Zum Hauptinhalt springen
Artikel
Lizenziert
Nicht lizenziert Erfordert eine Authentifizierung

Different Damage to the Mechanical Barrier Function of IPEC-J2 Induced by Soybean Allergen β-conglycinin Hydrolyzed Peptides

  • , , , und EMAIL logo
Veröffentlicht/Copyright: 31. August 2017
Veröffentlichen auch Sie bei De Gruyter Brill

Abstract

Three major enzyme-hydrolyzed peptides have been produced after simulative digestion in vitro of soybean β-conglycinin. The intestinal barrier of IPEC-J2 induced by β-conglycinin enzyme-hydrolyzed peptides was evaluated in this study. The increased alkaline phosphatase (AP) activity was actually linearly correlated with the incubation time by the hydrolysate, the purified 52 kD peptide, or the mixture of 25 and 30 kD peptides. The MTT and TEER values declined in dose-dependence (0–2 mg/mL, p \lt 0.05) or in time-dependence (2–24 h, p \lt 0.05). After treatment with different hydrolyzed peptides, the tight junction expression of claudin-3, claudin-4, occludin, and ZO-1 were reduced (p \lt 0.05). Finally, it is found out that the maximum damage to the epithelial barrier function was induced by the mixture of 25 and 30 kD peptide, whereas the minimum damage was caused by the 52 kD peptide.

Funding statement: This work was financially supported by the National Natural Science Foundation of China (No. 31572439 and No.31572415), the Natural Science Foundation of Jilin Province of China (No. 20160101348JC), “Twelfth Five-year Plan”for Sci & Tech Research Program of Jilin Education Department of P.R. China (No.2015198).

References

1. Friedman M, Brandon DL. Nutritional and health benefits of soy proteins. J Agri Food Chem 2001;49(3):1069–1086.10.1021/jf0009246Suche in Google Scholar

2. Li D, Nelssen J, Reddy P, Blecha F, Hancock J, Allee G, et al. Transient hypersensitivity to soybean meal in the early-weaned pig. J Anim Sci 1990;68(6):1790–1799.10.2527/1990.6861790xSuche in Google Scholar PubMed

3. Perez MD, Mills EN, Lambert N, Johnson IT, Morgan MR. The use of anti-soya globulin antisera in investigating soya digestion in vivo. J Sci Food Agr 2000;80(4):513–521.10.1002/(SICI)1097-0010(200003)80:4<513::AID-JSFA562>3.0.CO;2-NSuche in Google Scholar

4. Mills E, Madsen C, Shewry P, Wichers H. Food allergens of plant origin-their molecular and evolutionary relationships. Trends Food Sci Tech 2003;14(4):145–156.10.1016/S0924-2244(03)00026-8Suche in Google Scholar

5. Lehrer SB, Horner WE, Reese G, Taylor S. Why are some proteins allergenic? Implications for biotechnology. Crit Rev Food Sci Nutr 1996;36(6):553–564.10.1080/10408399609527739Suche in Google Scholar PubMed

6. Bannon GA. What makes a food protein an allergen? Curr Allergy Asthma Rep 2004;4(1):43–46.10.1007/s11882-004-0042-0Suche in Google Scholar PubMed

7. Adachi A, Horikawa T, Shimizu H, Sarayama Y, Ogawa T, Sjolander S, et al. Soybean β-conglycinin as the main allergen in a patient with food-dependent exercise-induced anaphylaxis by tofu: food processing alters pepsin resistance. Clin Exp Allergy 2009;39(1):167–173.10.1111/j.1365-2222.2008.03148.xSuche in Google Scholar

8. Lallès JP, Tukur HM, Salgado P, Mills EC, Morgan MR, Quillien L, et al. Immunochemical studies on gastric and intestinal digestion of soybean glycinin and β-conglycinin in vivo. J Agri Food Chem 1999;47(7):2797–2806.10.1021/jf980882+Suche in Google Scholar

9. Astwood JD, Leach JN, Fuchs RL. Stability of food allergens to digestion in vitro. Nat Biotechnol 1996;14(10):1269–1273.10.1038/nbt1096-1269Suche in Google Scholar PubMed

10. Moreno FJ. Clemente A: 2S albumin storage proteins: what makes them food allergens?. The Open Biochem 2008;2(1) 12–28.10.2174/1874091X00802010016Suche in Google Scholar

11. Zhao Y, Qin G, Han R, Wang J, Zhang X, Liu D. β-Conglycinin reduces the tight junction occludin and ZO-1 expression in IPEC-J2. Int J Mol Sci 2014;15(2):1915–1926.10.3390/ijms15021915Suche in Google Scholar PubMed PubMed Central

12. Zhao Y, Liu D, Han R, Zhang X, Zhang S, Qin G. Soybean allergen glycinin induced the destruction of the mechanical barrier function in IPEC-J2. Food Agr Immunol 2015;26(4):601–609.10.1080/09540105.2014.998638Suche in Google Scholar

13. Zheng S. The identification of potential allergenic subunits and epitope-containing peptide fragments in soybean protein glycinin and β-conglycinin. Ph. D. Thesis, Changchun, China: Jilin Agricultural University, 2009.Suche in Google Scholar

14. Iwabuchi S, Yamauchi F. Determination of glycinin and. beta.-conglycinin in soybean proteins by immunological methods. J Agri Food Chem 1987;35(2):200–205.10.1021/jf00074a009Suche in Google Scholar

15. Zhao Y, Qin GX, Sun ZW, Zhang B, Wang T. Stability and immunoreactivity of glycinin and β-conglycinin to hydrolysis in vitro. Food Agr Immunol 2010;21:253–263.10.1080/09540101003758954Suche in Google Scholar

16. Dunsford BR, Knabe D, Haensly W. Effect of dietary soybean meal on the microscopic anatomy of the small intestine in the early-weaned pig. J Anim Sci 1989;67(7):1855–1863.10.2527/jas1989.6771855xSuche in Google Scholar PubMed

17. Qin G, Xu L, Jiang H, van der Poel A, Bosch M, Verstegen M. The effects of Chinese and Argentine soybeans on nutrient digestibility and organ morphology in Landrace and Chinese Min pigs. Asian Austral J Anim 2002;15(4):555–564.10.5713/ajas.2002.555Suche in Google Scholar

18. Pitman RS, Blumberg RS. First line of defense: the role of the intestinal epithelium as an active component of the mucosal immune system. J Gastroenterol 2000;35(11):805–814.10.1007/s005350070017Suche in Google Scholar PubMed

19. Mariani V, Palermo S, Fiorentini S, Lanubile A, Giuffra E. Gene expression study of two widely used pig intestinal epithelial cell lines: IPEC-J2 and IPI-2I. Vet Immunol Immunopathol 2009;131(3):278–284.10.1016/j.vetimm.2009.04.006Suche in Google Scholar PubMed

20. Berin MC, Kiliaan AJ, Yang PC, Groot JA, Kitamura Y, Perdue MH. The influence of mast cells on pathways of transepithelial antigen transport in rat intestine. J Immunol 1998;161(5):2561–2566.10.4049/jimmunol.161.5.2561Suche in Google Scholar PubMed

21. Groschwitz KR, Hogan SP. Intestinal barrier function: molecular regulation and disease pathogenesis. J Allergy Clin Immun 2009;124(1):3–20.10.1016/j.jaci.2009.05.038Suche in Google Scholar PubMed PubMed Central

22. André C, André F, Colin N, Cavagna S. Measurement of intestinal permeability to mannitol and lactulose as a means of diagnosing food allergy and evaluating therapeutic effectiveness of disodium cromoglycate. Ann Allergy 1987;59(5 Pt 2):127–130.Suche in Google Scholar PubMed

23. Ventura M, Polimeno L, Amoruso A, Gatti F, Annoscia E, Marinaro M, et al. Intestinal permeability in patients with adverse reactions to food. Digest Liver Dis 2006;38(10):732–736.10.1016/j.dld.2006.06.012Suche in Google Scholar PubMed

24. Song DJ, Cho JY, Miller M, Strangman W, Zhang M, Varki A, et al. Anti-Siglec-F antibody inhibits oral egg allergen induced intestinal eosinophilic inflammation in a mouse model. Clin Immun 2009;131(1):157–169.10.1016/j.clim.2008.11.009Suche in Google Scholar PubMed PubMed Central

25. Perrier C, Corthesy B. Gut permeability and food allergies. Clin Exp Allergy 2011;41(1):20–28.10.1111/j.1365-2222.2010.03639.xSuche in Google Scholar PubMed

Published Online: 2017-8-31

© 2017 Walter de Gruyter GmbH, Berlin/Boston

Heruntergeladen am 19.4.2026 von https://www.degruyterbrill.com/document/doi/10.1515/ijfe-2016-0370/html
Button zum nach oben scrollen