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10.4049/jimmunol.1303062 http://scihub22266oqcxt.onion/10.4049/jimmunol.1303062 C4036085!4036085!24771854     free     free     free Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 233.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 267.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Immunol 2014 ; 192 (11): 5363-72 Nephropedia Template TP {{tp|p=24771854|t=2014. Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced sepsis |pdf=|usr=}}{{24771854}} gab.com Text Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced sepsis JO: J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=24771854 #FOAvip Cathelicidin LL-37 plays an essential role in innate immunity by killing invading microorganisms and regulating the inflammatory response. These activities depend on the cationic character of the peptide, which is conferred by arginine and lysine residues. At inflammatory foci in vivo, LL-37 is exposed to peptidyl arginine deiminase (PAD), an enzyme released by inflammatory cells. Therefore, we hypothesised that PAD-mediated citrullination of the arginine residues within LL-37 will abrogate its immunomodulatory functions. We found that when citrullinated, LL-37 was at least 40 times less efficient at neutralising the proinflammatory activity of LPS due to a marked decrease in its affinity for endotoxin. Also, the ability of citrullinated LL-37 to quench macrophage responses to LTA and Poly (I:C) signalling via TLR2 and TLR3, respectively, was significantly reduced. Furthermore, in stark contrast to native LL-37, the modified peptide completely lost the ability to prevent morbidity and mortality in a mouse model of D-galactosamine-sensitised endotoxin shock. In fact, administration of citrullinated LL-37 plus endotoxin actually exacerbated sepsis due to the inability of LL-37 to neutralise LPS and the subsequent enhancement of systemic inflammation due to increased serum levels of IL-6. Importantly, serum from septic mice showed increased PAD activity, which strongly correlated with the level of citrullination, indicating that PAD-driven protein modification occurs in vivo. Since LL-37 is a potential treatment for sepsis, its administration should be preceded by a careful analysis to ensure that the citrullinated peptide, is not generated in treated patients. Twit Text FOAVip Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced sepsis ????J Immunol http://www.kidney.de/pget.php?&tw=1&pmid=24771854 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24771854 #FOAvip English Wikipedia <ref>{{Cite pmid|24771854}}</ref> Citrullination alters immunomodulatory function of LL-37 essential for prevention of endotoxin-induced sepsis #MMPMID24771854 Koziel J; Bryzek D; Sroka A; Maresz K; Glowczyk I; Bielecka E; Kantyka T; Pyr? K; Svoboda P; Pohl J; Potempa J J Immunol 2014[Jun]; 192 (11): 5363-72 PMID24771854show ga Cathelicidin LL-37 plays an essential role in innate immunity by killing invading microorganisms and regulating the inflammatory response. These activities depend on the cationic character of the peptide, which is conferred by arginine and lysine residues. At inflammatory foci in vivo, LL-37 is exposed to peptidyl arginine deiminase (PAD), an enzyme released by inflammatory cells. Therefore, we hypothesised that PAD-mediated citrullination of the arginine residues within LL-37 will abrogate its immunomodulatory functions. We found that when citrullinated, LL-37 was at least 40 times less efficient at neutralising the proinflammatory activity of LPS due to a marked decrease in its affinity for endotoxin. Also, the ability of citrullinated LL-37 to quench macrophage responses to LTA and Poly (I:C) signalling via TLR2 and TLR3, respectively, was significantly reduced. Furthermore, in stark contrast to native LL-37, the modified peptide completely lost the ability to prevent morbidity and mortality in a mouse model of D-galactosamine-sensitised endotoxin shock. In fact, administration of citrullinated LL-37 plus endotoxin actually exacerbated sepsis due to the inability of LL-37 to neutralise LPS and the subsequent enhancement of systemic inflammation due to increased serum levels of IL-6. Importantly, serum from septic mice showed increased PAD activity, which strongly correlated with the level of citrullination, indicating that PAD-driven protein modification occurs in vivo. Since LL-37 is a potential treatment for sepsis, its administration should be preceded by a careful analysis to ensure that the citrullinated peptide, is not generated in treated patients. äCitrullination alters immunomodulatory function of LL-37 essential for(epmc).pdf DeepDyve Pubget Overpricing