By G.M. Salido (auth.), Dr. Gines Maria Salido, Dr. Juan Antonio Rosado (eds.)
Apoptosis: Involvement of Oxidative pressure and Intracellular Ca2+ Homeostasis
Apoptosis: Involvement of Oxidative pressure and Intracellular Ca2+ Homeostasis, offers a concise synthesis of the present wisdom and up to date advances within the mechanisms of apoptosis in several cells and the position of oxidative tension and Ca2+ signalling. specific recognition is given to the various positive aspects of apoptosis in designated telephone kinds, starting from hepatocytes to cardiovascular and blood cells, worried cells or spermatozoa.
Cutting-edge and common, this quantity serves as a finished source for these drawn to the interesting organic methods linked to programmed telephone dying or apoptosis. The ebook is split in significant bankruptcy sections: basic mechanisms of the apoptotic pathways and the function of oxidative pressure and intracellular Ca2+ homeostasis and a extra particular part devoted to the specificities of apoptosis in a few excitable and non-excitable cells.
All of the contributions are from experts within the box and the experiences offered, systemically learn the main intriguing and cutting edge elements of the apoptotic pathways of their specific parts of expertise.
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Extra info for Apoptosis: Involvement of Oxidative Stress and Intracellular Ca2+ Homeostasi
However, the cytosolic amino-terminus is considerably shorter and not conserved among species. The biological active form of TRAIL is a homotrimer. TRAIL seems to trigger apoptosis more specifically in tumour cell lines rather than in normal cells, although the reason for this differential sensitivity has not yet been explained. Like Fas, activated TRAIL-R1 and TRAIL-R2 recruit FADD and caspase 8 and caspase 10 to their respective DISCs, and they seem to trigger apoptosis through a pathway similar to that activated by Fas (Peter 2000).
Similarly, the large and small catalytic subunits, p20 and p10 are separated via a second cleavage event at an Asp-X bond between these two domains (Fuentes-Prior and Salvesen 2004; Riedl and Shi 2004). , caspase 3, 6, and 7, are activated by proteolytic processing by other caspases or granzyme B (Degterev et al. 2003; Fuentes-Prior and Salvesen 2004). Short prodomain caspases absolutely require processing for activation whereas caspase 9 and other caspases with long prodomains can have significant activity even in the unprocessed state (Stennicke et al.
Furthermore, a “calpain-cathepsin cascade” (Yamashima 2004) has also been proposed to integrate and enhance proteolytic activity during apoptosis. Finally, it has been described that DNA damage may also signal through the activation of caspase 2. The molecular mechanism of procaspase 2 activation in the course of apoptosis remains poorly defined. Some reports suggest that caspase 2 is implicated in cytochrome c release and is essential for drug-induced apoptosis in several human cell lines (Guo et al.