High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies

Riske, Frank; Hakimi, J; Mallamaci, Michael A.; Griffin, Margaret M.; Pilson, B; Tobkes, N; Lin, Psang Dain; Danho, Waleed; Kochan, Jarema; Chizzonite, R

doi:10.1016/s0021-9258(18)99155-6

Cited by 182 publications

(11 citation statements)

References 38 publications

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“…Fc6RI is a tetrameric structure composed of one 50-55-kD ol chain (FceKIot), one 33-kD fl chain (FceRIfl), and two disulphide-linked identical 7-9-kD 3' chains (FceRI'y) (16). Recently, a series of anti-FceKIoe mAbs were raised from mice immunized with a purified chimeric FceRIol expressed in Chinese hamster ovarian cells (10). Using two of these reagents, the anti-FceRIot antibodies 6F7 and 29C6, we investigated the expression of Fc.eRIo~ on cryosections from normal human skin by immunohistochemistry.…”

Section: Resultsmentioning

confidence: 99%

“…Unlabeled mAb IOT6 (IgG1; Immunotech, MarseiUe, France), and PE-labeled T6/RD1 (IgG1, Coulter Corp., Krefeld, Germany) react with CDla which is, in the skin, exclusively expressed on LC (9). Murine mAb 29C6 and 6F7 (both IgG1) were raised from mice immunized with a purified chimeric c~ subunit ofFceRI (FceRIo 0 expressed in Chinese hamster ovarian cells (10). FITC-labeled goat anti-mouse was obtained from Jackson Im-munoResearch Labs, Inc. (West Grove, PA) and unlabeled IgG1 and PE-labeled IgG1 from Becton Dickinson & Co. (Mountain View, CA).…”

Section: Methodsmentioning

confidence: 99%

See 1 more Smart Citation

Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

Bieber

Wollenberg

Hakimi

et al. 1992

The Journal of Experimental Medicine

462

205

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SummaryIt has been suggested that epidermal Langerhans cells (LC) bearing immunoglobulin E (IgE) may be involved in the genesis of atopic disease. The identity of the IgE receptor(s) on LC remained unclear, although it represents a crucial point in understanding cellular events linked to the binding of allergens to LC via IgE. In this report, we demonstrate that epidermal LC express the high affinity receptor for the Fc fragment of IgE (FceRI) which has, so far, only been described on mast cells and basophils. Epidermal LC react with antibodies specific for the u subunit of the tetrameric (oL,~,23') FceRI. Specific transcripts for Fc~RIo~ and FceRI3~ were detected in LC and correspond to those of human basophils and of the human basophil cell line KU812. Furthermore, human basophils, KU812 cells, and LC express the putative B subunit. Thus human LC express the complete structure of FceRI. This finding opens new perspectives in the putative functional role of this structure on antigen-presenting cells.T he demonstration of IgE molecules on epidermal Langerhans cells (LC) 1 in patients with atopic dermatitis has implied that these cells should perform a major function in the pathophysiology of atopic disease (1, 2). Although initially, only receptors for the Fc fragment of IgG were identified on epidermal LC (3, 4), the low affinity receptor for IgE FceRII/CD23 (5) and the human IgE binding protein (eBP) (6) have now also been found on these cells in lesional, as well as in normal skin. However, attempts to completely block IgE binding on LC by a variety of anti-FceRII/CD23, antieBP, and/or anti-Fc3,R reagents remained unsuccessful, suggesting the presence of a third IgE-binding structure actually responsible for a part of the IgE-binding capacity of LC. We report here, that normal human LC also express the high a~nity receptor for IgE, Fcelkl, demonstrating that the presence of this structure is not restricted to mast cells and basophils. Our results also document the presence of the putative/~ chain on both human basophils and LC.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

Bieber

Wollenberg

Hakimi

et al. 1992

The Journal of Experimental Medicine

462

205

View full text Add to dashboard Cite

show abstract

“…Reagents The monoclonal antibody (MoAb) 22E7 (a kind gift from Dr J.P. Kochan and Dr R. Chizzonite, Roche Inc., Nutley, NJ) recognizes the FceRI a-subunit (Riske et al, 1991). MoAb speci®c for FceRII/CD23 were clones MHM6 (DAKO, Glostrup, Denmark) and 9P.25 (Jackson, West Grove, PA).…”

Section: Methodsmentioning

confidence: 99%

Dichotomic Nature of Atopic Dermatitis Reflected by Combined Analysis of Monocyte Immunophenotyping and Single Nucleotide Polymorphisms of the Interleukin-4/Interleukin-13 Receptor Gene: The Dichotomy of Extrinsic and Intrinsic Atopic Dermatitis

Novak

Kruse

Kraft

et al. 2002

Journal of Investigative Dermatology

117

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Patients with atopic dermatitis display substantial immunologic abnormalities, among which elevated total IgE is considered as a hallmark; however, a subgroup of atopic dermatitis patients exhibits normal IgE levels, but mechanisms contributing to the so-called "intrinsic" or "nonallergic" form of atopic dermatitis are obscure. In order to unravel similarities and differences of both atopic dermatitis subtypes, the phenotype of monocytes, total serum IgE levels, and serum levels of cytokines regulating the IgE production from nonatopic individuals and patients with allergic rhinitis, and extrinsic and intrinsic atopic dermatitis were measured. Concomitantly, genomic DNA probes of all subjects were analyzed for single nucleotide polymorphisms of candidate genes of structures involved in the regulation of the IgE synthesis, such as interleukin-4 and the interleukin-4R/interleukin-13R. Our data show that the surface expression of the high- and low-affinity receptor for IgE (FcepsilonRI and FcepsilonRII/CD23) and the interleukin-4Ralpha chain were significantly elevated in monocytes from patients with extrinsic atopic dermatitis. Furthermore, serum levels of interleukin-13 were significantly increased in patients with intrinsic atopic dermatitis. In addition, the frequency of the interleukin-4Ralpha polymorphism C3223T and the interleukin-4 polymorphism C590T tended to be higher in extrinsic atopic dermatitis than in intrinsic atopic dermatitis. Altogether our findings indicate that intrinsic atopic dermatitis patients exhibit phenotypic and immunologic features, which differ from those of patients with extrinsic atopic dermatitis or other atopic disorders.

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“…The antibody against mast cell tryptase (AA1) (Walls et al, 1990) was kindly provided by A. Walls, Southampton, U.K., a competitively binding antibody against the a-chain of the FceRI (29C6) (Riske et al, 1991) by J. Hakimi, Nutley, U.S.A., a partially competitively binding antibody against c-Kit (YB5.B8) (Lerner et al, 1991;Ashman et al, 1994) by L. Ashman, Adelaide, Australia, and an HLA-DR antibody (Tu È36) by A. Ziegler, Berlin Germany (Ziegler et al, 1986). Antibodies against CD1, CD3, CD11b, CD14, CD26, CD33, CD34, CD64, and CD68 as well as isotype matched control antibodies against desmin and laminin were all purchased from Dianova (Hamburg, Germany).…”

Section: Monoclonal Antibodiesmentioning

confidence: 99%

Mast Cell and Myeloid Marker Expression During Early In Vitro Mast Cell Differentiation from Human Peripheral Blood Mononuclear Cells

Welker

Grabbe

Zuberbier

et al. 2000

Journal of Investigative Dermatology

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High affinity human IgE receptor (Fc epsilon RI). Analysis of functional domains of the alpha-subunit with monoclonal antibodies

Cited by 182 publications

References 38 publications

Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

Human epidermal Langerhans cells express the high affinity receptor for immunoglobulin E (Fc epsilon RI).

Dichotomic Nature of Atopic Dermatitis Reflected by Combined Analysis of Monocyte Immunophenotyping and Single Nucleotide Polymorphisms of the Interleukin-4/Interleukin-13 Receptor Gene: The Dichotomy of Extrinsic and Intrinsic Atopic Dermatitis

Mast Cell and Myeloid Marker Expression During Early In Vitro Mast Cell Differentiation from Human Peripheral Blood Mononuclear Cells

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