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10.1093/nar/gkw442 http://scihub22266oqcxt.onion/10.1093/nar/gkw442 C5027479!5027479!27198223     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nucleic+Acids+Res 2016 ; 44 (16): 7630-45 Nephropedia Template TP {{tp|p=27198223|t=2016. PKC? and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation |pdf=|usr=}}{{27198223}} gab.com Text PKC and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation JO: Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=27198223 #FOAvip Harmful oxidation of proteins, lipids and nucleic acids is observed when reactive oxygen species (ROS) are produced excessively and/or the antioxidant capacity is reduced, causing ?oxidative stress?. Nuclear poly-ADP-ribose (PAR) formation is thought to be induced in response to oxidative DNA damage and to promote cell death under sustained oxidative stress conditions. However, what exactly triggers PAR induction in response to oxidative stress is incompletely understood. Using reverse phase protein array (RPPA) and in-depth analysis of key stress signaling components, we observed that PAR formation induced by H2O2 was mediated by the PLC/IP3R/Ca2+/PKC? signaling axis. Mechanistically, H2O2-induced PAR formation correlated with Ca2+-dependent DNA damage, which, however, was PKC?-independent. In contrast, PAR formation was completely lost upon knockdown of PKC?, suggesting that DNA damage alone was not sufficient for inducing PAR formation, but required a PKC?-dependent process. Intriguingly, the loss of PAR formation observed upon PKC? depletion was overcome when the chromatin structure-modifying protein HMGB1 was co-depleted with PKC?, suggesting that activation and nuclear translocation of PKC? releases the inhibitory effect of HMGB1 on PAR formation. Together, these results identify PKC? and HMGB1 as important co-regulators involved in H2O2-induced PAR formation, a finding that may have important relevance for oxidative stress-associated pathophysiological conditions. Twit Text FOAVip PKC and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation ????Nucleic Acids Res http://www.kidney.de/pget.php?&tw=1&pmid=27198223 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27198223 #FOAvip English Wikipedia <ref>{{Cite pmid|27198223}}</ref> PKC? and HMGB1 antagonistically control hydrogen peroxide-induced poly-ADP-ribose formation #MMPMID27198223 Andersson A; Bluwstein A; Kumar N; Teloni F; Traenkle J; Baudis M; Altmeyer M; Hottiger MO Nucleic Acids Res 2016[Sep]; 44 (16): 7630-45 PMID27198223show ga Harmful oxidation of proteins, lipids and nucleic acids is observed when reactive oxygen species (ROS) are produced excessively and/or the antioxidant capacity is reduced, causing ?oxidative stress?. Nuclear poly-ADP-ribose (PAR) formation is thought to be induced in response to oxidative DNA damage and to promote cell death under sustained oxidative stress conditions. However, what exactly triggers PAR induction in response to oxidative stress is incompletely understood. Using reverse phase protein array (RPPA) and in-depth analysis of key stress signaling components, we observed that PAR formation induced by H2O2 was mediated by the PLC/IP3R/Ca2+/PKC? signaling axis. Mechanistically, H2O2-induced PAR formation correlated with Ca2+-dependent DNA damage, which, however, was PKC?-independent. In contrast, PAR formation was completely lost upon knockdown of PKC?, suggesting that DNA damage alone was not sufficient for inducing PAR formation, but required a PKC?-dependent process. Intriguingly, the loss of PAR formation observed upon PKC? depletion was overcome when the chromatin structure-modifying protein HMGB1 was co-depleted with PKC?, suggesting that activation and nuclear translocation of PKC? releases the inhibitory effect of HMGB1 on PAR formation. Together, these results identify PKC? and HMGB1 as important co-regulators involved in H2O2-induced PAR formation, a finding that may have important relevance for oxidative stress-associated pathophysiological conditions. äPKC? and HMGB1 antagonistically control hydrogen peroxide-induced poly(epmc).pdf DeepDyve Pubget Overpricing