IgE-Dependent Histamine-Releasing Factors

MacDonald, Susan; Langdon, Jacqueline M.; Greenlee, Brian M.; Kagey‐Sobotka, Anne; Lichtenstein, Lawrence M.

doi:10.1159/000235347

Cited by 12 publications

(10 citation statements)

References 46 publications

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“…Reasons for this are unclear, but the false-negative result might be because of the higher detection limit of the EXiLE system, as serum #94 contained no more than 2.99 U A /ml specific IgE. Another possibility is that other substances, like chemokines and cytokines, can induce histamine release from human basophils (29, 30). As RS-ATL8 cells only have human FcεRI, the cells would not be activated through IgE-independent mechanisms like these.…”

Section: Discussionmentioning

confidence: 99%

A convenient and sensitive allergy test: IgE crosslinking‐induced luciferase expression in cultured mast cells

Uchida

Higuchi

Nakamura

et al. 2010

Allergy

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BackgroundFor the detection of allergen-specific IgE in sera, solid-phase IgE-binding assays like the CAP test are commonly used. Although such immunochemical methods are very sensitive, they frequently produce false positives. Degranulation of the human IgE receptor (FcεRI)-transfected rat mast cell (RBL) lines seems to be a possible indicator for human IgE, but spontaneous mediator release from these cells in the presence of human sera is not negligible.MethodsThe nuclear factor of activated T-cells (NFAT)-responsive luciferase reporter gene was stably transfected into human FcεRI-expressing RBL-SX38 cells. One established clone (RS-ATL8) was sensitized with 1 : 100 dilution of sera from patients with egg white allergy and then stimulated with purified or a crude extract of egg white allergen.ResultsSensitization with 15 pg/ml IgE was sufficient to detect IgE crosslinking–induced luciferase expression (EXiLE) by anti-IgE stimulation. Allergen-specific EXiLE was elicited by as little as 1 fg/ml of egg white protein without cytotoxicity. There was a good correlation between results with EXiLE and oral food challenge tests on patients with egg allergy (P = 0.001687, Fisher's exact test). The measured values of EXiLE and the CAP test also correlated well (R = 0.9127, Spearman's test).ConclusionThe EXiLE test using RS-ATL8 cells is a promising in vitro IgE test to evaluate the biological activity of the binding between IgE and allergens.

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Section: Discussionmentioning

confidence: 99%

A convenient and sensitive allergy test: IgE crosslinking‐induced luciferase expression in cultured mast cells

Uchida

Higuchi

Nakamura

et al. 2010

Allergy

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“…Of the chemokines tested, monocyte chemotactic protein-1 (MCP-1) and MCP-3 are the most potent activators of basophils, inducing mediator release at nanomolar concentrations (14). The IgE-dependent HRFs, described as causing histamine release from cells expressing a particular type of IgE (designated as IgE+), had only been partially characterized (15). Recently, however, a cDNA clone that codes for a protein with a molecular weight of 23,000 daltons has been subcloned and expressed.…”

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confidence: 99%

An immunoglobulin E-dependent recombinant histamine-releasing factor induces interleukin-4 secretion from human basophils.

Schroeder¹,

Lichtenstein²,

MacDonald³

1996

The Journal of Experimental Medicine

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SummaryA novel recombinant histamine-releasing factor (rHFR), which stimulates secretion from a subpopulation of human basophils that express a particular type of immunoglobuhn E (IgE) or IgE +, was found to induce interleukin-4 (IL-4) production from cells isolated from these same donors. The secretion of IL-4 protein induced by rHRF significantly correlated with histamine release and the amount of protein generated, and the kinetics were identical to those caused by anti-IgE activation. Furthermore, the ability of rHRF to induce IL-4 protein production from cells not normally responsive to this protein was transferred by passive sensitization with plasma containing IgE + antibody. That this novel protein stimulates both mediator release and the secretion of IL-4 protein from human basophils suggests a prominent role for this molecule in allergic disease.

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“…These cells release a variety of soluble mediators upon cross-linking of their receptor-bound IgE by a cognate antigen. There is also evidence that IgE bound to the high affinity receptor on mast cells can be cross-linked by member(s) of a broad class of IgE-dependent histamine releasing factors (14). Studies involving histamine releasing factors have led to the suggestion of a functional heterogeneity of IgE.…”

Section: Discussionmentioning

confidence: 99%

“…Studies involving histamine releasing factors have led to the suggestion of a functional heterogeneity of IgE. The basis for this heterogeneity is not understood but has been speculated to be the result of differential glycosylation (14). IgE has also been suggested to participate in a variety of other immune processes such as antigen recognition, antibody-dependent cellular cytotoxicity, and B cell growth via binding to the high affinity IgE receptor (Fc⑀R I), the low affinity IgE receptor (Fc⑀R II), or galectin 3.…”

Section: Discussionmentioning

confidence: 99%

Expression of Novel Secreted Isoforms of Human Immunoglobulin E Proteins

Lyczak

Zhang

Saxon

et al. 1996

Journal of Biological Chemistry

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Four human IgE isoforms produced by alternative splicing of the epsilon primary transcript were expressed as chimeric mouse/human anti 5-dimethylamino-1-naphthalenesulfonyl antibodies in the murine myeloma cell line Sp2/0. The four isoforms include the classic secreted form and three novel isoforms with altered carboxyl termini. All of these isoforms lack the transmembrane region encoded by the M1/M1 exon and are therefore predicted to be secreted proteins. When expressed in Sp2/0 cells, three of the IgE isoforms are assembled into complete molecules of two Ig heavy chains and two Ig light chains, whereas the fourth isoform is predominately assembled into half-molecules of one Ig heavy chain and one Ig light chain. All four isoforms are secreted with similar kinetics. In contrast, when the isoform containing the C⑀4 domain joined directly to the M2 exon (IgE grandé ) is expressed in the J558L cell line, it is degraded intracellularly, suggesting a cell line-dependent regulation of secretion. These data show that these novel isoforms of human IgE, predicted to occur from in vivo and in vitro mRNA analysis, can be produced and secreted by mammalian cells. The different forms of IgE may have physiologically relevant but distinct roles in human IgE-mediated immune inflammation. The availability of purified recombinant human IgE isoforms makes it possible to analyze the functional differences among them.Alternative RNA splicing determines the production of secreted versus membrane-bound forms of immunoglobulins (1, 2). This is accomplished in mammals by the alternative usage of either a secreted terminus at the end of the last constant region domain or two downstream exons (M1 and M2) that encode the transmembrane and intracellular amino acids. Splicing to the M exons removes from the transcript the nucleotides that encode the hydrophilic COOH terminus and polyadenylation signal for the smaller, secreted form of the Ig.The one functional genomic locus encoding human epsilon heavy chain contains four Ig domain exons (C⑀1 to C⑀4) and the two membrane exons (M1 and M2). We (3-5) and others (6, 7) have previously shown that RNA prepared from the IgE-producing human cell line AF-10 and from fresh B lymphocytes stimulated to make IgE contain a variety of epsilon mRNAs produced by alternative splicing. In contrast to what is observed with other isotypes, the most common form of mRNA encoding membrane IgE is produced by splicing to a novel splice acceptor 156 base pairs upstream of the normal M1 acceptor site (4, 7). The M1Ј exon produced using this splice acceptor encodes 52 novel amino acids that are largely hydrophilic followed by the amino acids normally encoded by M1.Other alternatively spliced epsilon mRNAs are present that encode a series of potentially secreted proteins. The splicing events that generate these mRNAs utilize several novel exons including M2Ј, M2Љ, and C⑀5 in addition to the classic secreted form (see Fig. 1A). The M2Ј exon is created by splicing directly from C⑀4 to the normal M2 splice acceptor. The ...

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IgE-Dependent Histamine-Releasing Factors

Cited by 12 publications

References 46 publications

A convenient and sensitive allergy test: IgE crosslinking‐induced luciferase expression in cultured mast cells

A convenient and sensitive allergy test: IgE crosslinking‐induced luciferase expression in cultured mast cells

An immunoglobulin E-dependent recombinant histamine-releasing factor induces interleukin-4 secretion from human basophils.

Expression of Novel Secreted Isoforms of Human Immunoglobulin E Proteins

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