Aberrantly glycosylated serum IgA1 are closely associated with pathologic phenotypes of IgA nephropathy
Authors:
- 1 July 2005
- journal article
- Published by Elsevier in Kidney International
- Vol. 68 (1) , 167-172
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Aberrant glycosylation in IgA nephropathy (IgAN)Kidney International, 2004
- Binding capacity and pathophysiological effects of IgA1 from patients with IgA nephropathy on human glomerular mesangial cellsClinical and Experimental Immunology, 2004
- Enzymatically deglycosylated human IgA1 molecules accumulate and induce inflammatory cell reaction in rat glomeruliNephrology Dialysis Transplantation, 2002
- Mesangial IgA1 in IgA nephropathy exhibits aberrant O-glycosylation: Observations in three patientsKidney International, 2001
- Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathyKidney International, 2001
- Charge-dependent binding of polymeric IgA1 to human mesangial cells in IgA nephropathyKidney International, 2001
- Circulating immune complexes in IgA nephropathy consist of IgA1 with galactose-deficient hinge region and antiglycan antibodiesJournal of Clinical Investigation, 1999
- The Glycosylation and Structure of Human Serum IgA1, Fab, and Fc Regions and the Role of N-Glycosylation on Fcα Receptor InteractionsJournal of Biological Chemistry, 1998
- Galactosylation of N- and O-linked carbohydrate moieties of IgA1 and IgG in IgA nephropathyClinical and Experimental Immunology, 1995
- Pathogenesis of IgA nephropathy: In vitro activation of human mesangial cells by IgA immune complex leads to cytokine secretionThe Journal of Pathology, 1994