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  • 1
    Electronic Resource
    Electronic Resource
    Pathogenic potential of galactose-deficient IgA1 in IgA nephropathy (2002)
    Oxford, UK : Blackwell Publishing Ltd
    Nephrology 7 (2002), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SUMMARY: Recent studies have demonstrated that immune complexes (IC) in the circulation and mesangial deposits in IgA nephropathy (IgAN) patients contain IgA1 molecules deficient in galactose (Gal) in their O-linked hinge-region-associated glycans. Due to this Gal deficiency, terminal N-acetylgalactosamine (GaINAc) in these side chains is recognized by naturally occurring IgG and IgA1 antibodies as an antigenic determinant responsible for the formation of IC. Thus, IgAN can be classified as one of several human autoimmune diseases in which glycan aberrancies play a pathogenic role. In a rare disease, Tn syndrome, terminal GaINAc on cell surface glycoproteins of erythrocytes, platelets, lymphocytes, and/or monocytes is recognized by GaINAc-specific antibodies, resulting in their in vitro agglutination and in vivo manifestations (anaemia and thrombocytopenia). However, the antigenic determinants and corresponding antibodies in Tn syndrome differ from those of IgAN. the Tn antigen is composed of three adjacent GaINAc residues, a configuration not present in the IgA1 hinge region. the anti-Tn antibodies are of the IgM isotype while GaINAc-specific antibodies in IgAN patients are of the IgG and IgA1 isotypes. Furthermore, monoclonal antibodies to the Tn antigen and sialylated Tn antigens (NeuAcα2,6GaINAc) do not react with intact or glycan-modified IgA1 myeloma proteins. Antibodies to GaINAc are present in cord blood (devoid of IgM and IgA1) and in purified serum IgG. the true antigen (Gal-deficient IgA1)-antibody (IgG or IgA1) interaction, rather than nonspecific aggregation, was demonstrated by the dissociation of circulating IC from IgAN patients at acid pH but not in high-salt concentrations, and the in vitro reassociation at neutral pH (and its inhibition by de-galactosylated IgA1). the binding of anti-GaINAc antibodies to Gal-deficient IgA1 profoundly influences the catabolism and tissue distribution of the IgA1. the masking of GaINAc residues by corresponding antibodies diminishes binding to the hepatic asialoglycoprotein receptor (ASGP-R) specific for terminal Gal and GaINAc residues of glycoproteins, and results in the deposition of IgA1-containing IC deposit in the renal mesangium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1797.2002.tb00517.x
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  • 2
    Electronic Resource
    Electronic Resource
    Treatment options in IgA nephropathy (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Nephrology 3 (1997), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: IgA nephropathy (Berger's disease), the most common primary glomerulonephritis worldwide, leads to end-stage renal failure in 20–40% of patients after 20 years of clinical disease. No consensus has emerged about treatment to slow or prevent the loss of renal function, and in large part this has been due to a critical lack of understanding of the pathogenetic mechanisms. Several approaches that reduce glomerular scarring and inflammation in other renal diseases, including fish oil supplements, anti-inflammatory agents and angiotensin-converting enzyme inhibitors, have been used, with variable results. For patients reaching end-stage, transplantation has shown excellent long-term outcomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1797.1997.tb00198.x
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  • 3
    Electronic Resource
    Electronic Resource
    Pathogenic potential of galactose-deficient IgA1 in IgA nephropathy (2002)
    Oxford, UK : Blackwell Science Pty
    Nephrology 7 (2002), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: SUMMARY: Recent studies have demonstrated that immune complexes (IC) in the circulation and mesangial deposits in IgA nephropathy (IgAN) patients contain IgA1 molecules deficient in galactose (Gal) in their O-linked hinge-region-associated glycans. Due to this Gal deficiency, terminal n-acetylgalactosamine (GalNAc) in these side chains is recognized by naturally occurring IgG and IgA1 antibodies as an antigenic determinant responsible for the formation of IC. Thus, IgAN can be classified as one of several human autoimmune diseases in which glycan aberrancies play a pathogenic role. In a rare disease, Tn syndrome, terminal GalNAc on cell surface glycoproteins of erythrocytes, platelets, lymphocytes, and/or monocytes is recognized by GalNAc-specific antibodies, resulting in their in vitro agglutination and in vivo manifestations (anaemia and thrombocytopenia). However, the antigenic determinants and corresponding antibodies in Tn syndrome differ from those of IgAN. The Tn antigen is composed of three adjacent GalNAc residues, a configuration not present in the IgA1 hinge region. The anti-Tn antibodies are of the IgM isotype while GalNAc-specific antibodies in IgAN patients are of the IgG and IgA1 isotypes. Furthermore, monoclonal antibodies to the Tn antigen and sialylated Tn antigens (NeuAcα2,6GalNAc) do not react with intact or glycan-modified IgA1 myeloma proteins. Antibodies to GalNAc are present in cord blood (devoid of IgM and IgA1) and in purified serum IgG. The true antigen (Gal-deficient IgA1)–antibody (IgG or IgA1) interaction, rather than non-specific aggregation, was demonstrated by the dissociation of circulating IC from IgAN patients at acid pH but not in high-salt concentrations, and the in vitro reassociation at neutral pH (and its inhibition by de-galactosylated IgA1). The binding of anti-GalNAc antibodies to Gal-deficient IgA1 profoundly influences the catabolism and tissue distribution of the IgA1. The masking of GalNAc residues by corresponding antibodies diminishes binding to the hepatic asialoglycoprotein receptor (ASGP-R) specific for terminal Gal and GalNAc residues of glycoproteins, and results in the deposition of IgA1-containing IC deposit in the renal mesangium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1440-1797.7.s3.3.x
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  • 4
    Electronic Resource
    Electronic Resource
    Heterogeneity of carbohydrate moieties of IgA1 molecules from IgA nephropathy patients and normal individuals (1997)
    Oxford, UK : Blackwell Publishing Ltd
    Nephrology 3 (1997), S. 0 
    Details
    ISSN: 1440-1797
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Summary: IgA nephropathy (IgAN) is characterized by the deposition of IgA1 in kidney mesangia and the presence of IgA1-containing immune complexes in the circulation. Structural studies of IgA1 isolated from sera of IgAN patients indicated a statistically significant decrease in the content of galactose (Gal). Using a combination of lectins specific for glycans in O- or N-linked glycan side chains, this Gal deficiency was restricted to O-linked glycans present in the hinge region of IgA1 molecules. Gal-deficient IgA1 displayed a significantly higher binding to mesangial cells through a putative non-internalizing receptor specific for N-acetyl galactosamine (GalNAc) in O-linked glycans. These data suggest that Gal deficiency results in diversion of IgA1 molecules from the usual degradative pathway and deposition of altered IgA1 in the mesangium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1440-1797.1997.tb00195.x
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  • 5
    Electronic Resource
    Electronic Resource
    IgA nephropathy, the most common cause of glomerulonephritis, is linked to 6q22–23 (2000)
    [s.l.] : Nature America Inc.
    Nature genetics 26 (2000), S. 354-357 
    Details
    ISSN: 1546-1718
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Medicine
    Notes: [Auszug] End-stage renal disease (ESRD) is a major public health problem, affecting 1 in 1,000 individuals and with an annual death rate of 20% despite dialysis treatment. IgA nephropathy (IgAN) is the most common form of glomerulonephritis, a principal cause of ESRD worldwide; it affects up to 1.3% ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/81677
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  • 6
    Electronic Resource
    Electronic Resource
    Expression of stem cell factor by osteoblasts in normal and hyperparathyroid bone: relation to ectopic mast cell differentiation (1999)
    Springer
    Virchows Archiv 435 (1999), S. 50-57 
    Details
    ISSN: 1432-2307
    Keywords: Key words Kit ligand ; c-Kit ; Steel factor ; Interleukin-3 ; Bone turnover ; Mastocytosis ; Parathyroid hormone
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract  Mast cells accumulate in hyperparathyroid bone, but the reason is not clear. We compared the distribution of mast cells and related growth factors in normal and hyperparathyroid bone. Mast cell formation was strongly affected by proximity to bone-forming surfaces of hyperparathyroid bone. Hyperparathyroidism greatly increased the production by active, bone-synthesizing osteoblasts of stem cell factor (SCF) but not of IL-3. Osteoblast SCF was distributed to the basolateral cell membranes, and its cDNA sequence (GenBank AF119835) is homologous to the murine membrane-bound SCF. Quiescent osteoblasts did not produce detectable SCF. Synthetic osteoblasts in normal bone were SCF positive, but comprised a much smaller population of cells, in keeping with the slow turnover of normal bone. Major SCF isoforms on immunoblot analysis of osteoblast-fraction proteins from high-turnover bone had Mrs of about 48 and 40 kDa. Similar SCF isoforms were produced by MG63 osteoblast-derived cells and were identified by several anti-SCF antibodies. SCF is expressed in several mesenchymal cell types in a complementary fashion with cells bearing its receptor. SCF potently facilitates differentiation of mast cells, so the increase in paratrabecular mast cells in hyperparathyroid bone is probably driven by osteoblastic SCF. However, since mast cells are not normal components of bone, osteoblastic SCF probably regulates other cells, with mast cell differentiation occurring as a side effect greatly increased osteoblastic activity.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004280050394
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  • 7
    Electronic Resource
    Electronic Resource
    IgA-associated renal diseases: Antibodies to environmental antigens in sera and deposition of immunoglobulins and antigens in glomeruli (1986)
    Springer
    Journal of clinical immunology 6 (1986), S. 74-86 
    Details
    ISSN: 1573-2592
    Keywords: IgA nephropathy ; IgA subclasses, food antigens ; immunofluorescence
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Levels of IgA1, IgA2, IgM, and IgG antibodies specific for 10 ubiquitous food and bacterial antigens were examined by radioimmunoassay in the sera of 29 patients with IgA-associated renal diseases and 22 normal individuals. No significant differences were observed between patient and normal groups in the levels of IgA1 antibodies, and IgA2 antibodies were detected in only a few individuals in either group. Minor differences in IgM or IgG antibodies were seen against some antigens. Significant positive correlations between IgA1 and IgG and between IgA1 and IgM antibodies to casein were found in the patient group. Analysis of the molecular form of serum IgA1 antibodies revealed that although the pattern of polymeric and monomeric forms varied between individuals and between antibody specificities, there was no preponderance of one form in either patient or normal groups. Examination of kidney biopsies from 50 patients with IgA-associated renal diseases revealed that IgA1 represented the predominant subclass deposited in the glomerular mesangium; glomeruli from three patients contained both IgA1 and IgA2. Seventy-eight percent of the patients also had deposits of IgM, although IgA and IgM deposits did not always coincide. When IgG was present in glomeruli (45% of patients), the IgG1 subclass predominated. J chain was detectable in glomeruli of only four patients. C3 was detected in glomeruli of 95% of the patients, although the distribution of C3 did not always coincide with that of IgA. Indirect immunofluorescence staining with rabbit antisera to various environmental antigens showed that milk protein antigens could be deposited in association with IgA in the glomerular mesangium.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00915367
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  • 8
    Electronic Resource
    Electronic Resource
    Partial H (β1H) deficiency and glomerulonephritis in two families (1982)
    Springer
    Journal of clinical immunology 2 (1982), S. 110-117 
    Details
    ISSN: 1573-2592
    Keywords: Complement ; H ; C3 ; IgA nephropathy
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract H (β1H) controls the C3b amplification loop by its ability to displace Bb from the alternative pathway convertase, C3b,Bb, and acts as a cofactor with I (C3b inactivator) to produce inactive C3b. Serum C3 levels are dependent to a large extent on the levels of H and I. Partial H deficiency was found in two families. The index case in Family 1 had vasculitis, thrombocytopenia, proteinuria, and depressed serum H and C3 levels. The index case in Family 2 had depressed serum H and B (Factor B) levels and IgA nephropathy which progressed to renal failure. His sister also had IgA nephropathy and depressed serum H and C3 levels. The depressed serum C3 level, B level, and H level could be responsible for the development of the immune diseases found in some members of these families.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00916894
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