title: Recombinant human IL-1 alpha and -1 beta potentiate IgE-mediated histamine release from human basophils.
abstract: In this study, we have explored the relationship between interleukins and human basophil activation. Previous studies by ourselves and others have found that recombinant human (rh) IL-3 causes histamine release. The ability to release histamine has also been claimed for IL-1 but we cannot confirm this. In experiments with the basophils of 29 donors (excluding one D2O responder), histamine release with 100 ng/ml rhIL-1 alpha was 1.3 +/- 1% (SEM), whereas with rhIL-1 beta, it was 0.8 +/- 1%. Both IL-1 alpha and -1 beta were also used at concentrations of 0.01 to 1000 ng/ml without causing release. Neither increasing the Ca2+ concentration nor adding D2O or cytochalasin B caused IL-1 alpha and -1 beta to become secretagogues. rhIL-1, however, did augment IgE-dependent histamine release. The enhancement was similar with both rhIL-1 alpha and -1 beta, i.e. they were dose-dependent between 0.1 and 3 ng/ml and reached a plateau from 3 to 100 ng/ml. At submaximal histamine release (less than 10%), there was enhancement of three IgE-dependent secretagogues: 125% with goat anti-human IgE (n = 7), 215% with Ag E (n = 10), and 260% with a histamine releasing factor (n = 7). Non-IgE-dependent stimuli (formyl-methionine-leucine-phenylalanine and the ionophore A23187, n = 10) were enhanced less than 5%. rhIL-1-enhancement persisted after cell washing (n = 10). rhIL-1 was active in preparations of 50 to 75% pure basophils in which mononuclear cells were reduced by greater than 95% (n = 4), and mAbH34 to IL-1 beta blocked the enhancement caused by that molecule. We postulate that basophils have an IL-1 receptor which, when occupied, upregulates the response to IgE-related signals. Thus, this work characterizes a second interaction between interleukins and the cells central to the allergic response.
authors: Johns Hopkins University School of Medicine, Department of Medicine, Baltimore, MD 21239.
authors: W A
authors: WA
authors: Massey
authors: T C
authors: TC
authors: Randall
authors: A
authors: A
authors: Kagey-Sobotka
authors: J A
authors: JA
authors: Warner
authors: S M
authors: SM
authors: MacDonald
authors: S
authors: S
authors: Gillis
authors: A C
authors: AC
authors: Allison
authors: L M
authors: LM
authors: Lichtenstein
mesh_terms: D000276:Adjuvants, Immunologic / Q000494:pharmacology*; D000485:Allergens; D000888:Antibodies, Anti-Idiotypic / Q000502:physiology; D052179:Antigens, Plant; D001491:Basophils / Q000276:immunology*; D014408:Biomarkers, Tumor; D004306:Dose-Response Relationship, Immunologic; D004357:Drug Synergism; D006636:Histamine Release / Q000187:drug effects; D006801:Humans; D007073:Immunoglobulin E / Q000276:immunology / Q000502:physiology*; D007375:Interleukin-1 / Q000494:pharmacology*; D008222:Lymphokines / Q000494:pharmacology; D010940:Plant Proteins; D006109:Poaceae / Q000276:immunology; D011058:Pollen / Q000276:immunology; D011994:Recombinant Proteins / Q000494:pharmacology; D000090324:Tumor Protein, Translationally-Controlled 1
chemical_list: D000276:Adjuvants, Immunologic; D000485:Allergens; C026967:Amb a I protein, Ambrosia artemisiifolia; D000888:Antibodies, Anti-Idiotypic; D052179:Antigens, Plant; D014408:Biomarkers, Tumor; D007375:Interleukin-1; D008222:Lymphokines; D010940:Plant Proteins; D011994:Recombinant Proteins; D000090324:Tumor Protein, Translationally-Controlled 1; C026408:anti-IgE antibodies; D007073:Immunoglobulin E