nanoparticles a generally accepted paradigm is the generation of oxidative stress. This is also assumed to occur with regard to toxicity of ultrafine particles in urban air.Oxidative stress results from an imbalance between formation and elimination of reactive oxygen and nitrogen species (ROS/RNS) and is involved in normal aging processes as well as in pathogenesis of many acute and chronic diseases. Due to their high reactivity, quantification of ROS via stable cellular follow-up products is more amenable compared to direct measurement of these short-lived species. Cellular proteins can scavenge up to 50-70% of ROS. This suggests that the detection of oxidatively modified proteins can serve as a reli-able indicator for oxidative stress via ROS. The most common modifications are oxidations in Cys/Met side chains and the formation of protein carbonyls. Protein carbonyls are products of an irreversible modification and usually accompanied by the loss of protein function.

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Subjects

Framework programme

BMEL Frameworkprogramme 2008

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