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2014 ; 13
(11
): 3097-113
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Identification of distinct glycoforms of IgA1 in plasma from patients with
immunoglobulin A (IgA) nephropathy and healthy individuals
#MMPMID25071157
Lehoux S
; Mi R
; Aryal RP
; Wang Y
; Schjoldager KT
; Clausen H
; van Die I
; Han Y
; Chapman AB
; Cummings RD
; Ju T
Mol Cell Proteomics
2014[Nov]; 13
(11
): 3097-113
PMID25071157
show ga
Immunoglobulin A nephropathy (IgAN) is the most common form of glomerulonephritis
worldwide and is histologically characterized by the deposition of IgA1 and
consequent inflammation in the glomerular mesangium. Prior studies suggested that
serum IgA1 from IgAN patients contains aberrant, undergalactosylated O-glycans,
for example, Tn antigen and its sialylated version, SialylTn (STn), but the
mechanisms underlying aberrant O-glycosylation are not well understood. Here we
have used serial lectin separation technologies, Western blot, enzymatic
modifications, and mass spectrometry to explore whether there are different
glycoforms of IgA1 in plasma from patients with IgAN and healthy individuals.
Although total plasma IgA in IgAN patients was elevated ? 1.6-fold compared with
that in healthy donors, IgA1 in all samples was unexpectedly separable into two
distinct glycoforms: one with core 1 based O-glycans, and the other exclusively
containing Tn/STn structures. Importantly, Tn antigen present on IgA1 from IgAN
patients and controls was convertible into the core 1 structure in vitro by
recombinant T-synthase. Our results demonstrate that undergalactosylation of
O-glycans in IgA1 is not restricted to IgAN and suggest that in vivo inefficiency
of T-synthase toward IgA1 in a subpopulation of B or plasma cells, as well as
overall elevation of IgA, may contribute to IgAN pathogenesis.
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