Berthold Lumat Lb 9507 Manual Treadmill

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During cellular evolution, eukaryotic cells have developed mechanisms to cope with environmental challenges. The expression of heat shock proteins (Hsps) is one of the essential stress reactions of cells. The 70-kD protein, Hsp70, with its indispensable role in maintaining cellular homeostasis, is the most prominent molecular chaperone and has been investigated extensively among the Hsp family (). Its sequence homology between prokaryotic version DnaK and human is ∼60%, expressing the remarkable conservation of this protein in such a highly diverse organism (). A variety of environmental and cellular stress conditions are able to induce the Hsp70 response, including bacterial infections (), isolation stress (), immunotoxic effects (, ), DNA damaging through oxidative stress (), noise overstimulation (), or the classically defined stress response to hyperthermia (). The characteristic role of Hsp70 is to prevent cell death by interfering with the ability of cytochrome c and apoptotic protease-activating factor 1 to recruit procaspase-9, which leads to suppression of apoptosis by blocking the assembly of a functional apoptosome (). Many of these stress triggers have an impact on energy metabolism caused by ATP-consuming protein-protein interactions of Hsp70 serving as a molecular chaperone ().