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10.1038/cddis.2016.200 http://scihub22266oqcxt.onion/10.1038/cddis.2016.200 C5108309!5108309!27512953     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 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 269.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Cell+Death+Dis 2016 ; 7 (8): e2332- Nephropedia Template TP {{tp|p=27512953|t=2016. Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps |pdf=|usr=}}{{27512953}} gab.com Text Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps JO: Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=27512953 #FOAvip Neutrophil extracellular trap (NET) ejected from activated dying neutrophils is a highly ordered structure of DNA and selected proteins capable to eliminate pathogenic microorganisms. Biochemical determinants of the non-randomly formed stable NETs have not been revealed so far. Studying the formation of human NETs we have observed that polyamines were incorporated into the NET. Inhibition of myeloperoxidase, which is essential for NET formation and can generate reactive chlorinated polyamines through hypochlorous acid, decreased polyamine incorporation. Addition of exogenous primary amines that similarly to polyamines inhibit reactions catalyzed by the protein cross-linker transglutaminases (TGases) has similar effect. Proteomic analysis of the highly reproducible pattern of NET components revealed cross-linking of NET proteins through chlorinated polyamines and ?(?-glutamyl)lysine as well as bis-?-glutamyl polyamine bonds catalyzed by the TGases detected in neutrophils. Competitive inhibition of protein cross-linking by monoamines disturbed the cross-linking pattern of NET proteins, which resulted in the loss of the ordered structure of the NET and significantly reduced capacity to trap bacteria. Our findings provide explanation of how NETs are formed in a reproducible and ordered manner to efficiently neutralize microorganisms at the first defense line of the innate immune system. Twit Text FOAVip Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps ????Cell Death Dis http://www.kidney.de/pget.php?&tw=1&pmid=27512953 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27512953 #FOAvip English Wikipedia <ref>{{Cite pmid|27512953}}</ref> Protein cross-linking by chlorinated polyamines and transglutamylation stabilizes neutrophil extracellular traps #MMPMID27512953 Csomós K; Kristóf E; Jakob B; Csomós I; Kovács G; Rotem O; Hodrea J; Bagoly Z; Muszbek L; Balajthy Z; Cs?sz É; Fésüs L Cell Death Dis 2016[Aug]; 7 (8): e2332- PMID27512953show ga Neutrophil extracellular trap (NET) ejected from activated dying neutrophils is a highly ordered structure of DNA and selected proteins capable to eliminate pathogenic microorganisms. Biochemical determinants of the non-randomly formed stable NETs have not been revealed so far. Studying the formation of human NETs we have observed that polyamines were incorporated into the NET. Inhibition of myeloperoxidase, which is essential for NET formation and can generate reactive chlorinated polyamines through hypochlorous acid, decreased polyamine incorporation. Addition of exogenous primary amines that similarly to polyamines inhibit reactions catalyzed by the protein cross-linker transglutaminases (TGases) has similar effect. Proteomic analysis of the highly reproducible pattern of NET components revealed cross-linking of NET proteins through chlorinated polyamines and ?(?-glutamyl)lysine as well as bis-?-glutamyl polyamine bonds catalyzed by the TGases detected in neutrophils. Competitive inhibition of protein cross-linking by monoamines disturbed the cross-linking pattern of NET proteins, which resulted in the loss of the ordered structure of the NET and significantly reduced capacity to trap bacteria. Our findings provide explanation of how NETs are formed in a reproducible and ordered manner to efficiently neutralize microorganisms at the first defense line of the innate immune system. äProtein cross-linking by chlorinated polyamines and transglutamylation(epmc).pdf DeepDyve Pubget Overpricing