Relationship between Specific Circulating IgE, Basophil Cell-Bound IgE and Histamine Release Induced by Purified Allergens of &lt;i&gt;Dermatophagoides Farinae&lt;/i&gt;

Mao, J. Le; Weyer, A.; Dandeu, J P; Rabillon, J.; David, B.

doi:10.1159/000233709

Cited by 15 publications

(1 citation statement)

References 5 publications

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“…Basophils were more sensitive in their response to mite allergen than lym phocytes; 1,000 100.000 times lower doses of mite allergen could stimulate basophils to produce IL-4. This high sensi tivity must be caused by the high affinity of IgE to allergen, which is bound to the surface o f the basophils through Fee receptor 1 and correlates well with previous data for media tor release [24]. By contrast, much higher concentrations of allergens were required for the IL-4 production by lympho cytes, because cellular uptake of allergen was considered not to be mediated through its specific high affinity receptor in antigen-presenting cells.…”

Section: Il-4 Production From Basophilssupporting

confidence: 87%

Peripheral Blood T Lymphocytes and Basophils, Freshly Isolated from House-Dust-Mite-Sensitive Patients, Produce lnterleukin-4 in Response to Allergen-Specific Stimulation

Ochi

Tanaka

Katada

et al. 1996

Int Arch Allergy Immunol

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We examined the capacity of interleukin-4 (IL) production from lymphocytes and basophils, isolated from the peripheral blood of allergic patients sensitive to house dust mite, after stimulation with mite extract. IL-4 production was measured by a sensitive bioassay based on coculture with CT.h4S (a human IL-4-responsive cell line). Lymphocytes and basophils from patients with elevated serum IgE specific to mite allergen [radioallergosorbent test (RAST) score > 3] could produce detectable levels of IL-4 in response to mite extract, whereas those from patients with a RAST score of less than 2 or normal volunteers could not. The sensitivity of basophils to mite extract was high, so that a lower concentration of mite extract (1-10 ng/ml) could induce maximal IL-4 production. On the other hand, a higher concentration (10 μg/ml) was required for maximal IL-4 production from the lymphocytes. These findings demonstrate that allergen-specific IL-4-producing cells, lymphocytes and basophils, are generated in vivo in allergic patients and also that there exist characteristic differences between lymphocytes and basophils related to the in vivo source of IL-4.

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Section: Il-4 Production From Basophilssupporting

confidence: 87%

Peripheral Blood T Lymphocytes and Basophils, Freshly Isolated from House-Dust-Mite-Sensitive Patients, Produce lnterleukin-4 in Response to Allergen-Specific Stimulation

Ochi

Tanaka

Katada

et al. 1996

Int Arch Allergy Immunol

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Recombinant C5a enhances interleukin 1 and tumor necrosis factor release by lipopolysaccharide‐stimulated monocytes and macrophages

1990

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Lipopolysaccharide (LPS) is a potent inducer of interleukin 1 (IL 1) synthesis and release, and of tumor necrosis factor (TNF) secretion. Many signals can enhance the LPS-induced production of these cytokines. We have previously observed that addition of low amounts of normal human serum to the culture medium enhances IL 1 production. Among serum factors, anaphylatoxins C3a and C5a and/or their desArg derivatives have been shown to enhance LPS-induced IL 1 and TNF production. However, the capacity of natural anaphylatoxins to induce by themselves the production of cytokines remains a controversial issue. We have investigated the capacity of human recombinant C5a (hrC5a) to induce IL 1 and TNF production. Despite its lack of direct triggering, hrC5a was able to act synergistically with LPS, leading to higher IL 1 and TNF release by human monocytes and mouse peritoneal macrophages. As assessed by the comitogenic assay, hrC5a increased IL 1 release, whereas cell-associated IL 1 activity was not significantly modified. Measurement by enzyme-linked immunosorbent assay of human IL 1 beta led to similar conclusions, whereas measurement of IL 1 alpha by radioimmunoassay indicated, in addition, an increase in intracellular IL 1 alpha.

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Cyanogen bromide‐activated nitrocellulose membranes: A new tool for immunoprint techniques

et al. 1987

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C yanogen bromide-activated nitrocellulose membranes: A new tool for immunoprint techniquesNitrocellulose membranes were activated by cyanogen bromide in order to improve their binding capacities. Crude extracts of a grass pollen, Dactylis glomerata, and a mite, Dermatophagoides farinae, were separated by isoelectric focusing in agarose and blotted by capillary transfer onto nitrocellulose or activated nitrocellulose. The Dermatophagoides farinae components were visualized by Coomassie Brilliant Blue, Indiaink or Aurodye staining. The Dactylis glomerata and Dermatophagoides farinae allergens were revealed by radioimmunodetection using sera from allergic patients. A great increase of allergen binding was observed visually and by radioactive counting on activated nitrocellulose as compared with untreated nitrocellulose. New allergens which were not detectable on nitrocellulose appeared on activated nitrocellulose.Characterization of allergen molecules is of great interest in the standardization of allergens and elucidation of the mechanisms underlying the allergic manifestations [ 1-31. Immobilization by electrophoretic transfer [4] or capillary transfer 1. 51 onto membranes of nitrocellulose (NC) after electrophoretic separation of a complex crude extract is useful for characterization of antigens [6, 71. Cellulose acetate and cellulose membranes activated by cyanogen bromide (CNBr) had already been used for transfer [S, 91 but NC membranes were usually preferred owing to their facilitated handling and good binding capacity. In the present report, NC membranes were activated with CNBr to improve their binding capacity. Crude extracts of Dactylis glomerata (Dg) pollen and of Dermatophagoides farinae (Df) were separated by isoelectric focusing (IEF) followed by blotting of the separated constituents onto NC or CNBr-activated NC (a-NC) membranes and visualization by carbon or gold colloids. The aller-.gen binding was revealed by radioimmunodetection using sera from Dg or Df allergic patients.The Dg-soluble extract was obtained by stirring 60 mg Dg pollen from our own production, suspended in 500 pL distilled water for 1 h at room temperature. The Df-soluble extract was obtained from a whole mite culture as previously described {lo], lyophilized and dissolved in distilled water to a protein content of 50 mg/mL. The Dg and Df extracts were centrifugedfor 5 min at 9000 gjust beforeuse. Rabbit 1251-labelled antihuman IgE antibodies were obtained from Pharmacia (Uppsala, Sweden). Anti-Dg sera were obtained from Dg-pollensensitive patients whose radioallergo sorbent tests (RAST, Pharmacia) were of class IV, with total IgE levels less than 200 IU/mL. Anti-Df sera were obtained from Df-sensitive patients with different RAST class values (Fig. 3) and total IgE levels less than 400 IU/mL.A previously described technique [ 111 was modified to activate NC. Ten g CNBr (Merck, Darmstadt, FRG) were dis-~ ,.Abbreviations: a-NC, cyanogen bromide-activated nitrocellulose; CNBr, cyanogen bromide; Df, Dermatophagoides farinae; Dg, Dact...

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Relationship between Specific Circulating IgE, Basophil Cell-Bound IgE and Histamine Release Induced by Purified Allergens of <i>Dermatophagoides Farinae</i>

Cited by 15 publications

References 5 publications

Peripheral Blood T Lymphocytes and Basophils, Freshly Isolated from House-Dust-Mite-Sensitive Patients, Produce lnterleukin-4 in Response to Allergen-Specific Stimulation

Peripheral Blood T Lymphocytes and Basophils, Freshly Isolated from House-Dust-Mite-Sensitive Patients, Produce lnterleukin-4 in Response to Allergen-Specific Stimulation

Recombinant C5a enhances interleukin 1 and tumor necrosis factor release by lipopolysaccharide‐stimulated monocytes and macrophages

Cyanogen bromide‐activated nitrocellulose membranes: A new tool for immunoprint techniques

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