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10.18632/oncotarget.3573 http://scihub22266oqcxt.onion/10.18632/oncotarget.3573 C4484443!4484443 !25798539     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=25798539 &cmd=llinks): Failed to open stream: HTTP request failed! 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RNA-dependent protein kinase (PKR) depletes nutrients, inducing phosphorylation of AMP-activated kinase in lung cancer |pdf=|usr=}}{{25798539 }} gab.com Text RNA-dependent protein kinase (PKR) depletes nutrients, inducing phosphorylation of AMP-activated kinase in lung cancer JO: Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=25798539 #FOAvip We have demonstrated that RNA-dependent protein kinase (PKR) and its downstream protein p-eIF2? are independent prognostic markers for overall survival in lung cancer. In the current study, we further investigate the interaction between PKR and AMPK in lung tumor tissue and cancer cell lines. We examined PKR protein expression in 55 frozen primary lung tumor tissues by Western blotting and analyzed the association between PKR expression and expression of 139 proteins on tissue samples examined previously by Reverse Phase Protein Array (RPPA) from the same 55 patients. We observed that biomarkers were either positively (phosphorylated AMP-activated kinase(T172) [p-AMPK]) or negatively (insulin receptor substrate 1, meiotic recombination 11, ATR interacting protein, telomerase, checkpoint kinase 1, and cyclin E1) correlated with PKR. We further confirmed that induction of PKR with expression vectors in lung cancer cells causes activation of the AMPK protein independent of the LKB1, TAK1, and CaMKK? pathway. We found that PKR causes nutrient depletion, which increases AMP levels and decreases ATP levels, causing AMPK phosphorylation. We further demonstrated that inhibiting AMPK expression with compound C or siRNA enhanced PKR-mediated cell death. We next explored the combination of PKR and p-AMPK expression in NSCLC patients and observed that expression of p-AMPK predicted a poor outcome for adenocarcinoma patients with high PKR expression and a better prognosis for those with low PKR expression. These findings were consistent with our in vitro results. AMPK might rescue cells facing metabolic stresses, such as ATP depletion caused by PKR. Our data indicate that PKR causes nutrient depletion, which induces the phosphorylation of AMPK. AMPK might act as a protective response to metabolic stresses, such as nutrient deprivation. Twit Text FOAVip RNA-dependent protein kinase (PKR) depletes nutrients, inducing phosphorylation of AMP-activated kinase in lung cancer ????Oncotarget http://www.kidney.de/pget.php?&tw=1&pmid=25798539 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=25798539 #FOAvip English Wikipedia <ref>{{Cite pmid|25798539 }}</ref> RNA-dependent protein kinase (PKR) depletes nutrients, inducing phosphorylation of AMP-activated kinase in lung cancer #MMPMID25798539 Guo C ; Hao C ; Shao R ; Fang B ; Correa AM ; Hofstetter WL ; Roth JA ; Behrens C ; Kalhor N ; Wistuba II ; Swisher SG ; Pataer A Oncotarget 2015[May]; 6 (13 ): 11114-24 PMID25798539 show ga We have demonstrated that RNA-dependent protein kinase (PKR) and its downstream protein p-eIF2? are independent prognostic markers for overall survival in lung cancer. In the current study, we further investigate the interaction between PKR and AMPK in lung tumor tissue and cancer cell lines. We examined PKR protein expression in 55 frozen primary lung tumor tissues by Western blotting and analyzed the association between PKR expression and expression of 139 proteins on tissue samples examined previously by Reverse Phase Protein Array (RPPA) from the same 55 patients. We observed that biomarkers were either positively (phosphorylated AMP-activated kinase(T172) [p-AMPK]) or negatively (insulin receptor substrate 1, meiotic recombination 11, ATR interacting protein, telomerase, checkpoint kinase 1, and cyclin E1) correlated with PKR. We further confirmed that induction of PKR with expression vectors in lung cancer cells causes activation of the AMPK protein independent of the LKB1, TAK1, and CaMKK? pathway. We found that PKR causes nutrient depletion, which increases AMP levels and decreases ATP levels, causing AMPK phosphorylation. We further demonstrated that inhibiting AMPK expression with compound C or siRNA enhanced PKR-mediated cell death. We next explored the combination of PKR and p-AMPK expression in NSCLC patients and observed that expression of p-AMPK predicted a poor outcome for adenocarcinoma patients with high PKR expression and a better prognosis for those with low PKR expression. These findings were consistent with our in vitro results. AMPK might rescue cells facing metabolic stresses, such as ATP depletion caused by PKR. Our data indicate that PKR causes nutrient depletion, which induces the phosphorylation of AMPK. AMPK might act as a protective response to metabolic stresses, such as nutrient deprivation. |AMP-Activated Protein Kinases/antagonists & inhibitors/*metabolism [MESH] |Adenocarcinoma/*metabolism/mortality/pathology [MESH] |Adenosine Monophosphate/metabolism [MESH] |Adenosine Triphosphate/metabolism [MESH] |Blotting, Western [MESH] |Carcinoma, Non-Small-Cell Lung/*metabolism/mortality/pathology [MESH] |Carcinoma, Squamous Cell/*metabolism/mortality/pathology [MESH] |Flow Cytometry [MESH] |Glucose/*deficiency [MESH] |Humans [MESH] |Immunoenzyme Techniques [MESH] |Lactates/metabolism [MESH] |Lung Neoplasms/*metabolism/mortality/pathology [MESH] |Neoplasm Staging [MESH] |Prognosis [MESH] |Survival Rate [MESH] |Tumor Cells, Cultured [MESH]RNA-dependent protein kinase (PKR) depletes nutrients, inducing phosph(epmc).pdf DeepDyve Pubget Overpricing