Development of a functional <i>in vitro</i> assay as a novel tool for the standardization of allergen extracts in the human system

Vogel, Lothar; Lüttkopf, D.; Hatahet, Lina; Haustein, Dieter; Vieths, Stefan

doi:10.1111/j.1398-9995.2005.00803.x

Cited by 131 publications

(136 citation statements)

References 34 publications

(32 reference statements)

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“…Next, we wished to assess whether the observed activation is mediated by antibodies bound to high-affinity Fc receptors. Therefore, we eluted Igs by means of acid glycine buffer (9) and analyzed whether activation of basophils by citrullinated fibrinogen was inhibited. Flow cytometric analysis of eluted samples showed a complete loss of IgE expression on basophils after elution.…”

Section: Resultsmentioning

confidence: 99%

Evidence for a functional role of IgE anticitrullinated protein antibodies in rheumatoid arthritis

Schuerwegh¹,

Ioan‐Facsinay²,

Dorjée³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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Rheumatoid arthritis (RA) is a systemic autoimmune disease involving inflammation of the joints. Among the autoantibodies described in RA, anticitrullinated protein antibodies (ACPAs) are highly specific and predictive for RA. In addition, ACPAs have been implicated in the pathogenesis of RA. However, a direct functional response of immune cells from ACPA + RA patients toward citrullinated proteins has not been demonstrated. In this study, we show that exposure to citrullinated antigens leads to activation of basophils from ACPA + RA patients within 20 minutes. This was not observed after exposure of basophils to noncitrullinated control antigens or after stimulation of basophils from ACPA − RA patients and healthy controls. Basophil activation was correlated with the binding of citrullinated proteins to basophils. Furthermore, serum from ACPA + RA patients in contrast to that from ACPA − RA patients could specifically sensitize human FcεRI expressing rat basophil cells (RBL), enabling activation by citrullinated proteins. Mast cell degranulation products such as histamine levels were enhanced in synovial fluid of ACPA + RA patients as compared with ACPA − RA and osteoarthritis patients. In addition, histamine levels in synovial fluid from ACPA + RA patients correlated with IgE levels, suggesting degranulation of mast cells by cross-linking IgE. Immunohistochemistry on synovial biopsies demonstrated an increased number of degranulated CD117 + mast cells in ACPA + RA patients; IgE and FcεRI expression in synovial mast cells from ACPA + RA patients was increased. In conclusion, our results show an immunological response of immune cells from ACPA + RA patients in a citrulline-specific manner. Moreover, these data indicate a role for IgE-ACPAs and FcεRI-positive cells in the pathogenesis of RA.

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Section: Resultsmentioning

confidence: 99%

Evidence for a functional role of IgE anticitrullinated protein antibodies in rheumatoid arthritis

Schuerwegh¹,

Ioan‐Facsinay²,

Dorjée³

et al. 2010

Proc. Natl. Acad. Sci. U.S.A.

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“…Cells were grown under standard conditions (Vogel et al, 2005) and were passively sensitized with serum of a birch pollen symptomatic patient (skin prick test positive and RAST > 3). Dilutions of daily Chemvol samples were added to the cells and degranulation was quantitated as b-hexosaminidase release, determined as nitrophenol release from pNAG (p-nitrophenol-D-2-acetamido-2-deoxyglucopyranosid, SigmaeAldrich Corp, St. Louis, MO) in relation to total b-hexosaminidase activity after lysis of the cells with 1% Triton-X100 (Vogel et al, 2005). Only values within the linear doseeresponse range of the cells (5e45% degranulation) were reported.…”

Section: Degranulation Of Humanized Rblmentioning

confidence: 99%

Release of Bet v 1 from birch pollen from 5 European countries. Results from the HIALINE study

Buters

Thibaudon

Smith

et al. 2012

Atmospheric Environment

144

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“…To resolve this, RBL-2H3 cells were transfected with cDNA coding for human high-affinity IgE receptor (F ce RI) chains (Dibbern et al, 2003;Gilfillan et al, 1992;Kaul et al, 2007;Ladics et al, 2008;Takagi et al, 2003;Taudou et al, 1993;Vogel et al, 2005). The human F ce RI allowed these cells to bind IgE from sera of allergic subjects and subsequently be activated in allergen-specific manners.…”

Section: Rat Basophil Leukemia (Rbl) Cell Modelmentioning

confidence: 99%

“…Immunochemical methods depend on IgE that is present in allergen-specific polyclonal animal sera or human patient sera to bind to molecules bound to solid matrices like cellulose (enzyme allergosorbent test [EAST], Immuno-CAPs) or nitrocellulose (Western blotting). This binding to the matrix may change the structural integrity of the allergens and, thus, destroy the epitopes responsible for inducing allergy in vivo (Palmera et al, 2005;Vogel et al, 2005). Further, the results of immunochemical methods that are based on allergenspecific IgE are susceptible to a presence of IgG of the same specificity (Kadooka et al, 2000).…”

Section: Introductionmentioning

confidence: 99%

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

Sun

Zhou

Zhou³

et al. 2014

Journal of Immunotoxicology

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(2015) Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy, Journal of Immunotoxicology, 12:2, 199-205, DOI: 10.3109/1547691X.2014 AbstractFood allergy is an important public health problem that affects an estimated 8% of young children and 2% of adults. With an increasing interest in genetically-engineered foods, there is a growing need for development of sensitive and specific tests to evaluate potential allergenicity of foods and novel proteins as well as to determine allergic responses to ensure consumer safety. This review covers progress made in the field of development of cell models, specifically that involving a rat basophil leukemia (RBL) cell-based immunoassay, for use in allergen identification, diagnosis, and immunotherapy. The RBL assay has been extensively employed for determining biologically relevant cross-reactivities of food proteins, assessing the effect of processing on the allergenicity of food proteins, diagnosing allergic responses to whole-food products, and identifying anti-allergy food compounds. From the review of the literature, one might conclude the RBL cell-based assay is a better test system when compared to wild-type mast cell and basophil model systems for use in allergen identification, diagnosis, and analyses of potential immunotherapeutics. However, it is important to emphasize that this assay will only be able to identify those allergens to which the human has already been exposed, but will not identify a truly novel allergen, i.e. one that has never been encountered as in its preferred (humanized) configuration.

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Development of a functional in vitro assay as a novel tool for the standardization of allergen extracts in the human system

Cited by 131 publications

References 34 publications

Evidence for a functional role of IgE anticitrullinated protein antibodies in rheumatoid arthritis

Evidence for a functional role of IgE anticitrullinated protein antibodies in rheumatoid arthritis

Release of Bet v 1 from birch pollen from 5 European countries. Results from the HIALINE study

Use of a rat basophil leukemia (RBL) cell-based immunological assay for allergen identification, clinical diagnosis of allergy, and identification of anti-allergy agents for use in immunotherapy

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