scholarly journals [Retracted] Metabolic remodeling precedes mitochondrial outer membrane permeabilization in human glioma xenograft cells

2021 ◽  
Vol 58 (5) ◽  
Author(s):  
Shivani Ponnala ◽  
Chandramu Chetty ◽  
Krishna Veeravalli ◽  
Dzung Dinh ◽  
Jeffrey Klopfenstein ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Membrane Permeabilization ◽  
Mitochondrial Outer Membrane ◽  
Human Glioma ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
Metabolic Remodeling ◽  
Glioma Xenograft

scholarly journals Modulation of Mitochondrial Outer Membrane Permeabilization and Apoptosis by Ceramide Metabolism

PLoS ONE ◽  
2012 ◽  
Vol 7 (11) ◽  
pp. e48571 ◽  
Author(s):  
António Rego ◽  
Margarida Costa ◽  
Susana Rodrigues Chaves ◽  
Nabil Matmati ◽  
Helena Pereira ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Membrane Permeabilization ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Outer Membrane Permeabilization

scholarly journals Poliovirus Induces Bax-Dependent Cell Death Mediated by c-Jun NH2-Terminal Kinase

2007 ◽  
Vol 81 (14) ◽  
pp. 7504-7516 ◽  
Author(s):  
Arnaud Autret ◽  
Sandra Martin-Latil ◽  
Laurence Mousson ◽  
Aurélie Wirotius ◽  
Frédéric Petit ◽  
...  
Keyword(s):  
Cell Death ◽  
Outer Membrane ◽  
Motor Neurons ◽  
Cell Receptor ◽  
Cellular Level ◽  
Membrane Permeabilization ◽  
Paralytic Poliomyelitis ◽  
Receptor Interaction ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Outer Membrane Permeabilization

ABSTRACT Poliovirus (PV) is the causal agent of paralytic poliomyelitis, a disease that involves the destruction of motor neurons associated with PV replication. In PV-infected mice, motor neurons die through an apoptotic process. However, mechanisms by which PV induces cell death in neuronal cells remain unclear. Here, we demonstrate that PV infection of neuronal IMR5 cells induces cytochrome c release from mitochondria and loss of mitochondrial transmembrane potential, both of which are evidence of mitochondrial outer membrane permeabilization. PV infection also activates Bax, a proapoptotic member of the Bcl-2 family; this activation involves its conformational change and its redistribution from the cytosol to mitochondria. Neutralization of Bax by vMIA protein expression prevents cytochrome c release, consistent with a contribution of PV-induced Bax activation to mitochondrial outer membrane permeabilization. Interestingly, we also found that c-Jun NH2-terminal kinase (JNK) is activated soon after PV infection and that the PV-cell receptor interaction alone is sufficient to induce JNK activation. Moreover, the pharmacological inhibition of JNK by SP600125 inhibits Bax activation and cytochrome c release. This is, to our knowledge, the first demonstration of JNK-mediated Bax-dependent apoptosis in PV-infected cells. Our findings contribute to our understanding of poliomyelitis pathogenesis at the cellular level.

scholarly journals Mitochondrial release of apoptosis-inducing factor occurs downstream of cytochrome c release in response to several proapoptotic stimuli

2002 ◽  
Vol 159 (6) ◽  
pp. 923-929 ◽  
Author(s):  
Damien Arnoult ◽  
Philippe Parone ◽  
Jean-Claude Martinou ◽  
Bruno Antonsson ◽  
Jérôme Estaquier ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Outer Membrane ◽  
Actinomycin D ◽  
Membrane Permeabilization ◽  
Mitochondrial Outer Membrane ◽  
Simple Explanation ◽  
Cytochrome C Release ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
Mitochondrial Inner Membrane ◽  
Apoptosis Inducing Factor

Mitochondrial outer membrane permeabilization by proapoptotic Bcl-2 family proteins, such as Bax, plays a crucial role in apoptosis induction. However, whether this only causes the intracytosolic release of inducers of caspase-dependent death, such as cytochrome c, or also of caspase-independent death, such as apoptosis-inducing factor (AIF) remains unknown. Here, we show that on isolated mitochondria, Bax causes the release of cytochrome c, but not of AIF, and the association of AIF with the mitochondrial inner membrane provides a simple explanation for its lack of release upon Bax-mediated outer membrane permeabilization. In cells overexpressing Bax or treated either with the Bax- or Bak-dependent proapoptotic drugs staurosporine or actinomycin D, or with hydrogen peroxide, caspase inhibitors did not affect the intracytosolic translocation of cytochrome c, but prevented that of AIF. These results provide a paradigm for mitochondria-dependent death pathways in which AIF cannot substitute for caspase executioners because its intracytosolic release occurs downstream of that of cytochrome c.

The murine cytomegalovirus cell death suppressor m38.5 binds Bax and blocks Bax-mediated mitochondrial outer membrane permeabilization

APOPTOSIS ◽  
2008 ◽  
Vol 13 (9) ◽  
pp. 1100-1110 ◽  
Author(s):  
Damien Arnoult ◽  
Anna Skaletskaya ◽  
Jérôme Estaquier ◽  
Cecilie Dufour ◽  
Victor S. Goldmacher
Keyword(s):  
Cell Death ◽  
Outer Membrane ◽  
Membrane Permeabilization ◽  
Murine Cytomegalovirus ◽  
Mitochondrial Outer Membrane ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
Cell Death Suppressor

scholarly journals Resistance to Granzyme B-mediated Cytochrome c Release in Bak-deficient Cells

2001 ◽  
Vol 194 (9) ◽  
pp. 1325-1338 ◽  
Author(s):  
Gui-Qiang Wang ◽  
Eva Wieckowski ◽  
Leslie A. Goldstein ◽  
Brian R. Gastman ◽  
Asaf Rabinovitz ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Outer Membrane ◽  
Knockout Mice ◽  
Granzyme B ◽  
Membrane Permeabilization ◽  
Mitochondrial Outer Membrane ◽  
Target Cells ◽  
Cytochrome C Release ◽  
Mitochondrial Outer Membrane Permeabilization ◽  
S 100

Granzyme B (GrB), a serine protease with substrate specificity similar to the caspase family, is a major component of granule-mediated cytotoxicity of T lymphocytes. Although GrB can directly activate caspases, it induces apoptosis predominantly via Bid cleavage, mitochondrial outer membrane permeabilization, and cytochrome c release. To study the molecular regulators for GrB-mediated mitochondrial apoptotic events, we used a CTL-free cytotoxicity system, wherein target cells are treated with purified GrB and replication-deficient adenovirus (Ad). We report here that the Bcl-2 proapoptotic family member, Bak, plays a dominant role in GrB-mediated mitochondrial apoptotic events. A variant of Jurkat cells, deficient in Bak expression, was resistant to GrB/Ad-mediated apoptosis, as determined by lack of membranous phosphatidylserine exposure, lack of DNA breaks, lack of mitochondrial outer membrane permeabilization, and unchanged expression of inner mitochondrial membrane cardiolipin. The resistance of Bak-deficient cells to GrB/Ad cytotoxicity was reversed by transduction of the Bak gene into these cells. The requirement for both Bid and Bak, was further demonstrated in a cell-free system using purified mitochondria and S-100 cytosol. Purified mitochondria from Bid knockout mice, but not from Bax knockout mice, failed to release cytochrome c in response to autologous S-100 and GrB. Also, Bak-deficient mitochondria did not release cytochrome c in response to GrB-treated cytosol unless recombinant Bak protein was added. These results are the first to report a role for Bak in GrB-mediated mitochondrial apoptosis. This study demonstrates that GrB-cleaved Bid, which differs in size and site of cleavage from caspase-8-cleaved Bid, utilizes Bak for cytochrome c release, and therefore, suggests that deficiency in Bak may serve as a mechanism of immune evasion for tumor or viral infected cells.

scholarly journals In Vivo Imaging of Drug-Induced Mitochondrial Outer Membrane Permeabilization at Single-Cell Resolution

2012 ◽  
Vol 72 (12) ◽  
pp. 2949-2956 ◽  
Author(s):  
Sarah Earley ◽  
Claudio Vinegoni ◽  
Joshua Dunham ◽  
Rostic Gorbatov ◽  
Paolo Fumene Feruglio ◽  
...  
Keyword(s):  
Single Cell ◽  
Outer Membrane ◽  
In Vivo Imaging ◽  
Membrane Permeabilization ◽  
Mitochondrial Outer Membrane ◽  
Drug Induced ◽  
Mitochondrial Outer Membrane Permeabilization
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