2008
DOI: 10.1016/j.freeradbiomed.2007.12.012
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Oligomerization of the cysteinyl-rich oligopeptidase EP24.15 is triggered by S-glutathionylation

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Cited by 30 publications
(41 citation statements)
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“…It appeared that drug-induced glutathionylation can also generate intermolecular crosslinking of p53 (Fig. 3C) as has been observed for the oligopeptidase EP24.15 (42); such an event occurs through a thiol-disulfide exchange between thiolated and unthiolated protein molecules.…”
Section: Discussionmentioning
confidence: 61%
“…It appeared that drug-induced glutathionylation can also generate intermolecular crosslinking of p53 (Fig. 3C) as has been observed for the oligopeptidase EP24.15 (42); such an event occurs through a thiol-disulfide exchange between thiolated and unthiolated protein molecules.…”
Section: Discussionmentioning
confidence: 61%
“…It is therefore of interest that thimet oligopeptidase (EP24.15), a ubiquitously expressed thiol-rich metallopeptidase that is important in the degradation of peptides generated by the proteasome machinery, is constitutively glutathionylated intracellularly [96]. The findings suggested an unconventional property of protein glutathionylation, namely inducing oligomerization by interprotein thiol-disulfide exchange to a less active enzyme form [96]. These results may be relevant to the dual role of EP24.15 both in degrading antigenic peptides, which results in decreased antigen presentation, and in increasing production of antigenic peptides, for example, under conditions of oxidative stress.…”
Section: Biological Importance Of Protein Glutathionylationmentioning
confidence: 99%
“…These results may be relevant to the dual role of EP24.15 both in degrading antigenic peptides, which results in decreased antigen presentation, and in increasing production of antigenic peptides, for example, under conditions of oxidative stress. It is of further interest that the Rpn1 and Rpn2 subunits of purified human 26S proteasomes undergo glutathionylation, resulting in a less active complex when exposed to H 2 O 2 and GSH [96]. …”
Section: Biological Importance Of Protein Glutathionylationmentioning
confidence: 99%
“…In addition, a higher-molecular-mass species was detected around 113 kDa (top panel, lane 3, arrow), albeit to a lesser degree, presumably representing an S-glutathionylation-triggered multimeric APE1 form. 37 Since S-glutathionylation can be reversed by deglutathionylation with reducing agents, 37 we tested whether the observed modification could be reversed by dithiothreitol (DTT) treatment. As would be expected for S-glutathionylation, the observed modification of APE1 was fully reversed by DTT exposure (top panel, lane 4).…”
Section: Resultsmentioning
confidence: 99%