Title : Increased sialylation of polymeric lambda-IgA1 in patients with IgA nephropathy.

Pub. Date : 2002

PMID : 11835525






2 Functional Relationships(s)
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1 This unusual glycosylation and sialylation pattern of the lambda-IgA1 may have important implications for the pathogenesis of IgAN, as both the masking effect of sialic acid on galactose and the reduced galactosylation will hinder the clearance of macromolecular lambda-IgA1 by asialoglycoprotein receptor of hepatocytes. N-Acetylneuraminic Acid IGAN1 Homo sapiens
2 The negative charge from sialic acid may also favor mesangial deposition of macromolecular lambda-IgA1 in IgAN. N-Acetylneuraminic Acid IGAN1 Homo sapiens