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- Aniansson Zdolsek, Helena, 1961-, et al.
(författare)
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Expression of the T–cell markers CD3, CD4 and CD8 in healthy and atopic Children during the first 18 months of life
- 1999
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Ingår i: International Archives of Allergy and Immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 119:1, s. 6-12
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Tidskriftsartikel (refereegranskat)abstract
- Background: There is little information available about the development of T–cell immunity in healthy and atopic children. We have studied prospectively the mean fluorescence intensity of the T–cell receptor complex–associated CD3, CD4 and CD8 in relation to atopic family history (AFH) and the development of atopic disease.Methods: Children with a defined AFH (n = 172) were followed from birth to 18 months and the cumulative history of atopic disease was recorded. Blood samples were obtained at birth and at 18 months, and in a subgroup of 78 children also at 3, 6 and 12 months. Multicolour flow cytometry was used to analyse pan T–cells (CD3+CD45+CD14–), T–helper–(CD3+CD4+) and T–cytotoxic–(CD3+CD8+) cells.Results: At 18 months, 31 children were atopic and 118 non–atopic. Children who developed atopic disease had a higher CD4 expression (mean fluorescence intensity, MFI) on CD4+CD3+ lymphocytes at birth and at 3 months, particularly as compared with non–atopic children without AFH. Furthermore, the CD3 expression on CD3+CD45+CD14– lymphocytes increased more slowly with age in children with double atopic heredity, as compared with children with no or only one atopic family member.Conclusions: The higher expression of the CD4 receptor in early infancy in children who developed atopic disease compared with non–atopics suggests a delayed expression in T–helper cells. Children with a strong AFH had a slower increase in the expression of CD3, indicating a delayed T–cell maturation.
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| 4. |
- Cederbrant, Karin, et al.
(författare)
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In vitro Lymphocyte Proliferation as Compared to Patch Test Using Gold, Palladium and Nickel
- 1997
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Ingår i: International Archives of Allergy and Immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 112:3, s. 212-217
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Tidskriftsartikel (refereegranskat)abstract
- Background: A conventional lymphocyte transformation test (LTT) was compared to the commercially available MELISA® (memory lymphocyte immuno-stimulation assay), a lymphoproliferative assay that has been suggested to be a valuable instrument for the diagnosis of metal allergy. Sensitivity and specificity of the two assays were calculated using a patch test as a reference method.Methods: 34 patients were patch-tested for gold sodium thiosulfate, palladium chloride and nickel sulfate, and the lymphocyte proliferation to these metals was tested in vitro using mononuclear cells from peripheral blood.Results: No significant differences regarding sensitivity and specificity were found between MELISA and conventional LTT. The sensitivity varied between 55 and 95% and the specificity between 17 and 79%.Conclusions: The low specificity of the two in vitro assays suggests that they are not useful for diagnosis of contact allergy to the metals gold, palladium and nickel, since a large number of false-positive results will be obtained.
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| 6. |
- Egesten, Arne, et al.
(författare)
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Eosinophil granulocyte interaction with serum-opsonized particles: binding and degranulation are enhanced by tumor necrosis factor alpha
- 1998
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Ingår i: International Archives of Allergy and Immunology. - : S. Karger AG. - 1423-0097 .- 1018-2438. ; 115:2, s. 121-128
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Tidskriftsartikel (refereegranskat)abstract
- Eosinophils participate in the inflammatory response seen in allergy and helminthic infestation. Their release of granule-bound cationic proteins may play a role in these diseases. Therefore, we investigated mechanisms involved in the release of eosinophil cationic protein (ECP). Serum-opsonized zymosan was phagocytosed by eosinophils, and ECP was released into the phagosomes as judged by immunoelectron microscopy. Degranulation to the external milieu was induced by serum-opsonized, non-phagocytosable Sephadex beads (SOS), and ECP release was determined by use of an enzyme-linked immunosorbent assay. CD11b, CD18, and CD32 monoclonal antibodies inhibited degranulation, demonstrating dependence on complement receptor type 3 (CR3), and the low-affinity Fc receptor for IgG. Tumor necrosis factor-alpha (TNF-alpha) and interleukin (IL)-5 both rapidly enhanced the binding of eosinophils to serum-opsonized zymosan, and also the release of ECP upon interaction with SOS. The cytokine-induced increase in ECP release was inhibited by the phospholipase A2 (PLA2) inhibitor mepacrine, indicating an involvement of PLA2 in the enhanced response but not in baseline degranulation. Autocrine stimulation by the platelet-activating factor (PAF) is unlikely since the PAF receptor antagonist WEB 2086 did not inhibit the enhanced response. In conclusion, the main signals for eosinophil degranulation on serum-opsonized particles are mediated by CR3 and receptors for immunoglobulins. As for IL-5, TNF-alpha changes eosinophil phenotype from a resting to an activated state.
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| 7. |
- Elfman, LHM, et al.
(författare)
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IgE binding capacity of synthetic and recombinant peptides of the major storage mite (Lepidoglyphus destructor) allergen, Lep d 2
- 1998
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Ingår i: International archives of allergy and immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 117:3, s. 167-173
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Tidskriftsartikel (refereegranskat)abstract
- <b>Background:</b> Lepidoglyphus destructor is an important non–pyroglyphid mite species in Europe and a dominant allergen in farming environments. The major allergen of L. destructor, Lep d 2, is a protein of 13.2 kD that is recognised by about 90% of sera RAST positive to this mite species. <b>Methods:</b> The cDNA of two isoallergens of the Lep d 2 has previously been sequenced and the protein expressed in different protein expression systems. In order to map the B–cell epitopes, the full length protein and the truncated forms of the protein have been expressed in Escherichia coli as glutathione–S–transferase (GST) fusion proteins. Recombinant Lep d 2 fragments and synthetic overlapping 15 mer peptides spanning Lep d 2 were probed with sera from patients allergic to storage mite. <b>Results:</b> The full–length (125 amino acids) GST fusion protein reacted strongly with patient IgE in Western blots and dot blots. Synthetic peptides failed to react with IgE antibodies from mite–allergic patients and the truncated fusion proteins displayed weak IgE–binding capacity. <b>Conclusion:</b> We conclude that there are no dominant linear IgE–binding epitopes in Lep d 2. Recombinant or synthetic Lep d 2 fragments may, however, be further evaluated as hypoallergenic candidate molecules for specific immunotherapy.
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| 8. |
- Eriksson, TLJ, et al.
(författare)
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Identification and characterisation of two allergens from the dust mite Acarus siro, homologous with fatty acid-binding proteins
- 1999
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Ingår i: International archives of allergy and immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 119:4, s. 275-281
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Tidskriftsartikel (refereegranskat)abstract
- <b>Background:</b> Dust mites are a major cause of allergic disease worldwide. The dust mite <i>Acarus siro</i> is an inducer of occupational allergy among farmers, but sensitisation has also been found in non–farming populations. <b>Methods:</b> A degenerate primer was designed to the N–terminal amino acid sequence of a 15–kD IgE–binding protein in <i>A. siro</i> extract. The cDNA sequence was obtained by using reverse transcriptase polymerase chain reaction, standard cloning and sequencing techniques. The protein was expressed in <i>Escherichia coli</i> with a 6–histidine tag at its C–terminus. Immunoblotting of the recombinant protein and whole extract was performed using patient sera. <b>Results and conclusion:</b> 15 and 17–kD allergens were identified in a fraction of <i>A. siro</i> extract. The cDNA of the 15–kD allergen was isolated, cloned and sequenced and the allergen was expressed as a recombinant protein. The calculated molecular weight of the cDNA–encoded protein is 14.2 kD. The predicted amino acid sequence has one potential N–glycosylation site at position 4–6 and a cytosolic fatty acid–binding protein signature at position 5–22. The protein has 64% sequence identity with Blo t 13, an allergen from the dust mite <i>Blomia tropicalis</i>, as well as homology with several other fatty acid–binding proteins (FABPs) from different organisms. The allergen was named Aca s 13 and was recognised strongly by 3 of 13 (23%) of the subjects investigated. The amino acid sequence of the 17–kD protein was partly determined and it also showed high sequence homology with Blo t 13 and FABPs.
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| 9. |
- Fagerås Böttcher, Malin, 1969-, et al.
(författare)
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Cytokines in breast milk from allergic and nonallergic mothers
- 1999
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Ingår i: International Archives of Allergy and Immunology. - : S. Karger AG. - 1018-2438 .- 1423-0097. ; 118:2-4, s. 319-320
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Tidskriftsartikel (refereegranskat)abstract
- Sorry, there is no abstract. Read the first few lines of the text instead!The allergy–preventing effect of breast–feeding is controversial [1, 2]. This may be due to individual variations of the composition of human milk. Allergy is associated with a bias to production of cytokines involved in IgE synthesis, e.g. IL–4 and IL–13 [3] and the eosinophil chemotactic [4] and survival [5] factor IL–5. In contrast, IFN–=γ, which inhibits IgE synthesis [6], is downregulated [7]. Cytokines involved in IgA production, IL–6, IL–10 and TGF–β [8, 9] have also been proposed to be involved in IgE synthesis [10, 11, 12].
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