bromochloroacetic-acid and Food-Hypersensitivity

bromochloroacetic-acid has been researched along with Food-Hypersensitivity* in 2 studies

Other Studies

2 other study(ies) available for bromochloroacetic-acid and Food-Hypersensitivity

ArticleYear
The nonlesional skin surface distinguishes atopic dermatitis with food allergy as a unique endotype.
    Science translational medicine, 2019, 02-20, Volume: 11, Issue:480

    Skin barrier dysfunction has been reported in both atopic dermatitis (AD) and food allergy (FA). However, only one-third of patients with AD have FA. The purpose of this study was to use a minimally invasive skin tape strip sampling method and a multiomics approach to determine whether children with AD and FA (AD

    Topics: Adolescent; Area Under Curve; Child; Child, Preschool; Dendritic Cells; Dermatitis, Atopic; Epidermis; Filaggrin Proteins; Food Hypersensitivity; Humans; Intermediate Filament Proteins; Keratins; Lipids; Microbiota; Skin; Surgical Tape; Transcriptome; Water Loss, Insensible

2019
Glycine-rich cell wall proteins act as specific antigen targets in autoimmune and food allergic disorders.
    International immunology, 2000, Volume: 12, Issue:5

    Our objective was to investigate the presence of a B and T cell immune response directed against the glycine-rich cell wall protein (GRP) in patients with different autoimmune disorders and with food allergy. GRP is an ubiquitous food protein that has high homology with cytokeratins and other self proteins [Epstein-Barr virus nuclear antigen-1 (EBNA-I), heterogeneous nuclear ribonucleoprotein, fibrillar collagen] which are common targets in autoimmune disorders. A peptide (GGYGDGGAHGGGYGG) derived from GRP was used to screen human sera in direct and competitive ELISA assay. Anti-GRP-specific IgG were analyzed for their ability to cross-react with autoantigens. The intracellular cytokine profiles of the peptide-specific T cell clones obtained from representative patients have been studied. BALB/c mice were immunized with the peptide coupled to the carrier protein keyhole limpet hemocyanin (KLH). Serum IgG antibodies directed against the GRP peptide were detected in several autoimmune disorders and in food allergic patients, and were able to cross-react with autoantigens including keratin, collagen and EBNA-I. Twenty-five T cell clones showed a specific proliferative response to the GRP peptide and were of the T(h)0 phenotype. Eight of the 10 BALB/c mice immunized with the peptide coupled to KLH developed an autoimmune response. Our data suggest that phylogenetically highly conserved epitopes in plants, viruses and humans may be responsible for an autoimmune response in susceptible individuals. They also indicate that the antigen spreading of a particular sequence among apparently divergent proteins may participate to initiate or amplify an immune response.

    Topics: Amino Acid Sequence; Animals; Antigens, Surface; Autoantigens; Autoimmune Diseases; Cell Division; Collagen; Cross Reactions; Cytokines; Enzyme-Linked Immunosorbent Assay; Epitopes; Epstein-Barr Virus Nuclear Antigens; Flow Cytometry; Food Hypersensitivity; Hemocyanins; Humans; Immunoglobulin G; Keratins; Mice; Mice, Inbred BALB C; Molecular Sequence Data; Plant Proteins; T-Lymphocytes, Helper-Inducer

2000