Apoptosis: Involvement of Oxidative Stress and Intracellular by G.M. Salido (auth.), Dr. Gines Maria Salido, Dr. Juan PDF

By G.M. Salido (auth.), Dr. Gines Maria Salido, Dr. Juan Antonio Rosado (eds.)

ISBN-10: 1402098723

ISBN-13: 9781402098727

ISBN-10: 1402098731

ISBN-13: 9781402098734

Apoptosis: Involvement of Oxidative tension 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 function of oxidative rigidity and Ca2+ signalling. specific realization is given to the various positive factors of apoptosis in exact cellphone kinds, starting from hepatocytes to cardiovascular and blood cells, apprehensive cells or spermatozoa.

Cutting-edge and straight forward, this quantity serves as a complete source for these attracted to the interesting organic procedures linked to programmed mobilephone loss of life or apoptosis. The e-book 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 stories awarded, systemically research the main interesting and cutting edge points 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

Example text

At the same time, there is increasing evidence that at the DISC, when present at low concentrations, the isoform c-FLIPL facilitates the cleavage of procaspase 8 by forming a heterodimer with this procaspase (Micheau et al. 2002). The baculoviral p35 protein is a pan-caspase inhibitor that targets most caspases by forming an inhibitory complex with them (Xu et al. 2001). Baculovirus p35 is an effective inhibitor of caspases 1 to 8 (Stennicke et al. 2002). Another pan-caspase inhibitor is ser-pin CrmA, derived from cowpox virus.

FADD binds and activates caspase 8, promoting apoptosis through a pathway similar, though probably not identical, to that triggered by Fas. RIP binds RAIDD, which engages a death pathway by recruitment of caspase 2 through homophilic interaction between homologous sequences in its amino-terminal domain and the prodomain of caspase 2. RIP also associates with TRAF-2, stimulating pro-survival pathways and regulating the immune response. This apoptotic pathway is under the regulatory control of number of gene products.

DED and CARD domains are responsible for the recruitment of initiator caspases into these complexes. This appears to facilitate proteolytic autoactivation of the apical caspases, because “inactive” caspase zymogens possess low but detectable catalytic activity that is sufficient to process other caspases in circumstances where sustained close proximity between the zymogens is achieved (Boatright et al. 2003). The presence of Asp at the maturation cleavage sites is consistent with the ability of caspases to autoactivate or to be activated by other caspases, as part of an amplification cascade.

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Apoptosis: Involvement of Oxidative Stress and Intracellular Ca2+ Homeostasi by G.M. Salido (auth.), Dr. Gines Maria Salido, Dr. Juan Antonio Rosado (eds.)


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