(Q57082822)

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Caspase activation is not death

article by Jean-Luc Perfettini & Guido Kroemer published April 2003 in Nature Immunology

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Caspase activation is not death (English)

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Jean-Luc Perfettini

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Guido Kroemer

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English

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April 2003

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308-310

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Caspase inhibition causes hyperacute tumor necrosis factor-induced shock via oxidative stress and phospholipase A2.

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The mitochondrial death/life regulator in apoptosis and necrosis

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Inhibition of caspases increases the sensitivity of L929 cells to necrosis mediated by tumor necrosis factor.

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Sensitization to death receptor cytotoxicity by inhibition of fas-associated death domain protein (FADD)/caspase signaling. Requirement of cell cycle progression

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Structure/Function analysis of p55 tumor necrosis factor receptor and fas-associated death domain. Effect on necrosis in L929sA cells.

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Fas triggers an alternative, caspase-8-independent cell death pathway using the kinase RIP as effector molecule

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Platelet formation is the consequence of caspase activation within megakaryocytes

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Caspase 3 activity is required for skeletal muscle differentiation

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Specific involvement of caspases in the differentiation of monocytes into macrophages

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Caspase activation is required for T cell proliferation

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10.1038/NI0403-308

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PubMed publication ID

12660728

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