Degranulation of basophilic leukemia cells on branched-chain peptide array with an OVA–DNP double epitope
| Autor: | Toshimi Sugiura, Noriyasu Okazaki, Mina Okochi, Hiroyuki Honda, Hisayuki Sugiura |
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| Rok vydání: | 2014 |
| Předmět: |
chemistry.chemical_classification
Environmental Engineering biology Biomedical Engineering Degranulation chemical and pharmacologic phenomena Bioengineering Peptide Immunoglobulin E Molecular biology Epitope Amino acid Basophilic Ovalbumin chemistry Biochemistry biology.protein Biotechnology Egg white |
| Zdroj: | Biochemical Engineering Journal. 87:8-14 |
| ISSN: | 1369-703X |
| Popis: | Simple method for identification of heterovalent allergen epitopes was constructed to reflect the allergic reaction initiated by the cross-linking of the IgE receptors. The peptide array-based degranulation assay that enables interaction between solid support-bound peptide pairs and IgE sensitized basophilic leukemia cells was developed. Using lysine side chains, a chicken egg white ovalbumin (OVA) epitope and a dinitrophenol (DNP) modified amino acid was synthesized in the branched-chain peptide array. The basophilic leukemia cells sensitized with anti-OVA IgE and anti-DNP IgE induced degranulation directly on the branched-chain peptide array. The OVA–DNP double peptide disk caused the release of 37.5% of β-hexosaminidase whereas the DNP-only peptide disk caused the release by 20.9%. These results show that the double epitope branched-chain peptide array can induce degranulation, and would represent a suitable model for screening the heterovalent epitope pairs of allergens. |
| Databáze: | OpenAIRE |
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