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10.1681/ASN.2015070745 http://scihub22266oqcxt.onion/10.1681/ASN.2015070745 C5407710!5407710!27932477     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 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 265.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       J+Am+Soc+Nephrol 2017 ; 28 (5): 1462-74 Nephropedia Template TP {{tp|p=27932477|t=2017. Moss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic Application in Complement Disorders |pdf=|usr=}}{{27932477}} gab.com Text Moss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic Application in Complement Disorders JO: J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=27932477 #FOAvip Genetic defects in complement regulatory proteins can lead to severe renal diseases, including atypical hemolytic uremic syndrome and C3 glomerulopathies, and age-related macular degeneration. The majority of the mutations found in patients with these diseases affect the glycoprotein complement factor H, the main regulator of the alternative pathway of complement activation. Therapeutic options are limited, and novel treatments, specifically those targeting alternative pathway activation, are highly desirable. Substitution with biologically active factor H could potentially treat a variety of diseases that involve increased alternative pathway activation, but no therapeutic factor H is commercially available. We recently reported the expression of full-length recombinant factor H in moss (Physcomitrella patens). Here, we present the production of an improved moss-derived recombinant human factor H devoid of potentially immunogenic plant?specific sugar residues on protein N-glycans, yielding approximately 1 mg purified moss?derived human factor H per liter of initial P. patens culture after a multistep purification process. This glycosylation-optimized factor H showed full in vitro complement regulatory activity similar to that of plasma-derived factor H and efficiently blocked LPS-induced alternative pathway activation and hemolysis induced by sera from patients with atypical hemolytic uremic syndrome. Furthermore, injection of moss-derived factor H reduced C3 deposition and increased serum C3 levels in a murine model of C3 glomerulopathy. Thus, we consider moss-produced recombinant human factor H a promising pharmaceutical product for therapeutic intervention in patients suffering from complement dysregulation. Twit Text FOAVip Moss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic Application in Complement Disorders ????J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=27932477 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=27932477 #FOAvip English Wikipedia <ref>{{Cite pmid|27932477}}</ref> Moss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic Application in Complement Disorders #MMPMID27932477 Michelfelder S; Parsons J; Bohlender LL; Hoernstein SN; Niederkrüger H; Busch A; Krieghoff N; Koch J; Fode B; Schaaf A; Frischmuth T; Pohl M; Zipfel PF; Reski R; Decker EL; Häffner K J Am Soc Nephrol 2017[May]; 28 (5): 1462-74 PMID27932477show ga Genetic defects in complement regulatory proteins can lead to severe renal diseases, including atypical hemolytic uremic syndrome and C3 glomerulopathies, and age-related macular degeneration. The majority of the mutations found in patients with these diseases affect the glycoprotein complement factor H, the main regulator of the alternative pathway of complement activation. Therapeutic options are limited, and novel treatments, specifically those targeting alternative pathway activation, are highly desirable. Substitution with biologically active factor H could potentially treat a variety of diseases that involve increased alternative pathway activation, but no therapeutic factor H is commercially available. We recently reported the expression of full-length recombinant factor H in moss (Physcomitrella patens). Here, we present the production of an improved moss-derived recombinant human factor H devoid of potentially immunogenic plant?specific sugar residues on protein N-glycans, yielding approximately 1 mg purified moss?derived human factor H per liter of initial P. patens culture after a multistep purification process. This glycosylation-optimized factor H showed full in vitro complement regulatory activity similar to that of plasma-derived factor H and efficiently blocked LPS-induced alternative pathway activation and hemolysis induced by sera from patients with atypical hemolytic uremic syndrome. Furthermore, injection of moss-derived factor H reduced C3 deposition and increased serum C3 levels in a murine model of C3 glomerulopathy. Thus, we consider moss-produced recombinant human factor H a promising pharmaceutical product for therapeutic intervention in patients suffering from complement dysregulation. äMoss-Produced, Glycosylation-Optimized Human Factor H for Therapeutic (epmc).pdf DeepDyve Pubget Overpricing