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10.1016/j.cellimm.2015.06.002 http://scihub22266oqcxt.onion/10.1016/j.cellimm.2015.06.002 C4556539!4556539!26123077     free     free     free Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Immunol 2015 ; 297 (1): 40-5 Nephropedia Template TP {{tp|p=26123077|t=2015. Genipin Suppresses NLRP3 Inflammasome Activation Through Uncoupling Protein-2 |pdf=|usr=}}{{26123077}} gab.com Text Genipin Suppresses NLRP3 Inflammasome Activation Through Uncoupling Protein-2 JO: Cell Immunol http://www.kidney.de/pget.php?&tw=1&pmid=26123077 #FOAvip Incomplete clearance of apoptotic cells and reactive oxygen species (ROS) release are known to trigger inflammasome activation causing severe inflammation in acute lung injury and various metabolic and autoimmune diseases. Moreover, it has been reported that apoptotic cell clearance and ROS-mediated apoptosis critically depend on mitochondrial uncoupling protein-2 (UCP2). However, the relationship between UCP2 and inflammasome activation has not been studied. This report investigates the role of UCP2 in the expression and activation of NACHT, LRR and PYD domains-containing protein 3 (NLRP3) inflammasome in human macrophages. We found that UCP2 overexpression significantly enhanced the expression levels of NLRP3. The NLRP3 expression levels were significantly suppressed in THP1 cells treated with genipin, a UCP2 inhibitor, compared to controls. In addition, genipin altered adenosine triphosphate (ATP)- and hydrogen peroxide (H2O2)-mediated interleukin-1 beta (IL-1?) secretion and significantly suppressed caspase-1 activity in inflammasome-activated human macrophages. Taken together, our results suggest that genipin modulates NLRP3 inflammasome activation and ATP- or H2O2-mediated IL-1? release. Twit Text FOAVip Genipin Suppresses NLRP3 Inflammasome Activation Through Uncoupling Protein-2 ????Cell Immunol http://www.kidney.de/pget.php?&tw=1&pmid=26123077 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=26123077 #FOAvip English Wikipedia <ref>{{Cite pmid|26123077}}</ref> Genipin Suppresses NLRP3 Inflammasome Activation Through Uncoupling Protein-2 #MMPMID26123077 Rajanbabu V; Galam L; Fukumoto J; Enciso J; Tadikonda P; Lane TN; Bandyopadhyay S; Parthasarathy PT; Cho Y; Cho SH; Lee YC; Lockey RF; Kolliputi N Cell Immunol 2015[Sep]; 297 (1): 40-5 PMID26123077show ga Incomplete clearance of apoptotic cells and reactive oxygen species (ROS) release are known to trigger inflammasome activation causing severe inflammation in acute lung injury and various metabolic and autoimmune diseases. Moreover, it has been reported that apoptotic cell clearance and ROS-mediated apoptosis critically depend on mitochondrial uncoupling protein-2 (UCP2). However, the relationship between UCP2 and inflammasome activation has not been studied. This report investigates the role of UCP2 in the expression and activation of NACHT, LRR and PYD domains-containing protein 3 (NLRP3) inflammasome in human macrophages. We found that UCP2 overexpression significantly enhanced the expression levels of NLRP3. The NLRP3 expression levels were significantly suppressed in THP1 cells treated with genipin, a UCP2 inhibitor, compared to controls. In addition, genipin altered adenosine triphosphate (ATP)- and hydrogen peroxide (H2O2)-mediated interleukin-1 beta (IL-1?) secretion and significantly suppressed caspase-1 activity in inflammasome-activated human macrophages. Taken together, our results suggest that genipin modulates NLRP3 inflammasome activation and ATP- or H2O2-mediated IL-1? release. äGenipin Suppresses NLRP3 Inflammasome Activation Through Uncoupling Pr(epmc).pdf DeepDyve Pubget Overpricing