Abstract
An immunoglobulin E (IgE)-dependent histamine-releasing factor (HRF) produced by lymphocytes of atopic children and present in biological fluids of allergic patients has been identified and purified. Amino-terminal sequencing revealed extensive homology to a mouse protein, p21, and its human homolog, p23. Both recombinant proteins caused histamine release from the human basophils of a subpopulation of donors, and this release was dependent on IgE. Polyclonal antibodies recognized and removed the biological activity of recombinant and native HRF. HRF identifies a heterogeneity of IgE and is believed to play a prominent role in chronic allergic disease processes.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Antibodies / immunology
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Base Sequence
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Basophils / immunology
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Biomarkers, Tumor*
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Cell Line
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Cloning, Molecular
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Histamine Release*
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Humans
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Immunoglobulin E / immunology*
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Kinetics
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Lymphokines / chemistry*
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Lymphokines / immunology
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Lymphokines / isolation & purification
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Lymphokines / pharmacology
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Macrophages / metabolism
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Mice
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Molecular Sequence Data
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Recombinant Fusion Proteins / pharmacology
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Sequence Homology, Amino Acid
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Tumor Protein, Translationally-Controlled 1
Substances
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Antibodies
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Biomarkers, Tumor
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Lymphokines
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Recombinant Fusion Proteins
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Tumor Protein, Translationally-Controlled 1
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Immunoglobulin E