Evaluation of the specific structures of IgA1 hinge glycopeptide in 30 IgA nephropathy patients by mass spectrometry.

H Odani, K Yamamoto, S Iwayama, H Iwase… - Journal of …, 2010 - europepmc.org
H Odani, K Yamamoto, S Iwayama, H Iwase, A Takasaki, K Takahashi, Y Fujita, S Sugiyama…
Journal of nephrology, 2010europepmc.org
Background Although many reports have described the abnormal structures of O-glycan in
the IgA1 hinge region in IgA nephropathy (IgAN), the specific glycopeptide that can be used
as a diagnostic biomarker for IgAN has not yet been identified. To pursue this diagnostic
approach, we used mass spectrometric analysis to search for specific structures in IgA1
hinge glycopeptides in 30 IgAN patients contrasted with 30 healthy controls. Method IgA1
hinge glycopeptides were individually purified from the sera of 30 biopsy-proven IgAN …
Background
Although many reports have described the abnormal structures of O-glycan in the IgA1 hinge region in IgA nephropathy (IgAN), the specific glycopeptide that can be used as a diagnostic biomarker for IgAN has not yet been identified. To pursue this diagnostic approach, we used mass spectrometric analysis to search for specific structures in IgA1 hinge glycopeptides in 30 IgAN patients contrasted with 30 healthy controls.
Method
IgA1 hinge glycopeptides were individually purified from the sera of 30 biopsy-proven IgAN patients and 30 healthy controls. The structure of each glycopeptide was analyzed by ion trap mass spectrometry. Sugar conformations in each glycopeptide were estimated by collision-induced dissociation tandem mass spectrometry. Furthermore, to search for specific O-glycans in IgAN patients with a statistical significance, the identified hinge glycopeptides were analyzed by Fisher exact test.
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