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- Dahlbom, I, et al.
(författare)
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Immunoglobulin g (IgG) anti-tissue transglutaminase antibodies used as markers for IgA-deficient celiac disease patients
- 2005
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Ingår i: Clinical and Diagnostic Laboratory Immunology. - 1071-412X. ; 12:2, s. 254-258
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Tidskriftsartikel (refereegranskat)abstract
- The role of immunoglobulin A (IgA) anti-tissue transglutaminase antibodies (IgA-tTG) as predictors of untreated celiac disease (CoD) is well documented, and the presence and levels of these antibodies are most accurately monitored with native or recombinant human antigens. However, IgA-deficient CoD patients are not identified by IgA serology, and conflicting results concerning the diagnostic validity of IgG antibodies against gliadin (IgG-AGA), endomysium (IgG-EmA), and tTG (IgG-tTG) have been reported. The aim of the present study was to evaluate the utility of IgG-tTG for the detection of CoD in IgA-deficient patients. Samples from 115 IgA-deficient and 200 IgA-sufficient subjects were collected and tested for the presence of IgA and IgG antibodies against tTG, EmA, and AGA. Antibodies against tTG were measured by an enzyme-linked immunosorbent assay based on recombinant human tTG, and antibodies against EmA were determined by immunofluorescence. The values for IgG-tTG showed a higher correlation (correlation coefficient [r] = 0.91) with those for IgG-EmA for the IgA-deficient subjects than for the IgA-sufficient subjects (r = 0.88). The overall concordance of the positive and negative results between IgG-tTG and IgG-EmA was 97%, and the IgG-tTG assay discriminated between IgG-EmA-positive and -negative subjects with IgA deficiency at a rate of 100%. Elevated levels of IgG-tTG and IgG-EmA were measured in 70% of the IgA-sufficient subjects. IgG-tTG detection with recombinant human tTG is a good alternative to IgG-EmA detection, and the addition of IgG-tTG assessment to present screening methods may improve the ability to identify IgA-deficient subjects with CoD.
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- Kaca, W, et al.
(författare)
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Complement activation by Proteus mirabilis negatively charged lipopolysaccharides
- 2000
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Ingår i: Journal of endotoxin research. - : SAGE Publications. - 0968-0519. ; 6:3, s. 223-234
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Tidskriftsartikel (refereegranskat)abstract
- Proteus mirabilis strains are human pathogens responsible for urinary tract infections and bacteremias and may be involved in rheumatoid arthritis. Lipopolysaccharide (LPS, bacterial endotoxin), the major component of the cell wall, is one of the virulence factors of Proteus. In the presented studies, we have investigated complement activation by LPSs isolated from P. mirabilis O10, O23, O30, and O43 strains, which differ in the number of negative COO— groups on their polysaccharide components. Four P. mirabilis strains studied were sensitive to complement-mediated killing, despite complement binding by their LPSs. The optimal complement binding by LPSs was detected in serum with functional assays for both the classical and alternative pathways. Complement activation in 80% serum by the smooth, uronic acid, and hexosamine containing P. mirabilis LPSs was not critically determined by the structure of their O-chain polysaccharides. One of four LPSs used as a model, P. mirabilis O10 LPS, fragmented C3 in an LPS dose- and time-dependent manner. It was detected by crossed-immunoelectrophoresis and capture ELISA with anti-C3c antibodies. The lower complement activation by O23 LPS correlates with its reduced C3 fragmentation, compared with three other Proteus LPSs studied. Rabbit anti-O antibodies enhanced the complement binding and factor C3 fragmentation by O10, O23, O30, and O43 P. mirabilis LPSs.
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- Vaziri-Sani, Fariba, et al.
(författare)
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Phenotypic expression of factor H mutations in patients with atypical hemolytic uremic syndrome
- 2006
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Ingår i: Kidney International. - : Nature Publishing Group. - 0085-2538 .- 1523-1755. ; 69:6, s. 981-988
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Tidskriftsartikel (refereegranskat)abstract
- We investigated the phenotypic expression of factor H mutations in two patients with atypical hemolytic uremic syndrome (HUS). Factor H in serum was assayed by rocket immunoelectrophoresis, immunoblotting, and double immunodiffusion and in tissue by immunohistochemistry. Functional activity was analyzed by hemolysis of sheep erythrocytes and binding to endothelial cells. A homozygous mutation in complement control protein (CCP) domain 10 of factor H was identified in an adult man who first developed membranoproliferative glomerulonephritis and later HUS. C3 levels were very low. The patient had undetectable factor H levels in serum and a weak factor H 150 kDa band. Double immunodiffusion showed partial antigenic identity with factor H in normal serum owing to the presence of factor H-like protein 1. Strong specific labeling for factor H was detected in glomerular endothelium, mesangium and in glomerular and tubular epithelium as well as in bone marrow cells. A heterozygous mutation in CCP 20 of factor H was found in a girl with HUS. C3 levels were moderately decreased at onset. Factor H levels were normal and a normal 150 kDa band was present. Double immunodiffusion showed antigenic identity with normal factor H. Factor H labeling was minimal in the renal cortex. Factor H dysfunction was demonstrated by increased sheep erythrocyte hemolysis and decreased binding to endothelial cells. In summary, two different factor H mutations associated with HUS were examined: in one, factor H accumulated in cells, and in the other, membrane binding was reduced.
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