Serum IgA Class Anti-IgA Antibody in IgA Nephropathy

Hiki, Yoshiyuki; Saitoh, Michiyo; Kobayashi, Yutaka

doi:10.1159/000186643

Cited by 17 publications

(8 citation statements)

References 10 publications

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“…This would readily explain the weak affinity of binding between Fab and Fc in rheumatoid factors, and the mon ovalency of their interaction with IgG [23] and their selective cross-reactivity with IgG from other species [23,24]. We previously reported a significant increase of serum IgA having an affinity to human IgA in patients with IgAN and with seropositive RA [25]. The IgA was speculated to be one of the rheumatoid factors because of the positive results in seropositive RA patients and the existence of IgA rheumatoid factor in IgAN patients [26,27], This hypothesis that the formation of macromolecule IgA is not due to an immunological mechanism would resolve the question put forth by Shibata [28] as to why the clinical course of IgAN is continuous and slowly pro gressive.…”

Section: Discussionmentioning

confidence: 99%

Reactivity of Glomerular and Serum lgA1 to Jacalin in IgA Nephropathy

Hiki¹,

Iwase

Saitoh³

et al. 1996

Nephron

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To analyze O-linked oligosaccharides (O-glycans) in the hinge region of IgAl in IgA nephropathy (IgAN), the reactivity of IgA1 to jacalin, which specifically binds to O-glycans, was investigated. Initially, renal biopsy specimens from 5 patients with IgAN and 3 patients with other renal diseases were investigated in an immunofluorescence study with jacalin, monoclonal antihuman IgAl and IgA2 antibodies. All of the renal biopsy specimens of IgAN and none of other renal diseases were positively stained by both FITC-labeled jacalin and monoclonal anti-IgA1 antibody. The glomerular staining patterns of FITC-jacalin were similar to those of the monoclonal anti-IgA1 antibody. IgA2 was negative in all specimens. Based on the positive reactivity of deposited IgA1 to jacalin, the binding ability of serum IgA1 to jacalin was evaluated by inhibition assay using D-galactose in patients with IgAN (n = 58), other primary glomerulonephritides (PGN) (n = 41), and healthy controls (n = 52). The frequencies of the patients with serum IgA1 having a high affinity for jacalin were significantly greater in IgAN (19/58, 32.8%) compared with the healthy controls (2/52, 3.8%) and other PGN (4/41, 9.8%). These results suggested that the increased reactivity of O-glycan(s) in the IgAl hinge region to jacalin is due to an unusual glycosylation of serum IgA1 in IgAN.

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Section: Discussionmentioning

confidence: 99%

Reactivity of Glomerular and Serum lgA1 to Jacalin in IgA Nephropathy

Hiki¹,

Iwase

Saitoh³

et al. 1996

Nephron

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“…It is suggested that IgAassociated molecules including dimeric IgA (11s) itself must contribute to the increased IgA 1 in these fractions during adolescence, since an increased production of dimeric IgA in the bone marrow [24] or an increased ratio of dimeric IgA 1 to polymeric IgA 1 in serum [25] has been demonstrated in patients with IgA nephropathy. Sancho et al [17] showed that some monomeric as well as polymeric IgA was present as immune complexes in the SDGU fractions with large sedimentation coefficients.…”

Section: Discussionmentioning

confidence: 99%

Contribution of macromolecular IgA 1 to IgA abnormality in IgA nephropathy

Itö

Waga

Tanaka

et al. 2000

Pediatric Nephrology

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To evaluate the contribution of macromolecular IgA1 to IgA abnormality in childhood IgA nephropathy, serum samples from 29 healthy children and 26 patients with IgA nephropathy in different age-groups (7-9, 10-12, and 13-15 years) were each separated by sucrose density gradient ultracentrifugation and assayed for IgA1 using an enzyme-linked immunosorbent assay. IgA1 in fraction I (sedimentation coefficient >11.4s) was significantly greater in patients 7-15 years of age (median 36.3-57.0 mg/dl) than in the age-matched controls (median 8.8-10.4 mg/dl). IgA1 in fraction II (11.4-9.3s) was significantly greater in patients 10-15 years of age (median 46.7-52.6 mg/dl) than in the controls (median 27.8-35.5 mg/dl), and IgA1 in fraction III (<9.3s) was significantly greater in patients 13-15 years of age (median 156.9 mg/dl) than in the controls (median 120.7 mg/dl). The ratio of IgA1 in fractions I-III was higher in the patients of each age-group (median 0.233-0.314) than in the controls (median 0.067-0.082), while the ratio of IgA1 in fractions II-III was not significantly high in patients 7-12 years old (median 0.268 to 0.318) compared with the controls (median 0.182-0.264). Thus, IgA abnormality in childhood IgA nephropathy would be better represented by an increase in macromolecular IgA1 of >11.4s than by an increase in IgA1 in fractions of 11.4-9.3s or <9.3s.

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“…From my previous paper on IgA-IgA binding [9] and as described in the section on CIC theory, I suspected that the incomplete carbohydrate chains in IgA1 molecules may induce self-aggregation of IgA molecules in IgAN patients. The stability of IgA1 molecules in serum samples was assessed by observing the increase in turbidity of the sample, which reflects an increase in aggregated IgA1, upon heating the sample to 63°C [31].…”

Section: Self-aggregation Of Aberrant Iga1mentioning

confidence: 99%

“…However, the theory was not consistent with the fact that the staining intensity of IgG deposition in the mesangial area was much less than that of IgA deposition in IgAN patients. On the basis of these published reports, I started to analyze the IgA that tended to bind to IgA, found that its level was increased in IgAN patients, and reported it as IgA-type anti-IgA-antibody [9]. During the course of the experiment, the question of ''Is this IgA-IgA binding really due to an immunological interaction?''…”

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confidence: 99%

O-linked oligosaccharides of the IgA1 hinge region: roles of its aberrant structure in the occurrence and/or progression of IgA nephropathy

Hiki

2009

Clin Exp Nephrol

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Primary IgA nephropathy (IgAN) has been regarded as an immune complex-mediated glomerulonephritis characterized immunohistologically by the predominant deposition of IgA in the glomerular mesangial area with a variety of histopathologic injuries (Clarkson et al. in Ann Rev Med 38:157-168, 1987). In 1992, the characteristic structure of O-linked oligosaccharides (O-glycans) in the IgA1 hinge and its possible aberrancy were simultaneously and independently proposed by Mesteckey et al. (Cont Nephrol 104:172-182, 1993), and our group (Cont Nephrol 104:217, 1993) at the International Congress of Nephrology (IgA Nephropathy 25th year) held in Nancy, France. Since then, the aberrancy has been confirmed by several research groups and is suspected to play a role in the occurrence and/or the progression of IgAN. At the end of the 1980s, I took an interest in the existence of O-glycans in the hinge region of IgA1 and have pursued the structure of the carbohydrate chains. Since an excellent review on the structure and the role of the carbohydrate in IgA molecules was recently published by Narita et al. (Clin Ex Nephrol 12:332-338, 2008), this review focuses on the process by which I developed the idea of aberrant O-glycosylation in IgA1 molecules in IgAN patients and summarizes our recent observations concerning IgA1 molecules.

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Serum IgA Class Anti-IgA Antibody in IgA Nephropathy

Cited by 17 publications

References 10 publications

Reactivity of Glomerular and Serum lgA1 to Jacalin in IgA Nephropathy

Reactivity of Glomerular and Serum lgA1 to Jacalin in IgA Nephropathy

Contribution of macromolecular IgA 1 to IgA abnormality in IgA nephropathy

O-linked oligosaccharides of the IgA1 hinge region: roles of its aberrant structure in the occurrence and/or progression of IgA nephropathy

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