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10.1016/j.redox.2018.03.009 http://scihub22266oqcxt.onion/10.1016/j.redox.2018.03.009 C5952998!5952998!29573705     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Redox+Biol 2018 ; 16 (ä): 314-21 Nephropedia Template TP {{tp|p=29573705|t=2018. Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases |pdf=|usr=}}{{29573705}} gab.com Text Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases JO: Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=29573705 #FOAvip Collagen IV is a major component of the basement membrane in epithelial tissues. The NC1 domains of collagen IV protomers are covalently linked together through sulfilimine bonds, the formation of which is catalyzed by peroxidasin. Although hydrogen peroxide is essential for this reaction, the exact source of the oxidant remains elusive. Members of the NOX/DUOX NADPH oxidase family are specifically devoted to the production of superoxide and hydrogen peroxide. Our aim in this study was to find out if NADPH oxidases contribute in vivo to the formation of collagen IV sulfilimine crosslinks. We used multiple genetically modified in vivo model systems to provide a detailed assessment of this question. Our data indicate that in various peroxidasin-expressing tissues sulfilimine crosslinks between the NC1 domains of collagen IV can be readily detected in the absence of functioning NADPH oxidases. We also analyzed how subatmospheric oxygen levels influence the collagen IV network in collagen-producing cultured cells with rapid matrix turnover. We showed that collagen IV crosslinks remain intact even under strongly hypoxic conditions. Our hypothesis is that during collagen IV network formation PXDN cooperates with a NOX/DUOX-independent H2O2 source that is functional also at very low ambient oxygen levels. Twit Text FOAVip Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases ????Redox Biol http://www.kidney.de/pget.php?&tw=1&pmid=29573705 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29573705 #FOAvip English Wikipedia <ref>{{Cite pmid|29573705}}</ref> Peroxidasin-mediated crosslinking of collagen IV is independent of NADPH oxidases #MMPMID29573705 Sirokmány G; Kovács HA; Lázár E; Kónya K; Donkó Á; Enyedi B; Grasberger H; Geiszt M Redox Biol 2018[Jun]; 16 (ä): 314-21 PMID29573705show ga Collagen IV is a major component of the basement membrane in epithelial tissues. The NC1 domains of collagen IV protomers are covalently linked together through sulfilimine bonds, the formation of which is catalyzed by peroxidasin. Although hydrogen peroxide is essential for this reaction, the exact source of the oxidant remains elusive. Members of the NOX/DUOX NADPH oxidase family are specifically devoted to the production of superoxide and hydrogen peroxide. Our aim in this study was to find out if NADPH oxidases contribute in vivo to the formation of collagen IV sulfilimine crosslinks. We used multiple genetically modified in vivo model systems to provide a detailed assessment of this question. Our data indicate that in various peroxidasin-expressing tissues sulfilimine crosslinks between the NC1 domains of collagen IV can be readily detected in the absence of functioning NADPH oxidases. We also analyzed how subatmospheric oxygen levels influence the collagen IV network in collagen-producing cultured cells with rapid matrix turnover. We showed that collagen IV crosslinks remain intact even under strongly hypoxic conditions. Our hypothesis is that during collagen IV network formation PXDN cooperates with a NOX/DUOX-independent H2O2 source that is functional also at very low ambient oxygen levels. äPeroxidasin-mediated crosslinking of collagen IV is independent of NAD(epmc).pdf DeepDyve Pubget Overpricing