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10.1371/journal.pone.0137193 http://scihub22266oqcxt.onion/10.1371/journal.pone.0137193 C4567180!4567180 !26334640     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 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 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\26334640 .jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       PLoS+One 2015 ; 10 (9 ): e0137193 Nephropedia Template TP {{tp|p=26334640 |t=2015. The Molecular Mechanism of Amyloid ?42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins |pdf=|usr=}}{{26334640 }} gab.com Text The Molecular Mechanism of Amyloid 42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins JO: PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26334640 #FOAvip Our study focused on the relationship between amyloid ? 1-42 (A?), sphingosine kinases (SphKs) and mitochondrial sirtuins in regulating cell fate. SphK1 is a key enzyme involved in maintaining sphingolipid rheostat in the brain. Deregulation of the sphingolipid metabolism may play a crucial role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial function and mitochondrial deacetylases, i.e. sirtuins (Sirt3,-4,-5), are also important for cell viability. In this study, we evaluated the interaction between A?1-42, SphKs and Sirts in cell survival/death, and we examined several compounds to indicate possible target(s) for a strategy protecting against cytotoxicity of A?1-42. PC12 cells were subjected to A?1-42 oligomers and SphK inhibitor SKI II for 24-96 h. Our data indicated that A?1-42 enhanced SphK1 expression and activity after 24 h, but down-regulated them after 96 h and had no effect on Sphk2. A?1-42 and SKI II induced free radical formation, disturbed the balance between pro- and anti-apoptotic proteins and evoked cell death. Simultaneously, up-regulation of anti-oxidative enzymes catalase and superoxide dismutase 2 was observed. Moreover, the total protein level of glycogen synthase kinase-3? was decreased. A?1-42 significantly increased the level of mitochondrial proteins: apoptosis-inducing factor AIF and Sirt3, -4, -5. By using several pharmacologically active compounds we showed that p53 protein plays a significant role at very early stages of A?1-42 toxicity. However, during prolonged exposure to A?1-42, the activation of caspases, MEK/ERK, and alterations in mitochondrial permeability transition pores were additional factors leading to cell death. Moreover, SphK product, sphingosine-1-phosphate (S1P), and Sirt activators and antioxidants, resveratrol and quercetin, significantly enhanced viability of cells subjected to A?1-42. Our data indicated that p53 protein and inhibition of SphKs may be early key events responsible for cell death evoked by A?1-42. We suggest that activation of S1P-dependent signalling and Sirts may offer a promising cytoprotective strategy. Twit Text FOAVip The Molecular Mechanism of Amyloid 42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins ????PLoS One http://www.kidney.de/pget.php?&tw=1&pmid=26334640 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26334640 #FOAvip English Wikipedia <ref>{{Cite pmid|26334640 }}</ref> The Molecular Mechanism of Amyloid ?42 Peptide Toxicity: The Role of Sphingosine Kinase-1 and Mitochondrial Sirtuins #MMPMID26334640 Cie?lik M ; Czapski GA ; Strosznajder JB PLoS One 2015[]; 10 (9 ): e0137193 PMID26334640 show ga Our study focused on the relationship between amyloid ? 1-42 (A?), sphingosine kinases (SphKs) and mitochondrial sirtuins in regulating cell fate. SphK1 is a key enzyme involved in maintaining sphingolipid rheostat in the brain. Deregulation of the sphingolipid metabolism may play a crucial role in the pathogenesis of Alzheimer's disease (AD). Mitochondrial function and mitochondrial deacetylases, i.e. sirtuins (Sirt3,-4,-5), are also important for cell viability. In this study, we evaluated the interaction between A?1-42, SphKs and Sirts in cell survival/death, and we examined several compounds to indicate possible target(s) for a strategy protecting against cytotoxicity of A?1-42. PC12 cells were subjected to A?1-42 oligomers and SphK inhibitor SKI II for 24-96 h. Our data indicated that A?1-42 enhanced SphK1 expression and activity after 24 h, but down-regulated them after 96 h and had no effect on Sphk2. A?1-42 and SKI II induced free radical formation, disturbed the balance between pro- and anti-apoptotic proteins and evoked cell death. Simultaneously, up-regulation of anti-oxidative enzymes catalase and superoxide dismutase 2 was observed. Moreover, the total protein level of glycogen synthase kinase-3? was decreased. A?1-42 significantly increased the level of mitochondrial proteins: apoptosis-inducing factor AIF and Sirt3, -4, -5. By using several pharmacologically active compounds we showed that p53 protein plays a significant role at very early stages of A?1-42 toxicity. However, during prolonged exposure to A?1-42, the activation of caspases, MEK/ERK, and alterations in mitochondrial permeability transition pores were additional factors leading to cell death. Moreover, SphK product, sphingosine-1-phosphate (S1P), and Sirt activators and antioxidants, resveratrol and quercetin, significantly enhanced viability of cells subjected to A?1-42. Our data indicated that p53 protein and inhibition of SphKs may be early key events responsible for cell death evoked by A?1-42. We suggest that activation of S1P-dependent signalling and Sirts may offer a promising cytoprotective strategy. |Amyloid beta-Peptides/*toxicity [MESH] |Animals [MESH] |Mitochondria/*metabolism [MESH] |PC12 Cells [MESH] |Peptide Fragments/*toxicity [MESH] |Phosphotransferases (Alcohol Group Acceptor)/*metabolism [MESH] |Rats [MESH]The Molecular Mechanism of Amyloid ?42 Peptide Toxicity: The Role of S(epmc).pdf DeepDyve Pubget Overpricing