Molecular structure of human lymphocyte receptor for immunoglobulin E

Kikutani, Hitoshi; Inui, Shigeru; Satō, Ryōichi; Barsumian, E L; Owaki, Hajime; Yamasaki, Kouji; Kaisho, Tsuneyasu; Uchibayashi, Naoto; Hardy, Richard R.; Hirano, Toshio; Tsunasawa, Susumu; Sakiyama, Fumio; Suemura, Masaki; Kishimoto, Tadamitsu

doi:10.1016/0092-8674(86)90508-8

Cited by 367 publications

(168 citation statements)

References 38 publications

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“…In the former case it seems reasonable that a significant divergence in structure is required for two related proteins to recognize two diverging members of the immunoglobulin family. In fact, the degree of sequence homology between the specified areas of eBP and Fc'yR is consistent with that between the constant regions of IgE and IgG (34 (31,35) and rat IgE-binding factor (36).…”

Section: Discussionmentioning

confidence: 50%

“…The abundance of proline residues and the repeated sequences in this domain suggest multiple turns and a possible recurrent folding structure for EBP. These features might also account for the discrepancy between the predicted molecular weight (27,573) and the apparent molecular weight of the purified protein as estimated from NaDodSO4/PAGE (31,000). …”

Section: Discussionmentioning

confidence: 99%

“…Metzger and coworkers (8) have proposed a tetrameric model for this receptor that includes a single highly glycosylated a subunit (Mr, 55,000), a single (3 subunit (Mr, 33,000), and two identical y subunits (Mr, 9000). Kulczycki and coworkers (9)(10)(11) have identified a protein of M, 31,000, in addition to the protein equivalent to the a subunit, in a two-cycle affinity purification of rat basophilic leukemia (RBL) cell lysates with IgE immunoadsorbents. A protein of similar properties was also found in rat mast cells (11,12).…”

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confidence: 99%

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An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor.

Albrandt¹,

Orida²,

Liu³

1987

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

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Proteins that bind IgE play important roles in both the synthesis and function of IgE and are therefore intimately involved in IgE-mediated human allergic disorders. This report describes the structure of an IgE-binding protein, as predicted from sequencing a cDNA cloned from rat basophilic leukemia cells. This protein contains two domains: the amino-terminal domain (140 amino acids) consists of a highly conserved repetitive amino acid sequence, Tyr-Pro-GlyPro/Gln-Ala/Thr-Pro/Ala-Pro-Gly-Ala, whereas the carbox- The IgE receptor on mast cells and basophils has been most extensively studied. Metzger and coworkers (8) have proposed a tetrameric model for this receptor that includes a single highly glycosylated a subunit (Mr, 55,000), a single (3 subunit (Mr, 33,000), and two identical y subunits (Mr, 9000). Kulczycki and coworkers (9-11) have identified a protein of M, 31,000, in addition to the protein equivalent to the a subunit, in a two-cycle affinity purification of rat basophilic leukemia (RBL) cell lysates with IgE immunoadsorbents. A protein of similar properties was also found in rat mast cells (11, 12). Other investigators, using different procedures, have discovered Mr 30,000-33,000 IgE-binding proteins from RBL cells (13). Recently, we have identified a Mr 31,000 protein with affinity for IgE in oocytes injected with mRNA isolated from RBL cells (14) and in the in vitro translation products of RBL mRNA (15). It was shown that this protein exhibits an intrinsic and specific IgE-binding activity and is reactive with a specific rabbit antiserum prepared against highly purified RBL cell proteins isolated by affinity chromatography using IgE immunoadsorbent (9). It was also demonstrated that this IgE-binding protein is expressed specifically in certain cell types known to possess IgE-specific receptors. The cDNA coding for this protein was cloned and the partial amino acid sequence of this protein was determined through DNA sequencing of a partial cDNA (15).We report here the cloning and nucleotide sequence of a full-length cDNA revealing an IgE-binding protein (EBP) containing two distinct structural domains. One of the domains contains a highly conserved repetitive amino acid sequence and the other shares significant sequence homology with the receptor for the Fc portion of IgG (FcyR).t MATERIALS AND METHODSCell Lines and Reagents. The RBL cell line (16) was provided by H. Metzger of the National Institutes of Health. Mouse monoclonal IgE (H1-DNP-e-26.82) and IgG1 (Hi-DNP-y1-109.3) specific for 2,4-dinitrophenyl (DNP) have been described previously (17). Immunoadsorbents were prepared by conjugating 10 mg of protein to 1 g (dry weight) of CNBr-activated Sepharose 4B (Pharmacia).Preparation of RNA. Total cellular RNA was extracted from RBL cells by the guanidinium thiocyanate procedure (18). Isolation of poly(A)+ RNA by oligo(dT)-cellulose affinity chromatography and sucrose density gradient fractionation of the poly(A)+ RNA was performed as described (14).cDNA Cloning, Screening, and Sequencing. ...

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Section: Discussionmentioning

confidence: 50%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor.

Albrandt¹,

Orida²,

Liu³

1987

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

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“…CD23, a 45-kDa type II integral membrane protein, is unique among Ig receptors in belonging to the animal C-type lectin rather than the Ig superfamily (10,11). The extracellular sequence comprises the lectin "head," N-terminal "stalk," and C-terminal "tail."…”

mentioning

confidence: 99%

Soluble CD23 Monomers Inhibit and Oligomers Stimulate IGE Synthesis in Human B Cells

McCloskey

Hunt

Beavil

et al. 2007

Journal of Biological Chemistry

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The low affinity IgE receptor, CD23, is implicated in IgE regulation and the pathogenesis of allergic disease. CD23 is a type II integral membrane protein, comprising a lectin "head," N-terminal "stalk," and C-terminal "tail" in the extracellular sequence. Endogenous proteases cleave CD23 in the stalk and the tail to release soluble fragments that either stimulate or inhibit IgE synthesis in human B cells. The molecular basis of these paradoxical activities is not understood. We have characterized three fragments of CD23, monomeric derCD23, monomeric exCD23, and oligomeric lzCD23. We show that the monomers inhibit and the oligomer stimulates IgE synthesis in human B cells after heavy chain switching to IgE. CD23 fragments could be targets for therapeutic intervention in allergic disease.

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“…In this context, it is interesting to note that CD23 is a member of a Ca2*-dependent lectin family (26)(27)(28). We demonstrate here that the interaction of CD23 with its ligand is Ca 2 + dependent.…”

Section: Discussionmentioning

confidence: 85%

Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes.

Pochon¹,

Graber²,

Yeager³

et al. 1992

The Journal of Experimental Medicine

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SummaryRecombinant full-length human CD23 has been incorporated into fluorescent liposomes to demonstrate the existence of a ligand for CD23 that is different from the previously known ligand, immunoglobnlin E (IgE). The novel ligand for CD23 is expressed on subsets of normal T cells and B ceUs as well as on some myeloma ceU lines. The interaction of full-length CD23 with its ligand is specifically inhibited by anti-CD23 monodonal antibodies and by IgE, and it is Ca z+ dependent. Moreover, tunicamycin treatment of a CD23-binding cell line, RPMI 8226, significantly reduced the binding of CD23 incorporated into fluorescent liposomes, and a sugar, fucose-l-phosphate, was found to inhibit CD23-liposome binding to RPMI 8226 cells, suggesting the contribution of sugar structures on the CD23 ligand. In addition, CD23-transfected COS cells were shown to form specific conjugates with the cell line RPMI 8226. These data demonstrate that CD23 interacts with a ligand, which is different from IgE, and that CD23 can be considered as a new surface adhesion mohcule involved in cell-cell interactions.

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Molecular structure of human lymphocyte receptor for immunoglobulin E

Cited by 367 publications

References 38 publications

An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor.

An IgE-binding protein with a distinctive repetitive sequence and homology with an IgG receptor.

Soluble CD23 Monomers Inhibit and Oligomers Stimulate IGE Synthesis in Human B Cells

Demonstration of a second ligand for the low affinity receptor for immunoglobulin E (CD23) using recombinant CD23 reconstituted into fluorescent liposomes.

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