Abstract：
:Premature senescence, a death escaping pathway for cells experiencing stress, is conducive to aging and cardiovascular diseases. The molecular switch between senescent and apoptotic fate remains, however, poorly recognized. Nrf2 is an important transcription factor orchestrating adaptive response to cellular stress. Here, we show that both human primary endothelial cells (ECs) and murine aortas lacking Nrf2 signaling are senescent but unexpectedly do not encounter damaging oxidative stress. Instead, they exhibit markedly increased S-nitrosation of proteins. A functional role of S-nitrosation is protection of ECs from death by inhibition of NOX4-mediated oxidative damage and redirection of ECs to premature senescence. S-nitrosation and senescence are mediated by Keap1, a direct binding partner of Nrf2, which colocalizes and precipitates with nitric oxide synthase (NOS) and transnitrosating protein GAPDH in ECs devoid of Nrf2. We conclude that the overabundance of this "unrestrained" Keap1 determines the fate of ECs by regulation of S-nitrosation and propose that Keap1/GAPDH/NOS complex may serve as an enzymatic machinery for S-nitrosation in mammalian cells.
journal_name
Redox Bioljournal_title
Redox biologyauthors
Kopacz A,Klóska D,Proniewski B,Cysewski D,Personnic N,Piechota-Polańczyk A,Kaczara P,Zakrzewska A,Forman HJ,Dulak J,Józkowicz A,Grochot-Przęczek Adoi
10.1016/j.redox.2019.101304subject
Has Abstractpub_date
2020-01-01 00:00:00pages
101304issn
2213-2317pii
S2213-2317(19)30383-0journal_volume
28pub_type
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