BCL-2, BCL-XL Sequester BH3 Domain-Only Molecules Preventing BAX- and BAK-Mediated Mitochondrial Apoptosis
Emily H. Cheng,Michael C. Wei,Solly Weiler,Richard A. Flavell,Tak W. Mak,Tullia Lindsten,Stanley J. Korsmeyer +6 more
TL;DR: In mammals, BH3 domain-only molecules activate multidomain proapoptotic members to trigger a mitochondrial pathway, which both releases cytochrome c to activate caspases and initiates caspase-independent mitochondrial dysfunction.
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About: This article is published in Molecular Cell. The article was published on 01 Sep 2001. and is currently open access. The article focuses on the topics: Mitochondrial apoptosis-induced channel & Bcl-2-associated X protein.
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Citations
Role of Bim in apoptosis induced in H460 lung tumor cells by the spindle poison Combretastatin-A4
TL;DR: It is demonstrated that Bim is required for the CA-4-induced cell death in the H460 lung cancer cell line via activation of the mitochondrial signalling pathway, underlining the relevance of the cytoskeleton integrity in the apoptotic response.
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Maintenance of the relative proportion of oligodendrocytes to axons even in the absence of BAX and BAK
Kumi Kawai,Takayuki Itoh,Takayuki Itoh,Aki Itoh,Aki Itoh,Makoto Horiuchi,Makoto Horiuchi,Kouji Wakayama,Kouji Wakayama,Peter Bannerman,Peter Bannerman,James Y. Garbern,David E Pleasure,David E Pleasure,Tullia Lindsten +14 more
TL;DR: This study indicates that homeostatic control of cell number is different for progenitors of the oligodendroglial and neuronal lineages and regulatory mechanism(s) operating in addition to apoptotic elimination through the intrinsic pathway, appear to prevent the overproduction of highly mitotic oligod endodendrocytes and progenitor cells.
Significant coexpression of GLUT-1, Bcl-xL, and Bax in colorectal cancer.
Andrzej Wincewicz,Mariola Sulkowska,Mariusz Koda,Luiza Kanczuga-Koda,Ewa Witkowska,Stanislaw Sulkowski +5 more
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Gasdermins in Apoptosis: New players in an Old Game.
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TL;DR: New evidence suggests that members of the gasdermin superfamily are novel pore-forming proteins that augment apoptosis by permeabilizing the mitochondria and participate in the final stages of the apoptotic program by inducing secondary necrosis/pyroptosis.
RU486, a glucocorticoid receptor antagonist, induces apoptosis in U937 human lymphoma cells through reduction in mitochondrial membrane potential and activation of p38 MAPK
Ji Hoon Jang,Seon Min Woo,Hee Jung Um,Eun-Jung Park,Kyoung-jin Min,Tae-Jin Lee,Sang-Hyun Kim,Yung Hyun Choi,Taeg Kyu Kwon +8 more
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References
Mitochondria and apoptosis
Douglas R. Green,John C. Reed +1 more
TL;DR: A variety of key events in apoptosis focus on mitochondria, including the release of caspase activators (such as cytochrome c), changes in electron transport, loss of mitochondrial transmembrane potential, altered cellular oxidation-reduction, and participation of pro- and antiapoptotic Bcl-2 family proteins.
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Cytochrome c and dATP-Dependent Formation of Apaf-1/Caspase-9 Complex Initiates an Apoptotic Protease Cascade
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TL;DR: Mutation of the active site of caspase-9 attenuated the activation of cazase-3 and cellular apoptotic response in vivo, indicating that casp enzyme-9 is the most upstream member of the apoptotic protease cascade that is triggered by cytochrome c and dATP.
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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
TL;DR: Overexpressed Bax accelerates apoptotic death induced by cytokine deprivation in an IL-3-dependent cell line and counters the death repressor activity of B cl-2, suggesting a model in which the ratio of Bcl-2 to Bax determines survival or death following an apoptotic stimulus.
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Bid, a Bcl2 Interacting Protein, Mediates Cytochrome c Release from Mitochondria in Response to Activation of Cell Surface Death Receptors
TL;DR: The purification of a cytosolic protein that induces cytochrome c release from mitochondria in response to caspase-8, the apical caspases activated by cell surface death receptors such as Fas and TNF is reported.
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Apaf-1, a Human Protein Homologous to C. elegans CED-4, Participates in Cytochrome c–Dependent Activation of Caspase-3
TL;DR: The purification and cDNA cloning of Apaf-1, a novel 130 kd protein from HeLa cell cytosol that participates in the cytochrome c-dependent activation of caspase-3, leading to apoptosis is reported here.
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