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10.3389/fimmu.2018.00553 http://scihub22266oqcxt.onion/10.3389/fimmu.2018.00553 C5867308!5867308!29616041     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Front+Immunol 2018 ; 9 (ä): ä Nephropedia Template TP {{tp|p=29616041|t=2018. Novel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmune Diseases |pdf=|usr=}}{{29616041}} gab.com Text Novel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmune Diseases JO: Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=29616041 #FOAvip The composition of the conserved N297 glycan in immunoglobulin G (IgG) has been shown to affect antibody effector functions via C1q of the complement system and Fc gamma receptors (Fc?R) on immune cells. Changes in the general levels of IgG-glycoforms, such as lowered total IgG galactosylation observed in many autoimmune diseases have been associated with elevated disease severity. Agalactosyslated IgG has therefore been regarded and classified by many as pro-inflammatory. However, and somewhat counterintuitively, agalactosylation has been shown by several groups to decrease affinity for Fc?RIII and decrease C1q binding and downstream activation, which seems at odds with this proposed pro-inflammatory nature. In this review, we discuss these circumstances where altered IgG galactosylation/glycosylation is found. We propose a novel model based on these observations and current biochemical evidence, where the levels of IgG galactosylation found in the total bulk IgG affect the threshold required to achieve immune activation by autoantibodies through either C1q or Fc?R. Although this model needs experimental verification, it is supported by several clinical observations and reconciles apparent discrepancies in the literature, and suggests a general mechanism in IgG-mediated autoimmune diseases. Twit Text FOAVip Novel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmune Diseases ????Front Immunol http://www.kidney.de/pget.php?&tw=1&pmid=29616041 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=29616041 #FOAvip English Wikipedia <ref>{{Cite pmid|29616041}}</ref> Novel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmune Diseases #MMPMID29616041 Dekkers G; Rispens T; Vidarsson G Front Immunol 2018[]; 9 (ä): ä PMID29616041show ga The composition of the conserved N297 glycan in immunoglobulin G (IgG) has been shown to affect antibody effector functions via C1q of the complement system and Fc gamma receptors (Fc?R) on immune cells. Changes in the general levels of IgG-glycoforms, such as lowered total IgG galactosylation observed in many autoimmune diseases have been associated with elevated disease severity. Agalactosyslated IgG has therefore been regarded and classified by many as pro-inflammatory. However, and somewhat counterintuitively, agalactosylation has been shown by several groups to decrease affinity for Fc?RIII and decrease C1q binding and downstream activation, which seems at odds with this proposed pro-inflammatory nature. In this review, we discuss these circumstances where altered IgG galactosylation/glycosylation is found. We propose a novel model based on these observations and current biochemical evidence, where the levels of IgG galactosylation found in the total bulk IgG affect the threshold required to achieve immune activation by autoantibodies through either C1q or Fc?R. Although this model needs experimental verification, it is supported by several clinical observations and reconciles apparent discrepancies in the literature, and suggests a general mechanism in IgG-mediated autoimmune diseases. äNovel Concepts of Altered Immunoglobulin G Galactosylation in Autoimmu(epmc).pdf DeepDyve Pubget Overpricing