We are analyzing https://link.springer.com/article/10.1007/s10495-007-0069-5.

Title:
Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death | Apoptosis
Description:
While increasing evidence shows that proteasome inhibition triggers oxidative damage, mitochondrial dysfunction and death in neuronal cells, the regulatory relationship among these events is unclear. Using mouse neuronal cells we show that the cytotoxicity induced by mild (0.25 μM) and potent (5.0 μM) doses of the proteasome inhibitor, N-Benzyloxycarbonyl-Ile-Glu (O-t-butyl)-Ala-leucinal, (PSI) involved a dose-dependent increase in caspase activation, overproduction of reactive oxygen species (ROS) and a mitochondrial dysfunction manifested by the translocation of the proapoptotic protein, Bax, from the cytoplasm to the mitochondria, membrane depolarization and the release of cytochrome c and the apoptosis inducing factor (AIF) from mitochondria to the cytoplasm and nucleus, respectively. Whereas caspase or Bax inhibition failed to prevent mitochondrial membrane depolarization and neuronal cell death, pretreatments with the antioxidant N-acetyl-l-cysteine (NAC) or overexpression of the antiapoptotic protein Bcl-xL abrogated these events in cells exposed to mild levels of PSI. These findings implicated ROS as a mediator of PSI-induced cytotoxicity. However, depletions in glutathione and Bcl-xL with potent proteasome inhibition exacerbated this response whereupon survival required the cooperative protection of NAC with Bcl-xL overexpression. Collectively, ROS induced by proteasome inhibition mediates a mitochondrial dysfunction in neuronal cells that culminates in death through caspase- and Bax-independent mechanisms.
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Keywords {🔍}

article, google, scholar, cas, pubmed, apoptosis, mitochondrial, cell, death, proteasome, cells, neuronal, oxygen, reactive, species, inhibition, dysfunction, res, bax, activation, biol, factor, inhibitor, caspase, release, bclxl, induces, neurosci, induced, ros, membrane, cytochrome, chem, caspaseindependent, rockwell, pathway, generation, bcl, privacy, cookies, content, oxidative, protein, mitochondria, response, mechanisms, brain, neurons, wang, cancer,

Topics {✒️}

antioxidant n-acetyl-l-cysteine bax-induced pro-oxidant state 1-methyl-4-phenylpyridinium ion-induced apoptosis month download article/chapter n-acetyl-cysteine gsh bcl-2-mitochondria-ros-inos pathway n-benzyloxycarbonyl-ile-glu mg132-induced mitochondrial dysfunction sulforaphane-induced cell death evan gomes & patricia rockwell caspase-independent neuronal death vander heiden mg caspase-independent cell death hyperoxia-induced bax activation serum-free cell death mitochondrial-dependent apoptosis induced bax/bak-mediated permeabilization mitochondrial apoptosis-inducing factor bax-inhibiting peptide derived neuroblastoma-2a cells involves reactive oxygen species voltage-dependent anion channel proteasome inhibition mediates article apoptosis aims independent neuronal death neuronal cell death full article pdf mitochondrial cell death bcl-xl promotes methylglyoxal-induced apoptosis mitochondrial signaling pathway proteasome inhibitor bortezomib caspase-mediated loss apoptosis inducing factor apoptosis-inducing factor mitochondrial dysfunction manifested privacy choices/manage cookies programmed neuronal death vdac-dependent permeabilization small cell lung ros-dependent pathway noxa activation independent protease-mediated apoptosis bax inhibition failed ubiquitin-mediated proteolysis outer mitochondrial membrane mitochondrial membrane potential neuronal cells induces electronic supplementary material multiple myeloma cells

Questions {❓}

Halliwell B (2006) Oxidative stress and neurodegeneration: where are we now?

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         description:While increasing evidence shows that proteasome inhibition triggers oxidative damage, mitochondrial dysfunction and death in neuronal cells, the regulatory relationship among these events is unclear. Using mouse neuronal cells we show that the cytotoxicity induced by mild (0.25 μM) and potent (5.0 μM) doses of the proteasome inhibitor, N-Benzyloxycarbonyl-Ile-Glu (O-t-butyl)-Ala-leucinal, (PSI) involved a dose-dependent increase in caspase activation, overproduction of reactive oxygen species (ROS) and a mitochondrial dysfunction manifested by the translocation of the proapoptotic protein, Bax, from the cytoplasm to the mitochondria, membrane depolarization and the release of cytochrome c and the apoptosis inducing factor (AIF) from mitochondria to the cytoplasm and nucleus, respectively. Whereas caspase or Bax inhibition failed to prevent mitochondrial membrane depolarization and neuronal cell death, pretreatments with the antioxidant N-acetyl-l-cysteine (NAC) or overexpression of the antiapoptotic protein Bcl-xL abrogated these events in cells exposed to mild levels of PSI. These findings implicated ROS as a mediator of PSI-induced cytotoxicity. However, depletions in glutathione and Bcl-xL with potent proteasome inhibition exacerbated this response whereupon survival required the cooperative protection of NAC with Bcl-xL overexpression. Collectively, ROS induced by proteasome inhibition mediates a mitochondrial dysfunction in neuronal cells that culminates in death through caspase- and Bax-independent mechanisms.
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      headline:Reactive oxygen species induced by proteasome inhibition in neuronal cells mediate mitochondrial dysfunction and a caspase-independent cell death
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