Title : Mass spectrometry proves under-O-glycosylation of glomerular IgA1 in IgA nephropathy.

Pub. Date : 2001 Mar

PMID : 11231363






5 Functional Relationships(s)
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1 The variety of O-glycan glycoform was determined by estimating the precise molecular weights of the IgA1 hinge glycopeptides using matrix-assisted laser desorption ionization time of flight mass spectrometry. Glycopeptides immunoglobulin heavy constant alpha 1 Homo sapiens
2 RESULTS: The peak distribution of IgA1 hinge glycopeptides clearly shifted to lesser molecular weights in both glomerular and serum IgA1 in IgAN compared with the serum IgA1 of controls. Glycopeptides immunoglobulin heavy constant alpha 1 Homo sapiens
3 RESULTS: The peak distribution of IgA1 hinge glycopeptides clearly shifted to lesser molecular weights in both glomerular and serum IgA1 in IgAN compared with the serum IgA1 of controls. Glycopeptides immunoglobulin heavy constant alpha 1 Homo sapiens
4 RESULTS: The peak distribution of IgA1 hinge glycopeptides clearly shifted to lesser molecular weights in both glomerular and serum IgA1 in IgAN compared with the serum IgA1 of controls. Glycopeptides immunoglobulin heavy constant alpha 1 Homo sapiens
5 These results indicate that the decreased sialylation and galactosylation of the IgA1 hinge glycopeptides play a crucial role in its glomerular deposition in IgAN. Glycopeptides immunoglobulin heavy constant alpha 1 Homo sapiens