Proteasome activation by poly-ADP-ribose-polymerase in human myelomonocytic cells after oxidative stress

Ullrich, Oliver; Ciftci, Özlem; Hass, Ralf

doi:10.1016/s0891-5849(00)00399-3

Cited by 39 publications

(30 citation statements)

References 33 publications

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“…This is consistent with the observation that the 20S but not the 26S proteasome activity is upregulated in cells treated with hydrogen peroxide. 7 As stress-induced degradation of Ran and importin-b can be decreased by MG132 and lactacystin, we conclude that their proteolysis in cells treated with oxidants is partially mediated by the 20S proteasome complex.…”

Section: In Cells Treated With Hydrogen Peroxide Ran and Importin-b mentioning

confidence: 63%

“…6 Hydrogen peroxide not only activates several signal transduction pathways, it may also activate the nuclear proteasome, thereby increasing the degradation of proteins damaged by oxidants. 7 Nucleocytoplasmic trafficking of macromolecules is sensitive to stress; heat shock, ethanol and oxidative stress inhibit classical nuclear protein import. 8,9,10 In growing yeast cells and in semi-permeabilized smooth muscle cells in vitro, oxidants have been shown to interfere with classical nuclear import.…”

Section: Introductionmentioning

confidence: 99%

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Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress

et al. 2004

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In growing HeLa cells, severe stress elicited by the oxidant hydrogen peroxide inhibits classical nuclear import. Oxidant treatment collapses the nucleocytoplasmic Ran concentration gradient, thereby elevating cytoplasmic GTPase levels. The Ran gradient dissipates in response to a stress-induced depletion of RanGTP and a decreased efficiency of Ran nuclear import. In addition, oxidative stress induces a relocation of the nucleoporin Nup153 as well as the nuclear carrier importin-b, and docking of the importin-a/b/cargo complex at the nuclear envelope is reduced. Moreover, Ran, importin-b and Nup153 undergo proteolysis upon oxidative stress. Caspases and the proteasome degrade Ran and importin-b; however, ubiquitination of these transport factors is not observed. Inhibition of caspases in stressed cells alleviates the mislocalization of importin-b, but does not restore the Ran concentration gradient or classical import. In summary, inhibition of classical nuclear import by hydrogen peroxide is caused by a combination of multiple mechanisms that target different components of the transport apparatus.

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Section: In Cells Treated With Hydrogen Peroxide Ran and Importin-b mentioning

confidence: 63%

Section: Introductionmentioning

confidence: 99%

Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress

et al. 2004

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“…We found no obvious upregulation of any proteasome subunits, or of overall proteolytic capacity, in response to oxidative stress, and we believe that the increased cytoplasmic proteolysis is largely due to increased susceptibility of substrates when oxidized. In contrast, we have recently shown that nuclear proteasome can be activated by poly-ADP ribosylation in nuclei of K562 human hematopoeitic cells [68,69]. Nuclear 20S proteasome activated by poly-ADP ribosylation can eliminate oxidatively damaged histones more efficiently [68,69].…”

Section: Regulation Of the Proteasome Pathway In Response To Oxidativmentioning

confidence: 89%

Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells

Shringarpure¹,

Grune²,

Davies³

2001

CMLS, Cell. Mol. Life Sci.

199

119

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The generation of reactive oxygen species is an inevitable aspect of aerobic life. In addition to being exposed to free radicals in the environment, aerobic organisms must also deal with oxygen radicals generated as byproducts of a number of physiological mechanisms for example, by the mitochondrial and endoplasmic reticulum electron transport chains, and by cells of the immune system. Although most organisms are equipped with several lines of defense against oxidative stress, these defensive mechanisms are not 100% effective, and oxidatively modified forms of proteins accumulate during aging, and in many pathological conditions. Oxidatively modified proteins can form large aggregates due to covalent cross-linking or increased surface hydrophobicity. Unless repaired or removed from cells, these oxidized proteins are often toxic and can threaten cell viability. Mammalian cells exhibit only limited direct repair mechanisms, and oxidatively damaged proteins appear to undergo selective proteolysis, primarily by the major cytosolic proteinase, the proteasome. Interestingly, it appears that the 20S 'core' proteasome conducts the recognition and elimination of oxidized proteins in an ATP-independent and ubiquitin-independent pathway.

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“…It has been shown that poly(ADP-ribose) polymer can also serve as an emergency source of energy used by the base excision machinery to synthesize ATP (Oei et al 2000). Furthermore, poly(ADP-ribose) may also serve as a signal for protein degradation in oxidatively injured cells (Ullrich et al 2000).…”

Section: Poly(adp-ribose) Polymerase and Its Activationmentioning

confidence: 99%

The pathogenesis of diabetic complications: the role of DNA injury and poly(ADP-ribose) polymerase activation in peroxynitrite-mediated cytotoxicity

Kiss

Szabó

2005

Mem. Inst. Oswaldo Cruz

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Proteasome activation by poly-ADP-ribose-polymerase in human myelomonocytic cells after oxidative stress

Cited by 39 publications

References 33 publications

Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress

Multiple mechanisms promote the inhibition of classical nuclear import upon exposure to severe oxidative stress

Protein oxidation and 20S proteasome-dependent proteolysis in mammalian cells

The pathogenesis of diabetic complications: the role of DNA injury and poly(ADP-ribose) polymerase activation in peroxynitrite-mediated cytotoxicity

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