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pubmed-article:17957128pubmed:abstractTextIgA nephropathy (IgAN) is characterized by mesangial deposition of polymeric IgA1 (pIgA1), yet the pathogeneic mechanism remains unresolved. In the present study, we examined the glycosylation profile of differently charged IgA1 from IgAN patients. The binding characteristics of these IgA1 fractions to cultured human mesangial cells (HMC) and hepatoma cell lines (HepG2) were studied.lld:pubmed
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pubmed-article:17957128pubmed:authorpubmed-author:RayR GRGlld:pubmed
pubmed-article:17957128pubmed:authorpubmed-author:LaiKar NengKNlld:pubmed
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pubmed-article:17957128pubmed:copyrightInfoCopyright 2007 S. Karger AG, Basel.lld:pubmed
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pubmed-article:17957128pubmed:volume107lld:pubmed
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pubmed-article:17957128pubmed:year2007lld:pubmed
pubmed-article:17957128pubmed:articleTitleGlycosylation profile of differently charged IgA1 and their binding characteristics to cultured mesangial cells in IgA nephropathy.lld:pubmed
pubmed-article:17957128pubmed:affiliationDepartment of Medicine, Queen Mary Hospital, University of Hong Kong, Hong Kong, SAR, China.lld:pubmed
pubmed-article:17957128pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:17957128pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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