Characteristics of IgA and Macromolecular IgA in Sera from IgA Nephropathy Transplanted Patients with and without IgAN Recurrence

Coppo, Rosanna; Amore, A; Cirina, Paola; Messina, Maria; Basolo, B; Segoloni, G. P.; Berthoux, F; Boulahrouz, R.; Egido, Jesús; Alcázar, Roberto

doi:10.1159/000423881

Cited by 17 publications

(6 citation statements)

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“…The increase in the IgA1 having affinity for type IV collagen (27), laminin (28), and fibronectin (29), which composed the glomerular basement membrane and mesangial matrix, had been found in patients with IgAN. Furthermore, Coppo et al suggested an important role of O-glycans in the hinge for the binding of IgA1 to type IV collagen, laminin, and fibronectin (30). Our recent study also showed that the IgA1 molecules acquired the reactivity with these extracellular matrix proteins when they were treated with sialidase.…”

Section: Discussionsupporting

confidence: 65%

Underglycosylation of IgA1 Hinge Plays a Certain Role for Its Glomerular Deposition in IgA Nephropathy

Hiki¹,

Kokubo²,

Iwase³

et al. 1999

Journal of the American Society of Nephrology

102

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Abstract. This study was performed to isolate and investigate the IgA1 that could accumulate in glomeruli (glomerulophilic IgA1). IgA1 was fractionated by the electric charge and the reactivity to Jacalin. Serum IgA1 of IgA nephropathy patients was separated and fractionated using a Jacalin column and subsequent ion-exchange chromatography. The fractions were divided into three groups of relatively cationic (C), neutral (N), and anionic (A). IgA1 was also divided into Jacalin low (L), intermediate (I), and high (H) affinity fractions by serial elution using 25, 100, and 800 mM galactose. The left kidneys of Wistar rats were perfused with 2, 5, or 10 mg of each group of IgA1. The rats were sacrificed 15 min, 30 min, 3 h, or 24 h after the perfusion. The accumulation of each IgA1 in the glomeruli was then observed by immunofluorescence. The IgA1 of the fractions N and H separated by the two methods was definitely accumulated in the rat glomeruli with a similar pattern. The electrophoresis revealed that the macromolecular IgA1 was increased in fraction H compared with other fractions. Therefore, Jacalin high-affinity IgA1 (fraction H) was applied on a diethylaminoethyl column and divided into electrically cationic (HC), neutral (HN), and anionic (HA). Only the asialo-Galβ1,3GalNAc chain was identified in the fraction HN IgA1 by gas-phase hydrazinolysis. Furthermore, the IgA1 fraction was strongly recognized by peanut agglutinin, Vicia Villosa lectins, and antisynthetic hinge peptide antibody. These results indicated that the IgA1 molecules having the underglycosylated hinge glycopeptide played a certain role in the glomerular accumulation of IgA1 in IgA nephropathy.

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Section: Discussionsupporting

confidence: 65%

Underglycosylation of IgA1 Hinge Plays a Certain Role for Its Glomerular Deposition in IgA Nephropathy

Hiki¹,

Kokubo²,

Iwase³

et al. 1999

Journal of the American Society of Nephrology

102

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“…Several recent studies have shown that a portion of IgA1 molecules in sera of IgAN patients display alterations in O-linked (9)(10)(11)(12)(13)(14)(15)(16)(17), and perhaps N-linked (10), glycans. The most frequently encountered changes were restricted to Gal (9)(10)(11)(12)(13)(14)(15)(16)(17) and NeuNAc (14) in O-linked IgA1 hinge region glycans, as determined by reactivities with NeuNAc-, Gal-, and GalNAc-specific lectins and direct carbohydrate analyses. Studies of lectin reactivities of serum fractions from IgAN patients and from healthy individuals obtained by size-exclusion chromatography revealed Gal-deficient IgA1 molecules in high-molecular-mass fractions containing IgA1 and IgG (9).…”

Section: Discussionmentioning

confidence: 99%

Circulating immune complexes in IgA nephropathy consist of IgA1 with galactose-deficient hinge region and antiglycan antibodies

Tomana¹,

Novák²,

Julian³

et al. 1999

J. Clin. Invest.

418

453

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“…Evidence that the primary cause of IgAN is extra-renal includes recurrence of the disease in 50-60% of patients undergoing renal transplantation (10)(11)(12)(13)(14). Moreover, in the few instances in which a kidney from a donor with subclinical IgAN has been engrafted into a patient with end-stage renal failure due to a disorder other than IgAN, the immune deposits cleared from the allograft within several weeks (15).…”

Section: Igan -An Immune-complex Glomerulonephritismentioning

confidence: 99%

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

Novák

Julian

Tomana

et al. 2008

Seminars in Nephrology

180

134

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Characteristics of IgA and Macromolecular IgA in Sera from IgA Nephropathy Transplanted Patients with and without IgAN Recurrence

Cited by 17 publications

References 0 publications

Underglycosylation of IgA1 Hinge Plays a Certain Role for Its Glomerular Deposition in IgA Nephropathy

Underglycosylation of IgA1 Hinge Plays a Certain Role for Its Glomerular Deposition in IgA Nephropathy

Circulating immune complexes in IgA nephropathy consist of IgA1 with galactose-deficient hinge region and antiglycan antibodies

IgA Glycosylation and IgA Immune Complexes in the Pathogenesis of IgA Nephropathy

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