[Complete information technology blackout in hospitals : Development of a concept for maintaining patient care].

The complete blackout of information technology (IT) in a hospital represents a major incident with acute loss of functionality. The immediate consequence is a rapidly progressive loss of treatment capacity. The major priority for the acute management of such an event is to keep patients safe and prevent life-threatening situations.

Ferritin levels in microglia depend upon activation: modulation by reactive oxygen species.

Iron is one of the trace elements playing a key role in the normal cellular metabolism. Since an excess of free iron is catalyzing the Fenton reaction, most of the intracellular iron is sequestered in the iron storage protein ferritin. The binding of iron into ferritin is well described for physiological conditions, however, under certain pathophysiological situations, the efficiency of this process is unknown.

Oxidation-induced ferritin turnover in microglial cells: role of proteasome.

Highly oxidized protein aggregates accumulating in the brain during neurodegenerative diseases are often surrounded by microglia. Most of the microglial cells surrounding these plaques are activated and release a high amount of oxidizing species. In order to develop their toxic effects numerous oxidizing species need iron.

Ubiquitin conjugation is not required for the degradation of oxidized proteins by proteasome.

Oxidatively modified proteins that accumulate in aging and many diseases can form large aggregates because of covalent cross-linking or increased surface hydrophobicity. Unless repaired or removed from cells, these oxidized proteins are often toxic, and threaten cell viability. Most oxidatively damaged proteins appear to undergo selective proteolysis, primarily by the proteasome.

Proteolytic response to oxidative stress in mammalian cells.

Oxidative stress in mammalian cells is an inevitable consequence of their aerobic metabolism. The production of reactive oxygen and nitric oxide species causes oxidative modifications of proteins often combined with a loss of their biological function. Like most partially denatured proteins, moderately oxidized proteins are more sensitive to proteolytic attack by proteases.