ENDOCRINOLOGICAL INTERRELATED DISEASES: CELIAC DISEASE AND DIABETES MELLITUS
https://doi.org/10.31677/2311-0651-2019-26-4-103-108
Abstract
About the Authors
K. A. TabanyukhovRussian Federation
Graduate Student
V. A. Scryabin
Russian Federation
Candidate of Technical Sciences, Associate Professor
References
1. Generation of wheat gluten hydrolysates with dipeptidyl peptidase IV (DPP-IV) inhibitory properties / A. B. Nongonierma, M. Hennemann, S. Paolella, R. J. Fitz Gerald // Food Funct. – 2017. – Vol. 8 (6). – P. 2249–2257. – DOI: 10.1039.
2. A food-grade enzyme preparation with modest gluten detoxification properties / J. Ehren, B. Moron, E. Martin [et al.] // PLoS One. – 2009. – Vol. 4 (7). – e6313. – doi:10.1371.
3. Skryabin V. A., Tabanyuhov K. A. Al’ternativnye prichiny razvitiya celiakii // Hleboprodukty. – 2018. – № 7. – S. 26–28.
4. Skryabin V. A., Tabanyuhov K. A. Himicheskaya ugroza prodovol’stvennoj bezopasnosti zerna // Innovacii i prodovol’stvennaya bezopasnost». – 2018. – № 4 (22). – S. 26–30.
5. Pat. № 2011134582/15. Ingibiruyushchee dipeptidilpeptidazu IV sredstvo i farmacevticheskaya kompoziciya na ego osnove / V. M. Kreminskaya, N. N. Zolotov – Opubl. 10.03.2013. Byul. № 18.
6. Production of a novel wheat gluten hydrolisate containing dipeptidyl peptidase – IV inhibitory tripeptides using ginger protease / Y. Taga, O. Hayashida, M. Kusubata [et al.] // Biosci Biotechnol Biochem. – 2017. – 81 (9). – P. 1823–1828. – DOI: 10.1080.
7. Kagnoff M. F. Celiac disease: pathogenesis of a model immunogenetic disease // J. Clin. Invest. – 2007. Vol. 117. – P. 41–49.
8. Duodenal histology in patients with celiac disease after treatment with a gluten-free diet / S. K. Lee, W. Lo, L. Memeo [et al.] // Gastrointest. Endosc. – 2003. – Vol. 57. – P. 187–191.
9. Low-dose gluten challenge in celiac sprue: malabsorptive and antibody responses / G. G. Pyle, B. Paaso, B. E. Anderson [et al.] // Clin. Gastroenterol. Hepatol. – 2005. – Vol. 3. – P. 679–686.
10. Guandalini S., Assiri A. Celiac disease: a review // JAMA Pediatr. – 2014. – Vol. 168 (3). – P. 272–278. – DOI:10.1001.
11. Etiology of nonresponsive celiac disease: results of a systematic approach / A. S. Abdulkarim, L. J. Burgart, J. See, J. A. Murray // Am. J. Gastroenterol. – 2002. – Vol. 97. – P. 2016–2021.
12. Etiologies and predictors of diagnosis in nonresponsive celiac disease / D. A. Leffler, M. Dennis, B. Hyett [et al.] // Clin. Gastroenterol. Hepatol. – 2007. – Vol. 7 (5). – P. 445–450.
13. Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue / J. Gass, M. T. Bethune, M. Siegel [et al.] // Gastroenterology. – 2007. – Vol. 133. – P. 472–480.
14. Analysis of secreted proteins during conidial germination of Aspergillus oryzae RIB40 / L. Y. Zhu, C. H. Nguyen, T. Sato, M. Z. Takeuchi // Biosci. Biotechnol. Biochem. – 2004. – Vol. 68. – P. 2607–2612.
15. Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease / M. T. Bethune, P. Strop, Y. Tang [et al.] // Chem. Biol. – 2006. – Vol. 13. – P. 637–647.
16. Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease / D. Stepniak, L. Spaenij-Dekking, C. Mitea [et al.] // Am. J. Physiol. Gastrointest. Liver Physiol. – 2006. – Vol. 291. – P. 621–629.
17. Toward the assessment of food toxicity for celiac patients: characterization of monoclonal antibodies to a main immunogenic gluten peptide / B. Moron, M. T. Bethune, I. Comino [et al.] // PLoS ONE. – 2008. – Vol. 3. – e2294.
18. Naveena B. M., Mendiratta S. K., Anjaneyulu A. S. Tenderization of buffalo meat using plant proteases from Cucumis trigonus Roxb (Kachri) and Zingiber officinale roscoe (Ginger rhizome) // Meat Sci. – 2004. – Vol. 68. – P. 363–369. – DOI:10.1016.
19. Kong X., Zhou H., Qian H. Enzymatic preparation and functional properties of wheat gluten hydrolysates // Food Chem. – 2007. – Vol. 101. – P. 615–620. – DOI:10.1016.
20. Dipeptidyl peptidase-IV inhibitory peptides generated by tryptic hydrolysis of a whey protein concentrate rich in β-lactoglobulin / S. T. Silveira, D. Martínez-Maqueda, I. Recio [et al.] // Food Chem. – 2013. – Vol. 141. – P. 1072–1077. – DOI:10.1016.
Review
For citations:
Tabanyukhov K.A., Scryabin V.A. ENDOCRINOLOGICAL INTERRELATED DISEASES: CELIAC DISEASE AND DIABETES MELLITUS. Innovations and Food Safety. 2019;(4):103-108. (In Russ.) https://doi.org/10.31677/2311-0651-2019-26-4-103-108