Title : Defective immunoglobulin A (IgA) glycosylation and IgA deposits in patients with IgA nephropathy.

Pub. Date : 2013 Sep

PMID : 23398317






2 Functional Relationships(s)
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1 A significant increase in N-acetylgalactosamine (GalNAc) in terminal position (p = 0.02) observed in some of the IgAN patients, became more pronounced when sialic acid was removed from IgA1, indicating enhanced expression of alpha-2,6-sialyltransferase in patients compared with controls (p < 0.0001). N-acetylgalactosaminuronic acid IGAN1 Homo sapiens
2 IgAN patients with both IgA1 and IgA2 glomerular deposits (21.7%) had increased GalNAc in terminal position (p = 0.003). N-acetylgalactosaminuronic acid IGAN1 Homo sapiens