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10.1038/cddis.2015.64 http://scihub22266oqcxt.onion/10.1038/cddis.2015.64 C4650746!4650746 !26181205     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26181205 &cmd=llinks): Failed to open stream: HTTP request failed! 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Intracellular oxygen determined by respiration regulates localization of Ras and prenylated proteins |pdf=|usr=}}{{26181205 }} gab.com Text Intracellular oxygen determined by respiration regulates localization of Ras and prenylated proteins JO: Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=26181205 #FOAvip Reduction of mitochondrial DNA (mtDNA) content induces the reduction of oxidative phosphorylation and dependence on fermentative glycolysis, that is, the Warburg effect. In aggressive prostate cancer (PCa), the reduction of mtDNA reduces oxygen consumption, increases intracellular oxygen concentration, and induces constitutive activation of Ras. Many essential proteins for cell death, growth, differentiation, and development, such as Ras, require prenylation for subcellular localization and activation. Prenylation of a protein is defined as the attachment of isoprenoids to a cysteine residue at or near the C-terminus. 3-Hydroxy-3-methyl-glutaryl-coenzyme A reductase (HMGR) produces isoprenoids, and is posttranslationally regulated by oxygen. We investigated a critical role of intracellular oxygen in membrane localization of prenylated proteins. Localization of prenylated proteins (H-Ras, prelamin A/C, and Rab5a) was observed in poorly differentiated PCa (PC-3) and well-differentiated PCa (LNCaP) cells. PC-3 cells exhibited high intracellular oxygen concentration, and H-Ras, prelamin A/C, and Rab5a were localized to various membranes (Golgi and plasma membrane, nuclear membrane, and early endosomes, respectively). Remarkably, exogenous hypoxia (0.2% O2) in PC-3 cells induced intracellular hypoxia and changed the localization of the prenylated proteins. H-Ras and Rab5a were translocated to cytosol, and prelamin A/C was in the nucleus forming an abnormal nuclear envelope. The localization was reversed by mevalonate indicating the involvement of mevalonate pathway. In contrast, in LNCaP cells, exhibiting low intracellular oxygen concentration, H-Ras and Rab5a were localized in the cytosol, and prelamin A/C was inside the nucleus forming an inadequate nuclear envelope. Exogenous hyperoxia (40% O2) increased the intracellular oxygen concentration and induced Ras translocation from cytosol to the membrane. Prelamin A/C was translocated to the nuclear membrane and formed a proper nuclear envelope. Rab5a was translocated to the early endosomes. The specific localizations of the prenylated proteins were dependent on intracellular oxygen concentration. These results demonstrate that intracellular oxygen concentration regulates the localization and activation of prenylated proteins. Twit Text FOAVip Intracellular oxygen determined by respiration regulates localization of Ras and prenylated proteins ????Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=26181205 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26181205 #FOAvip English Wikipedia <ref>{{Cite pmid|26181205 }}</ref> Intracellular oxygen determined by respiration regulates localization of Ras and prenylated proteins #MMPMID26181205 Kim A ; Davis R ; Higuchi M Cell Death Dis 2015[Jul]; 6 (7 ): e1825 PMID26181205 show ga Reduction of mitochondrial DNA (mtDNA) content induces the reduction of oxidative phosphorylation and dependence on fermentative glycolysis, that is, the Warburg effect. In aggressive prostate cancer (PCa), the reduction of mtDNA reduces oxygen consumption, increases intracellular oxygen concentration, and induces constitutive activation of Ras. Many essential proteins for cell death, growth, differentiation, and development, such as Ras, require prenylation for subcellular localization and activation. Prenylation of a protein is defined as the attachment of isoprenoids to a cysteine residue at or near the C-terminus. 3-Hydroxy-3-methyl-glutaryl-coenzyme A reductase (HMGR) produces isoprenoids, and is posttranslationally regulated by oxygen. We investigated a critical role of intracellular oxygen in membrane localization of prenylated proteins. Localization of prenylated proteins (H-Ras, prelamin A/C, and Rab5a) was observed in poorly differentiated PCa (PC-3) and well-differentiated PCa (LNCaP) cells. PC-3 cells exhibited high intracellular oxygen concentration, and H-Ras, prelamin A/C, and Rab5a were localized to various membranes (Golgi and plasma membrane, nuclear membrane, and early endosomes, respectively). Remarkably, exogenous hypoxia (0.2% O2) in PC-3 cells induced intracellular hypoxia and changed the localization of the prenylated proteins. H-Ras and Rab5a were translocated to cytosol, and prelamin A/C was in the nucleus forming an abnormal nuclear envelope. The localization was reversed by mevalonate indicating the involvement of mevalonate pathway. In contrast, in LNCaP cells, exhibiting low intracellular oxygen concentration, H-Ras and Rab5a were localized in the cytosol, and prelamin A/C was inside the nucleus forming an inadequate nuclear envelope. Exogenous hyperoxia (40% O2) increased the intracellular oxygen concentration and induced Ras translocation from cytosol to the membrane. Prelamin A/C was translocated to the nuclear membrane and formed a proper nuclear envelope. Rab5a was translocated to the early endosomes. The specific localizations of the prenylated proteins were dependent on intracellular oxygen concentration. These results demonstrate that intracellular oxygen concentration regulates the localization and activation of prenylated proteins. |Cell Line, Tumor [MESH] |DNA, Mitochondrial/metabolism [MESH] |Endosomes/genetics/metabolism [MESH] |Humans [MESH] |Hydroxymethylglutaryl CoA Reductases [MESH] |Male [MESH] |Oxidative Phosphorylation [MESH] |Oxygen Consumption/genetics [MESH] |Oxygen/*metabolism [MESH] |Prostatic Neoplasms/genetics/*metabolism/pathology [MESH] |Protein Prenylation/*genetics [MESH]Intracellular oxygen determined by respiration regulates localization (epmc).pdf DeepDyve Pubget Overpricing