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Download PDF by McAdie A.: A New Thermometer Scale (1916)(en)(3s)

By McAdie A.

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Studies conducted over the past two decades have revealed a complex web of molecules that execute and regulate apoptosis. Interestingly, during recent years, a paradigm shift has occurred as it becomes clear that proteins involved in apoptosis also exhibit cell death-unrelated functions (Galluzzi et al. 2008). Indeed, it seems plausible that evolution has not “invented” proapoptotic factors ex nihilo but rather has “appropriated” molecules that already had a function in vital processes (such as adaptation to stress) into the service of programmed cell death.

Indeed, it seems plausible that evolution has not “invented” proapoptotic factors ex nihilo but rather has “appropriated” molecules that already had a function in vital processes (such as adaptation to stress) into the service of programmed cell death. At the proteome level, most of the ultrastructural features of apoptosis are the consequence of hundreds of proteins undergoing restricted proteolysis during the so-called effector phase. However, up-to-date the relevance of the majority of these proteolytic events remains unclear.

Keeping in mind that the ultimate fate of the cell depends upon the cell context, simultaneous signalling events, and other stimuli, death receptors may be particularly important in immune regulation and tissue injury in disease states. For these reasons, they have already been targeted for the treatment of several human inflammatory and autoimmune diseases. Purposeful induction of apoptosis by death receptors may ultimately be useful also in cancer therapy. Nevertheless, much remains to be learned about the complexity of death-receptor signalling, both, in health and disease.

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