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10.1681/ASN.2013070771 http://scihub22266oqcxt.onion/10.1681/ASN.2013070771 C4033374!4033374!24511137     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       J+Am+Soc+Nephrol 2014 ; 25 (6): 1282-90 Nephropedia Template TP {{tp|p=24511137|t=2014. O-Linked Glycosylation Determines the Nephritogenic Potential of IgA Rheumatoid Factor |pdf=|usr=}}{{24511137}} gab.com Text O-Linked Glycosylation Determines the Nephritogenic Potential of IgA Rheumatoid Factor JO: J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=24511137 #FOAvip Deficient glycosylation of O-linked glycans in the IgA1 hinge region is associated with IgA nephropathy in humans, but the pathogenic contribution of the underlying structural aberrations remains incompletely understood. We previously showed that mice implanted with cells secreting the class-switch variant 6-19 IgA anti-IgG2a rheumatoid factor, but not 46-42 IgA anti-IgG2a rheumatoid factor, develop glomerular lesions resembling IgA nephropathy. Because the levels of O-linked glycosylation in the hinge region and the structures of N-linked glycans in the CH1 domain differ in 6-19 IgA and 46-42 IgA, we determined the respective contributions of O- and N-linked glycans to the nephritogenic potential of the 6-19 IgA rheumatoid factor in mice. Wild-type 6-19 IgA secreted by implanted cells induced significant formation of glomerular lesions, whereas poorly O-glycosylated 6-19 IgA glycovariants or a 6-19 IgA hinge mutant lacking O-linked glycans did not. However, we observed no apparent heterogeneity in the structure of N-linked glycans attached to three different sites of the Fc regions of nephritogenic and non-nephritogenic 6-19 IgAs. Collectively, our data suggest a critical role of O-linked glycans attached to the hinge region in the development of IgA nephropathy?like GN induced by 6-19 IgA rheumatoid factor in mice. Twit Text FOAVip O-Linked Glycosylation Determines the Nephritogenic Potential of IgA Rheumatoid Factor ????J Am Soc Nephrol http://www.kidney.de/pget.php?&tw=1&pmid=24511137 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=24511137 #FOAvip English Wikipedia <ref>{{Cite pmid|24511137}}</ref> O-Linked Glycosylation Determines the Nephritogenic Potential of IgA Rheumatoid Factor #MMPMID24511137 Kihara M; Ito K; Nakata J; Otani M; Tran NL; Morito N; Takahashi S; Wada Y; Izui S J Am Soc Nephrol 2014[Jun]; 25 (6): 1282-90 PMID24511137show ga Deficient glycosylation of O-linked glycans in the IgA1 hinge region is associated with IgA nephropathy in humans, but the pathogenic contribution of the underlying structural aberrations remains incompletely understood. We previously showed that mice implanted with cells secreting the class-switch variant 6-19 IgA anti-IgG2a rheumatoid factor, but not 46-42 IgA anti-IgG2a rheumatoid factor, develop glomerular lesions resembling IgA nephropathy. Because the levels of O-linked glycosylation in the hinge region and the structures of N-linked glycans in the CH1 domain differ in 6-19 IgA and 46-42 IgA, we determined the respective contributions of O- and N-linked glycans to the nephritogenic potential of the 6-19 IgA rheumatoid factor in mice. Wild-type 6-19 IgA secreted by implanted cells induced significant formation of glomerular lesions, whereas poorly O-glycosylated 6-19 IgA glycovariants or a 6-19 IgA hinge mutant lacking O-linked glycans did not. However, we observed no apparent heterogeneity in the structure of N-linked glycans attached to three different sites of the Fc regions of nephritogenic and non-nephritogenic 6-19 IgAs. Collectively, our data suggest a critical role of O-linked glycans attached to the hinge region in the development of IgA nephropathy?like GN induced by 6-19 IgA rheumatoid factor in mice. äO-Linked Glycosylation Determines the Nephritogenic Potential of IgA R(epmc).pdf DeepDyve Pubget Overpricing