Download e-book for kindle: Apoptosis : physiology and pathology by Douglas R. Green, John C. Reed

By Douglas R. Green, John C. Reed

ISBN-10: 0521886562

ISBN-13: 9780521886567

"Apoptosis, or telephone loss of life, may be pathological, an indication of sickness and harm, or physiological, a technique crucial for regular well-being. This pathological dysregulation of mobile demise should be characterised through both an excessive amount of lack of crucial cells within the middle, mind, and different tissues with little regenerative potential or by way of too little mobilephone turnover in self-renewing tissues, giving upward thrust to melanoma and different maladies. Read more...

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Extra resources for Apoptosis : physiology and pathology

Sample text

Binding of CD95 or TRAIL to their respective receptors leads to receptor trimerization and formation of the death-inducing signaling complex (DISC). The adaptor protein FADD is recruited to the DISC where the death domains (DD) of both proteins interact. Subsequently, procaspases 8 and 10 are recruited to the protein complex where they interact with FADD via the death effector domains (DEDs). cFLIP can compete with caspase-8 for the binding to FADD. Therefore, high levels of cFLIP can abrogate caspase-8 activation at the DISC.

1997). Subsequently, CD95L was also found to be responsible for the long-known perforin-independent killing activity of CD8+ cytotoxic T cells. Thus the CD95 system does not only play a role in the homeostatic regulation of the immune system, but is also employed in the defense mechanisms used by the immune system to fight infection. When research into the CD95/CD95L system began, it was hoped that agonists of CD95 would hold the promise that TNF unfortunately could not keep as a result of the detrimental effects associated with its systemic application.

Interactions with SMAC/Diablo and/or HtrA2/Omi can prevent IAP-mediated inhibition of caspases. N-terminal IBMs have been identified that seem to primarily target BIR2 of XIAP, including Nipsnap (Nsp) 3 and 4, glutamate dehydrogenase (GdH), leucine-rich pentatricopeptide (LRPPR), and 3-hydroxyisobutyrate dehydrogenase (3HB) and other proteins. Several of these proteins (GdH, Nsp4, and LRPPR) have been shown to antagonize XIAP inhibition of caspases-3 in vitro, although not as potently as SMAC. The importance of these other IBM-containing proteins requires additional experimentation.

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Apoptosis : physiology and pathology by Douglas R. Green, John C. Reed

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