Biomedical subjects

Myung-Hyun Sohn

Publications and source records attributed to Myung-Hyun Sohn.

3 recordsLinked to original sources

PubMed2005

Murine model of buckwheat allergy by intragastric sensitization with fresh buckwheat flour extract.

Food allergies affect about 4% of the Korean population, and buckwheat allergy is one of the most severe food allergies in Korea. The purpose of the present study was to develop a murine model of IgE-mediated buckwheat hypersensitivity induced by intragastric sensitization. Young female C3H/HeJ mice were sensitized and challenged intragastricly with fresh buckwheat flour (1, 5, 25 mg/dose of proteins) mixed in cholera toxin, followed by intragastric challenge. Anaphylactic reactions, antigen-specific antibodies, splenocytes proliferation assays and cytokine productions were evaluated. Oral buckwheat challenges of sensitized mice provoked anaphylactic reactions such as severe scratch, perioral/periorbital swellings, or decreased activity. Reactions were associated with elevated levels of buckwheatspecific IgE antibodies. Splenocytes from buckwheat allergic mice exhibited significantly greater proliferative responses to buckwheat than non-allergic mice. Buckwheat-stimulated IL-4, IL-5, and INF-gamma productions were associated with elevated levels of buckwheat-specific IgE in sensitized mice. In this model, 1 mg and 5 mg dose of sensitization produced almost the same degree of Th2-directed immune response, however, a 25 mg dose showed blunted antibody responses. In conclusion, we developed IgE-mediated buckwheat allergy by intragastric sensitization and challenge, and this model could provide a good tool for future studies.

Anaphylaxis↗

PubMed2004

German cockroach extract induces activation of human eosinophils to release cytotoxic inflammatory mediators.

BACKGROUND: Eosinophils play an important role in the pathogenesis of allergic diseases. Sensitization and exposure to cockroach allergen have been demonstrated to be one of the major risk factors for the development of bronchial asthma. However, little is known regarding the functional capacity of cockroach extract antigen to activate human eosinophils. OBJECTIVE: We investigated whether German cockroach extract can activate human eosinophils to release cytotoxic inflammatory mediators. METHODS: Purified eosinophils from the peripheral blood were incubated with various concentrations (0-200 microg/ml) of German cockroach extract antigen. Effector functions of eosinophils were checked by degranulation and superoxide anion production. In addition, we examined surface expression of CD11b and CD69, and intracellular activation of p38 mitogen-activated protein kinase (p38 MAP kinase) in cockroach-stimulated eosinophils. RESULTS: German cockroach extract induced degranulation and superoxide production from human eosinophils. In addition, incubation of eosinophils for 3 h with the cockroach extract resulted in an increased level of the surface expression of CD11b and CD69. Furthermore, cockroach-induced superoxide production from eosinophils was significantly inhibited by the pretreatment of cells with a p38 MAP kinase inhibitor SB202190. Indeed, a large amount of phosphorylated forms of p38 MAP kinase was detected in cockroach-stimulated eosinophils. CONCLUSIONS: Our results suggest that German cockroach extract induces activation of human eosinophils to release cytotoxic inflammatory mediators such as superoxide and granular proteins.

Allergens↗

PubMedDate not supplied

Genetically modified and wild soybeans: an immunologic comparison.

Most traits introduced into genetically engineered crops result from the expression of new proteins. As the first step toward assessing the allergenic potential of genetically modified organism (GMO) food, immunologic and physicochemical characterizations are needed. We prepared crude extract from GMO soybeans, wild soybeans, curd, and soy milk and then performed sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). After acidification with HCl, the samples were separated to globulin and whey. To evaluate changes in protein composition, either the samples were heated or pepsin was added. Polymerase chain reaction with primer encoding the 35S-promotor and the 3-enol-pyruvyl-shikimat-5-phosphat-synthase gene were performed, respectively, to detect the GMO component. SDS-PAGE results showed definite protein bands at 80 kDa in GMO soybean, 50 kDa in wild soybean, and a similar distribution of protein bands was noticed below 40 kDa. It was difficult to observe protein distribution because of modifications that occurred during processing in soybean-processed products. After heating, proteins of GMO and wild soybeans showed similar distributions and no distinct bands were detected at 50 and 80 kDa. Although SDS-PAGE analyses of raw GMO and wild soybeans differed, the same protein bands of 68, 37, and 20 kDa were observed in the globulin fraction after acidification. After adding pepsin, 20- and 68-kDa bands were found preserved in GMO and wild soybeans. The polymerase chain reaction procedures with primers specific to GMO soybeans showed that GMO soybeans and some curd samples included a GMO component. The skin test results of 49 patients showed 13 positive results to wild soybeans and 8 positive results to GMO soybeans. One patient had a positive skin test result to GMO soybeans only. Sera from nine patients with positive skin tests to the crude extract and a positive capsulated allergen product test to the soybean antigen were used for the immunoblotting of GMO and wild soybeans. GMO soybeans revealed a unique strong immunoglobulin E binding band at 25 kDa in some patients and wild soybeans showed a strong immunoglobulin E binding band at 30-36 kDa. To assess the allergenicity of GMO food, more research, including a selection of controlled sample materials and immunoassays of qualified sera, is needed.

Child↗