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10.1371/journal.pone.0137193 http://scihub22266oqcxt.onion/10.1371/journal.pone.0137193 C4567180!4567180!26334640     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=26334640&cmd=llinks): Failed to open stream: HTTP request failed! HTTP/1.1 429 Too Many Requests in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 215 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 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): ä 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): ä PMID26334640show 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. äThe Molecular Mechanism of Amyloid ?42 Peptide Toxicity: The Role of S(epmc).pdf DeepDyve Pubget Overpricing