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10.1016/j.bbamcr.2013.04.005 http://scihub22266oqcxt.onion/10.1016/j.bbamcr.2013.04.005 C4041949!4041949 !23597856     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\23597856 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Biochim+Biophys+Acta 2013 ; 1833 (8 ): 1985-91 Nephropedia Template TP {{tp|p=23597856 |t=2013. Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-?B transcriptional activity by preventing p65 de-acetylation |pdf=|usr=}}{{23597856 }} gab.com Text Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor- B transcriptional activity by preventing p65 de-acetylation JO: Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=23597856 #FOAvip NF-?B is a transcription factor that integrates pro-inflammatory and pro-survival responses in diverse cell types. The activity of NF-?B is regulated in part by acetylation of its p65 subunit at lysine 310, which is required for transcription complex formation. De-acetylation at this site is performed by sirtuin 1(SIRT1) and possibly other sirtuins in an NAD(+) dependent manner, such that SIRT1 inhibition promotes NF-?B transcriptional activity. It is unknown, however, whether changes in NAD(+) levels can influence p65 acetylation and cellular inflammatory responses. Poly(ADP-ribose)-1 (PARP-1) is an abundant nuclear enzyme that consumes NAD(+) in the process of forming (ADP-ribose)polymers on target proteins, and extensive PARP-1 activation can reduce intracellular NAD(+) concentrations. Here we tested the idea that PARP-1 activation can regulate NF-?B transcriptional activity by reducing NAD(+) concentrations and thereby inhibiting de-acetylation of p65. Primary astrocyte cultures were treated with the alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) to induce PARP-1 activation. This resulted in sustained acetylation of p65 and increased NF-?B transcriptional activity as monitored by a ?B-driven eGFP reporter gene. These effects of MNNG were negated by a PARP-1 inhibitor, in PARP-1(-/-) cells, and in PARP-1(-/-) cells transfected with a catalytically inactive PARP-1 construct, thus confirming that these effects are mediated by PARP-1 catalytic activity. The effects of PARP-1 activation were replicated by a SIRT1 inhibitor, EX-527, and were reversed by exogenous NAD(+). These findings demonstrate that PARP-1-induced changes in NAD(+) levels can modulate NF-?B transcriptional activity through effects on p65 acetylation. Twit Text FOAVip Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor- B transcriptional activity by preventing p65 de-acetylation ????Biochim Biophys Acta http://www.kidney.de/pget.php?&tw=1&pmid=23597856 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=23597856 #FOAvip English Wikipedia <ref>{{Cite pmid|23597856 }}</ref> Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclear factor-?B transcriptional activity by preventing p65 de-acetylation #MMPMID23597856 Kauppinen TM ; Gan L ; Swanson RA Biochim Biophys Acta 2013[Aug]; 1833 (8 ): 1985-91 PMID23597856 show ga NF-?B is a transcription factor that integrates pro-inflammatory and pro-survival responses in diverse cell types. The activity of NF-?B is regulated in part by acetylation of its p65 subunit at lysine 310, which is required for transcription complex formation. De-acetylation at this site is performed by sirtuin 1(SIRT1) and possibly other sirtuins in an NAD(+) dependent manner, such that SIRT1 inhibition promotes NF-?B transcriptional activity. It is unknown, however, whether changes in NAD(+) levels can influence p65 acetylation and cellular inflammatory responses. Poly(ADP-ribose)-1 (PARP-1) is an abundant nuclear enzyme that consumes NAD(+) in the process of forming (ADP-ribose)polymers on target proteins, and extensive PARP-1 activation can reduce intracellular NAD(+) concentrations. Here we tested the idea that PARP-1 activation can regulate NF-?B transcriptional activity by reducing NAD(+) concentrations and thereby inhibiting de-acetylation of p65. Primary astrocyte cultures were treated with the alkylating agent N-methyl-N'-nitro-N-nitrosoguanidine (MNNG) to induce PARP-1 activation. This resulted in sustained acetylation of p65 and increased NF-?B transcriptional activity as monitored by a ?B-driven eGFP reporter gene. These effects of MNNG were negated by a PARP-1 inhibitor, in PARP-1(-/-) cells, and in PARP-1(-/-) cells transfected with a catalytically inactive PARP-1 construct, thus confirming that these effects are mediated by PARP-1 catalytic activity. The effects of PARP-1 activation were replicated by a SIRT1 inhibitor, EX-527, and were reversed by exogenous NAD(+). These findings demonstrate that PARP-1-induced changes in NAD(+) levels can modulate NF-?B transcriptional activity through effects on p65 acetylation. |Acetylation/drug effects [MESH] |Animals [MESH] |Astrocytes/drug effects/enzymology/metabolism/physiology [MESH] |Carbazoles/pharmacology [MESH] |Cells, Cultured [MESH] |Humans [MESH] |Methylnitronitrosoguanidine/pharmacology [MESH] |Mice [MESH] |NAD/*deficiency/genetics/metabolism [MESH] |NF-kappa B/*genetics/*metabolism [MESH] |Poly (ADP-Ribose) Polymerase-1 [MESH] |Poly(ADP-ribose) Polymerase Inhibitors [MESH] |Poly(ADP-ribose) Polymerases/*genetics/*metabolism [MESH] |Sirtuin 1/antagonists & inhibitors/genetics/metabolism [MESH] |Transcription, Genetic/drug effects [MESH] |Transcriptional Activation/drug effects/genetics [MESH] |Transfection [MESH]Poly(ADP-ribose) polymerase-1-induced NAD(+) depletion promotes nuclea(epmc).pdf DeepDyve Pubget Overpricing