The Influence of the Time and Temperature of Heat Treatment on the Allergenicity of Egg White Proteins

Shin, Meeyong; Han, Youngshin; Ahn, Kangmo

doi:10.4168/aair.2013.5.2.96

Cited by 72 publications

(61 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…However, heat inactivation elicits the stimulatory effect of SD MVs on NF-κB activation and microtubule formation. Because heat inactivation has been recognized as a simple way of denaturing a protein, resulting in the loss of most of its original tertiary structure and its natural bioactivity [13] , these data suggest a vital role for protein composition in the biological function of SD MVs.…”

Section: Discussionmentioning

confidence: 97%

See 1 more Smart Citation

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

et al. 2013

View full text Add to dashboard Cite

Aim: To investigate the effects of serum deprivation (SD) on microvesicles (MVs) secreted from human myeloma cells and the implications for disease progression. Methods: RPMI 8226, U266, and KM3 human myeloma cells were incubated in medium containing 10% (non-SD) or 1% fetal bovine serum (SD) and MVs were isolated. The levels and size distribution of MVs were analyzed with flow cytometry. The protein profiles of MVs were studied using 2D SDS-PAGE, MALDI-TOF-MS, and Western blotting. NF-κB activation was analyzed using EMSA. Angiogenesis was examined in Eahy926 endothelial cells. Results: Exposure of RPMI 8226 cells to SD for 24 h did not alter the number of apoptotic cells. However, SD increased the number of MVs from RPMI 8226, U266, and KM3 cells to 2.5-, 4.3-, and 3.8-fold, respectively. The size distribution of SD MVs was also significantly different from that of non-SD MVs. Three proteins ZNF224, SARM, and COBL in SD MVs were found to be up-regulated, which were involved in cell cycle regulation, signal transduction and metabolism, respectively. Co-culture of SD MVs and RPMI 8226 cells increased NF-κB activation in the target RPMI 8226 cells. Furthermore, SD MVs from RPMI 8226 cells significantly increased the microtubule formation capacity of Eahy926 endothelial cells compared with non-SD MVs. Conclusion: SD elevates the levels of microvesicles with different size distribution and selectively enriched proteins in human myeloma cells in vitro. The selectively enriched proteins, especially ZNF224, may play key roles in regulation of myeloma cells, allowing better adaptation to SD.

show abstract

Section: Discussionmentioning

confidence: 97%

“…Coculture of the same concentration of heat-inactivated (HI)-non-SD MVs or HI-SD MVs was set as a control. Heat inactivation of MVs was performed at 100 °C for 10 min [13] . Electrophoretic mobility shift assays (EMSAs) were performed using a LightShift kit (Pierce, Rockford, IL, USA).…”

Section: Western Blot Analysismentioning

confidence: 99%

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

et al. 2013

View full text Add to dashboard Cite

show abstract

“…Ovotransferrin, an iron-binding protein, is a heat-labile and digestible allergen 75,76 accounting for 12% of egg white proteins. Thirty-seven percent of egg-allergic patients were reportedly sensitized to this component.…”

Section: Ovotransferrin (Gal D 3)mentioning

confidence: 99%

Common food allergens and their IgE-binding epitopes

Matsuo

Yokooji

Taogoshi

2015

Allergology International

208

135

View full text Add to dashboard Cite

Food allergy is an adverse immune response to certain kinds of food. Although any food can cause allergic reactions, chicken egg, cow's milk, wheat, shellfish, fruit, and buckwheat account for 75% of food allergies in Japan. Allergen-specific immunoglobulin E (IgE) antibodies play a pivotal role in the development of food allergy. Recent advances in molecular biological techniques have enabled the efficient analysis of food allergens. As a result, many food allergens have been identified, and their molecular structure and IgE-binding epitopes have also been identified. Studies of allergens have demonstrated that IgE antibodies specific to allergen components and/or the peptide epitopes are good indicators for the identification of patients with food allergy, prediction of clinical severity and development of tolerance. In this review, we summarize our current knowledge regarding the allergens and IgE epitopes in the well-researched allergies to chicken egg, cow's milk, wheat, shrimp, and peanut.

show abstract

“…The IgE binding activity of the samples was further assessed by competitive inhibition ELISA, as described by Shin, Han, and Ahn (2013), with some modifications. We performed inhibition ELISA with the pooled sera of the 4 shrimp-allergic patients.…”

Section: Competitive Inhibition Elisa Analysismentioning

confidence: 99%

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Lin

Yuan

et al. 2016

Food Chemistry

View full text Add to dashboard Cite

The Influence of the Time and Temperature of Heat Treatment on the Allergenicity of Egg White Proteins

Cited by 72 publications

References 29 publications

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

Serum deprivation elevates the levels of microvesicles with different size distributions and selectively enriched proteins in human myeloma cells in vitro

Common food allergens and their IgE-binding epitopes

Effect of 4-hydroxy-2-nonenal treatment on the IgE binding capacity and structure of shrimp (Metapenaeus ensis) tropomyosin

Contact Info

Product

Resources

About