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10.1074/jbc.M114.567685 http://scihub22266oqcxt.onion/10.1074/jbc.M114.567685 C4175329!4175329 !25107906     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25107906 &cmd=llinks): Failed to open stream: HTTP request failed! 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Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses |pdf=|usr=}}{{25107906 }} gab.com Text Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses JO: J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25107906 #FOAvip With oxidative injury as well as in some solid tumors and myeloid leukemia cells, heme oxygenase-1 (HO-1), the anti-oxidant, anti-inflammatory, and anti-apoptotic microsomal stress protein, migrates to the nucleus in a truncated and enzymatically inactive form. However, the function of HO-1 in the nucleus is not completely clear. Nuclear factor erythroid 2-related factor 2 (Nrf2), a transcription factor and master regulator of numerous antioxidants and anti-apoptotic proteins, including HO-1, also accumulates in the nucleus with oxidative injury and in various types of cancer. Here we demonstrate that in oxidative stress, nuclear HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3? (GSK3?)-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus. This regulation of Nrf2 post-induction by nuclear HO-1 is important for the preferential transcription of phase II detoxification enzymes such as NQO1 as well as glucose-6-phosphate dehydrogenase (G6PDH), a regulator of the pentose phosphate pathway. Using Nrf2 knock-out cells, we further demonstrate that nuclear HO-1-associated cytoprotection against oxidative stress depends on an HO-1/Nrf2 interaction. Although it is well known that Nrf2 induces HO-1 leading to mitigation of oxidant stress, we propose a novel mechanism by which HO-1, by modulating the activation of Nrf2, sets an adaptive reprogramming that enhances antioxidant defenses. Twit Text FOAVip Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses ????J Biol Chem http://www.kidney.de/pget.php?&tw=1&pmid=25107906 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25107906 #FOAvip English Wikipedia <ref>{{Cite pmid|25107906 }}</ref> Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and activation of Nrf2, impacting metabolic and anti-oxidant defenses #MMPMID25107906 Biswas C ; Shah N ; Muthu M ; La P ; Fernando AP ; Sengupta S ; Yang G ; Dennery PA J Biol Chem 2014[Sep]; 289 (39 ): 26882-26894 PMID25107906 show ga With oxidative injury as well as in some solid tumors and myeloid leukemia cells, heme oxygenase-1 (HO-1), the anti-oxidant, anti-inflammatory, and anti-apoptotic microsomal stress protein, migrates to the nucleus in a truncated and enzymatically inactive form. However, the function of HO-1 in the nucleus is not completely clear. Nuclear factor erythroid 2-related factor 2 (Nrf2), a transcription factor and master regulator of numerous antioxidants and anti-apoptotic proteins, including HO-1, also accumulates in the nucleus with oxidative injury and in various types of cancer. Here we demonstrate that in oxidative stress, nuclear HO-1 interacts with Nrf2 and stabilizes it from glycogen synthase kinase 3? (GSK3?)-mediated phosphorylation coupled with ubiquitin-proteasomal degradation, thereby prolonging its accumulation in the nucleus. This regulation of Nrf2 post-induction by nuclear HO-1 is important for the preferential transcription of phase II detoxification enzymes such as NQO1 as well as glucose-6-phosphate dehydrogenase (G6PDH), a regulator of the pentose phosphate pathway. Using Nrf2 knock-out cells, we further demonstrate that nuclear HO-1-associated cytoprotection against oxidative stress depends on an HO-1/Nrf2 interaction. Although it is well known that Nrf2 induces HO-1 leading to mitigation of oxidant stress, we propose a novel mechanism by which HO-1, by modulating the activation of Nrf2, sets an adaptive reprogramming that enhances antioxidant defenses. |*Oxidative Stress [MESH] |Animals [MESH] |Antioxidants/*metabolism [MESH] |Cell Nucleus/genetics/*metabolism [MESH] |Cells, Cultured [MESH] |Glucosephosphate Dehydrogenase/genetics/metabolism [MESH] |Glycogen Synthase Kinase 3 beta [MESH] |Glycogen Synthase Kinase 3/genetics/metabolism [MESH] |Heme Oxygenase-1/genetics/*metabolism [MESH] |Membrane Proteins/genetics/*metabolism [MESH] |Mice [MESH] |Mice, Knockout [MESH] |NAD(P)H Dehydrogenase (Quinone)/genetics/metabolism [MESH] |NF-E2-Related Factor 2/genetics/*metabolism [MESH] |Phosphorylation/genetics [MESH] |Proteasome Endopeptidase Complex/genetics/metabolism [MESH]Nuclear heme oxygenase-1 (HO-1) modulates subcellular distribution and(epmc).pdf DeepDyve Pubget Overpricing