메뉴 건너뛰기




Volumn 73, Issue 8, 2015, Pages 544-552

Possible association between celiac disease and bacterial transglutaminase in food processing: a hypothesis

Author keywords

celiac disease; food processing; gluten; microbial transglutaminase; tissue transglutaminase

Indexed keywords

BACTERIAL ENZYME; CELL PROTEIN; FOOD ADDITIVE; IMMUNOGLOBULIN A; IMMUNOGLOBULIN G; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE; GLUTEN;

EID: 85017759799     PISSN: 00296643     EISSN: 17534887     Source Type: Journal    
DOI: 10.1093/NUTRIT/NUV011     Document Type: Article
Times cited : (84)

References (77)
  • 1
    • 72149093493 scopus 로고    scopus 로고
    • New therapeutic strategies in celiac disease
    • Lerner A. New therapeutic strategies in celiac disease. Autoimm Rev. 2010;9: 144-147.
    • (2010) Autoimm Rev , vol.9 , pp. 144-147
    • Lerner, A.1
  • 2
    • 79960136115 scopus 로고    scopus 로고
    • Environmental and lifestyle influences on disorders of the large and small intestine: implication for treatment
    • Hall EH, Crowe SE. Environmental and lifestyle influences on disorders of the large and small intestine: implication for treatment. Dig Dis. 2011;29:249-254.
    • (2011) Dig Dis , vol.29 , pp. 249-254
    • Hall, EH1    Crowe, SE.2
  • 3
    • 0028207178 scopus 로고
    • Factors affecting the clinical presentation and time diagnosis of celiac disease: the Jerusalem and the West Bank-Gaza experience
    • Lerner A. Factors affecting the clinical presentation and time diagnosis of celiac disease: the Jerusalem and the West Bank-Gaza experience. Isr J Med Sci. 1994;11: 294-295.
    • (1994) Isr J Med Sci , vol.11 , pp. 294-295
    • Lerner, A.1
  • 4
    • 84875687071 scopus 로고    scopus 로고
    • The thrombophilic network of autoantibodies in celiac disease
    • Lerner A, Agmon-Levin N, Shapira Y, et al. The thrombophilic network of autoantibodies in celiac disease. BMC Med. 2013;11:89-95.
    • (2013) BMC Med , vol.11 , pp. 89-95
    • Lerner, A1    Agmon-Levin, N2    Shapira, Y3
  • 5
    • 85010315030 scopus 로고    scopus 로고
    • Nonnutritional environmental factors associated with celiac disease: the infectome
    • Y Shoenfeld, N Rose, eds. 2nd ed. San Diego: Elsevier B.V
    • Lerner A, Reif S. Nonnutritional environmental factors associated with celiac disease: the infectome. In: Y Shoenfeld, N Rose, eds. Infection and Autoimmunity. 2nd ed. San Diego: Elsevier B.V; 2015:829-835.
    • (2015) Infection and Autoimmunity , pp. 829-835
    • Lerner, A1    Reif, S.2
  • 6
    • 84904105948 scopus 로고    scopus 로고
    • Early microbial markers of celiac disease
    • Viitasalo L, Niemi L, Ashorn M, et al. Early microbial markers of celiac disease. J Clin Gastroenterol. 2014;48:620-624.
    • (2014) J Clin Gastroenterol , vol.48 , pp. 620-624
    • Viitasalo, L1    Niemi, L2    Ashorn, M3
  • 8
    • 67649200339 scopus 로고    scopus 로고
    • Increased prevalence and mortality in undiagnosed celiac disease
    • Rubio-Tapia A, Kyle RA, Kaplan EL, et al. Increased prevalence and mortality in undiagnosed celiac disease. Gastroenterology. 2009;137:88-93.
    • (2009) Gastroenterology , vol.137 , pp. 88-93
    • Rubio-Tapia, A1    Kyle, RA2    Kaplan, EL3
  • 9
    • 33747622078 scopus 로고    scopus 로고
    • Celiac disease: India on the global map
    • Yachha SK. Celiac disease: India on the global map. J Gastroenterol Hepatol. 2006; 21:1511-1513.
    • (2006) J Gastroenterol Hepatol , vol.21 , pp. 1511-1513
    • Yachha, SK.1
  • 10
    • 85027927818 scopus 로고    scopus 로고
    • Microbial transglutaminase and its application in the food industry. A review
    • Kieliszek M, Misiewicz A. Microbial transglutaminase and its application in the food industry. A review. Folia Microbiol. 2014;59:241-250.
    • (2014) Folia Microbiol , vol.59 , pp. 241-250
    • Kieliszek, M1    Misiewicz, A.2
  • 11
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama K, Nio N, Kikuchi Y. Properties and applications of microbial transglutaminase. Appl Microbiol Biotechnol. 2004;64:447-454.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 447-454
    • Yokoyama, K1    Nio, N2    Kikuchi, Y.3
  • 12
    • 84905968414 scopus 로고    scopus 로고
    • Transglutaminases: recent achievements and new sources
    • Martins IM, Matos M, Costa R, et al. Transglutaminases: recent achievements and new sources. Appl Microbiol Biotechnol. 2014;98:6957-6964.
    • (2014) Appl Microbiol Biotechnol , vol.98 , pp. 6957-6964
    • Martins, IM1    Matos, M2    Costa, R3
  • 13
    • 70449107878 scopus 로고    scopus 로고
    • Recent patents on transglutaminase production and applications: a brief review
    • Santos M, Torné JM. Recent patents on transglutaminase production and applications: a brief review. Recent Pat Biotechnol. 2009;3:166-174.
    • (2009) Recent Pat Biotechnol , vol.3 , pp. 166-174
    • Santos, M1    Torné, JM.2
  • 14
    • 33646138479 scopus 로고    scopus 로고
    • Transglutaminases: a meeting point for wheat allergy, celiac disease, and food safety
    • Malandain H. Transglutaminases: a meeting point for wheat allergy, celiac disease, and food safety. Europ Ann Aller Clin Immun. 2005;37:397-403.
    • (2005) Europ Ann Aller Clin Immun , vol.37 , pp. 397-403
    • Malandain, H.1
  • 15
    • 85159551828 scopus 로고    scopus 로고
    • Food and beverage enzyme demands
    • Cleveland, OH: The Freedonia Group. December Accessed December 2011
    • The Freedonia Group. Food and beverage enzyme demands. In: World Enzymes: Industry Study with Forecast for 2015 & 2020. Cleveland, OH: The Freedonia Group. December 2011. http://www.freedoniagroup.com/brochure/28xx/2824smwe.pdf. Accessed December 2011.
    • (2011) World Enzymes: Industry Study with Forecast for 2015 & 2020
  • 16
    • 84899993229 scopus 로고    scopus 로고
    • Incidence and prevalence of celiac disease and dermatitis herpetiformis in the UK over two decades: population-based Study
    • West J, Fleming KM, Tata LJ, et al. Incidence and prevalence of celiac disease and dermatitis herpetiformis in the UK over two decades: population-based Study. Am J Gastroenterol. 2014;109:757-768.
    • (2014) Am J Gastroenterol , vol.109 , pp. 757-768
    • West, J1    Fleming, KM2    Tata, LJ3
  • 17
    • 8744249320 scopus 로고    scopus 로고
    • Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO decision tree
    • Pedersen MH, Hansen TK, Sten E, et al. Evaluation of the potential allergenicity of the enzyme microbial transglutaminase using the 2001 FAO/WHO decision tree. Mol Nutr Food Res. 2004;48:434-440.
    • (2004) Mol Nutr Food Res , vol.48 , pp. 434-440
    • Pedersen, MH1    Hansen, TK2    Sten, E3
  • 18
    • 84901445820 scopus 로고    scopus 로고
    • Microbial transglutaminase: a new and emerging occupational allergen
    • De Palma G, Apostoli P, Mistrello G, et al. Microbial transglutaminase: a new and emerging occupational allergen. Ann Allergy Asthma Immunol. 2014;112: 553-554.
    • (2014) Ann Allergy Asthma Immunol , vol.112 , pp. 553-554
    • De Palma, G1    Apostoli, P2    Mistrello, G3
  • 19
    • 1042290533 scopus 로고    scopus 로고
    • Tissue transglutaminase - the key player in celiac disease: a review
    • Reif S, Lerner A. Tissue transglutaminase - the key player in celiac disease: a review. Autoimmun Rev. 2004;3:40-45.
    • (2004) Autoimmun Rev , vol.3 , pp. 40-45
    • Reif, S1    Lerner, A.2
  • 20
    • 7044233640 scopus 로고    scopus 로고
    • Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease
    • Skovbjerg H, Koch C, Anthonsen D, et al. Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease. Biochem Biophys Acta. 2004;1690:220-230.
    • (2004) Biochem Biophys Acta , vol.1690 , pp. 220-230
    • Skovbjerg, H1    Koch, C2    Anthonsen, D3
  • 21
    • 33748437518 scopus 로고    scopus 로고
    • Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten
    • Yong YH, Yamaguchi S, Matsumura Y. Effects of enzymatic deamidation by protein-glutaminase on structure and functional properties of wheat gluten. J Agric Food Chem. 2006;54:6034-6040.
    • (2006) J Agric Food Chem , vol.54 , pp. 6034-6040
    • Yong, YH1    Yamaguchi, S2    Matsumura, Y.3
  • 22
    • 39649089846 scopus 로고    scopus 로고
    • Microbial transglutaminases generate T cell stimulatory epitopes involved in celiac disease
    • Dekking EHA, Van Veblen PA, de Ru A, et al. Microbial transglutaminases generate T cell stimulatory epitopes involved in celiac disease. J Cereal Sci. 2008;47:339-346.
    • (2008) J Cereal Sci , vol.47 , pp. 339-346
    • Dekking, EHA1    Van Veblen, PA2    de Ru, A3
  • 23
    • 84905284806 scopus 로고    scopus 로고
    • Microbial transglutaminase treatment in pasta-production does not affect the immunoreactivity of gliadin with celiac disease patients' sera
    • Ruh T, Ohsam J, Pasternack R, et al. Microbial transglutaminase treatment in pasta-production does not affect the immunoreactivity of gliadin with celiac disease patients' sera. J Agric Food Chem. 2014;62:7604-7611.
    • (2014) J Agric Food Chem , vol.62 , pp. 7604-7611
    • Ruh, T1    Ohsam, J2    Pasternack, R3
  • 24
    • 54049147249 scopus 로고    scopus 로고
    • The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions
    • Stamnaes J, Fleckenstein B, Sollid LM. The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions. Biochim Biophys Acta. 2008;1784:1804-1811.
    • (2008) Biochim Biophys Acta , vol.1784 , pp. 1804-1811
    • Stamnaes, J1    Fleckenstein, B2    Sollid, LM.3
  • 25
    • 84870558602 scopus 로고    scopus 로고
    • Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase
    • Jiang J, Xiong YL. Extreme pH treatments enhance the structure-reinforcement role of soy protein isolate and its emulsions in pork myofibrillar protein gels in the presence of microbial transglutaminase. Meat Sci. 2013;93:469-476.
    • (2013) Meat Sci , vol.93 , pp. 469-476
    • Jiang, J1    Xiong, YL.2
  • 26
    • 0037072829 scopus 로고    scopus 로고
    • Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation process
    • Fleckenstein B, Molberg Ø, Qiao SW, et al. Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation process. J Biol Chem. 2002;277:34109-34116.
    • (2002) J Biol Chem , vol.277 , pp. 34109-34116
    • Fleckenstein, B1    Molberg, Ø2    Qiao, SW3
  • 27
    • 0021969767 scopus 로고
    • Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease
    • Bruce SE, Bjarnason I, Peters TJ. Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease. Clin Sci. 1985;68:573-579.
    • (1985) Clin Sci , vol.68 , pp. 573-579
    • Bruce, SE1    Bjarnason, I2    Peters, TJ.3
  • 28
    • 0035988899 scopus 로고    scopus 로고
    • Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of celiac disease
    • Skovbjerg H, Noren O, Anthonsen D, et al. Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of celiac disease. Scand J Gastroenterol. 2002;37:812-817.
    • (2002) Scand J Gastroenterol , vol.37 , pp. 812-817
    • Skovbjerg, H1    Noren, O2    Anthonsen, D3
  • 29
    • 27344458520 scopus 로고    scopus 로고
    • Addition of transglutaminase to cereal products may generate the epitope responsible for coeliac disease
    • Gerrard JA, Sutton KH. Addition of transglutaminase to cereal products may generate the epitope responsible for coeliac disease. Trends in Food Sci Technol. 2005;16:510-512.
    • (2005) Trends in Food Sci Technol , vol.16 , pp. 510-512
    • Gerrard, JA1    Sutton, KH.2
  • 30
    • 84886191464 scopus 로고    scopus 로고
    • Protein cross-linking in food-structure, applications, implications for health and food safety
    • YH Hui, ed. 2nd ed. Ames, IA: Blackwell
    • Cottam JRA, Gerrard JA. Protein cross-linking in food-structure, applications, implications for health and food safety. In: YH Hui, ed. Food Biochemistry and Food Processing, 2nd ed. Ames, IA: Blackwell; 2012:207-223.
    • (2012) Food Biochemistry and Food Processing , pp. 207-223
    • Cottam, JRA1    Gerrard, JA.2
  • 31
    • 0037070314 scopus 로고    scopus 로고
    • NMR-based screening method for transglutaminases: rapid analysis of their substrate specificities and reaction rates
    • Shimba N, Yokoyama K, Suzuki E. NMR-based screening method for transglutaminases: rapid analysis of their substrate specificities and reaction rates. J Agric Food Chem. 2002;50:1330-1334.
    • (2002) J Agric Food Chem , vol.50 , pp. 1330-1334
    • Shimba, N1    Yokoyama, K2    Suzuki, E.3
  • 33
    • 42949105493 scopus 로고    scopus 로고
    • Microstructure, fundamental rheology and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase
    • Renzetti S, Dal Bello F, Arendt EK. Microstructure, fundamental rheology and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase. J Cereal Sci. 2008;48:33-45.
    • (2008) J Cereal Sci , vol.48 , pp. 33-45
    • Renzetti, S1    Dal Bello, F2    Arendt, EK.3
  • 34
    • 13944267448 scopus 로고    scopus 로고
    • Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough
    • Autio K, Kruus K, Knaapila A, et al. Kinetics of transglutaminase-induced cross-linking of wheat proteins in dough. J Agric Food Chem. 2005;53:1039-1045.
    • (2005) J Agric Food Chem , vol.53 , pp. 1039-1045
    • Autio, K1    Kruus, K2    Knaapila, A3
  • 35
    • 84891876048 scopus 로고    scopus 로고
    • Microbial transglutaminase displays broad acyl-acceptor substrate specificity
    • Gundersen MT, Keillor JW, Pelletier JN. Microbial transglutaminase displays broad acyl-acceptor substrate specificity. App Microbiol Biotechnol. 2013;98:219-230.
    • (2013) App Microbiol Biotechnol , vol.98 , pp. 219-230
    • Gundersen, MT1    Keillor, JW2    Pelletier, JN.3
  • 36
    • 0034526856 scopus 로고    scopus 로고
    • Substrate specificities of microbial transglutaminase for primary amines
    • Ohtsuka T, Sawa A, Kawabata R, et al. Substrate specificities of microbial transglutaminase for primary amines. J Agric Food Chem. 2000;48:6230-6233.
    • (2000) J Agric Food Chem , vol.48 , pp. 6230-6233
    • Ohtsuka, T1    Sawa, A2    Kawabata, R3
  • 37
    • 72649084947 scopus 로고    scopus 로고
    • Substrate specificity of microbial transglutaminase as revealed by three-dimentional docking simulation and mutagenesis
    • Tagami U, Shimba N, Nakaamura M, et al. Substrate specificity of microbial transglutaminase as revealed by three-dimentional docking simulation and mutagenesis. Protein Eng Des Sel. 2009;22:747-752.
    • (2009) Protein Eng Des Sel , vol.22 , pp. 747-752
    • Tagami, U1    Shimba, N2    Nakaamura, M3
  • 38
    • 84870764794 scopus 로고    scopus 로고
    • Improvement of gluten-free bread quality using transglutaminase, various extruded flours and protein isolates
    • Smerdel B, Pollak L, Novotni D, et al. Improvement of gluten-free bread quality using transglutaminase, various extruded flours and protein isolates. J Food Nutr Res. 2012;51:242-253.
    • (2012) J Food Nutr Res , vol.51 , pp. 242-253
    • Smerdel, B1    Pollak, L2    Novotni, D3
  • 39
    • 42949105493 scopus 로고    scopus 로고
    • Microstructural, fundamental rheology, and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase
    • Brenzetti S, Dal Bello F, Arendt EK. Microstructural, fundamental rheology, and baking characteristics of batters and breads from different gluten-free flours treated with a microbial transglutaminase. J Cereal Sci. 2008;48:33-45.
    • (2008) J Cereal Sci , vol.48 , pp. 33-45
    • Brenzetti, S1    Dal Bello, F2    Arendt, EK.3
  • 40
    • 67549106787 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on dough proteins of hard and soft (Triticum aestivium) and durum (Triticum durum) wheat cultivars
    • Medina-Rodríguez CL, Torres P, Martínez-Bustos F, et al. Effect of microbial transglutaminase on dough proteins of hard and soft (Triticum aestivium) and durum (Triticum durum) wheat cultivars. Cereal Chemist. 2009;86:127-132.
    • (2009) Cereal Chemist , vol.86 , pp. 127-132
    • Medina-Rodríguez, CL1    Torres, P2    Martínez-Bustos, F3
  • 41
    • 79955073132 scopus 로고    scopus 로고
    • Effect of cooking on physical and sensory properties of fresh yellow alkaline noodles prepared by partial substitution of wheat flour with soy protein isolate and treated with cross-linking agents
    • Yeoh SY, Alkarkhi AF, Ramli SB, et al. Effect of cooking on physical and sensory properties of fresh yellow alkaline noodles prepared by partial substitution of wheat flour with soy protein isolate and treated with cross-linking agents. Int J Food Sci Nutr. 2011;62:410-417.
    • (2011) Int J Food Sci Nutr , vol.62 , pp. 410-417
    • Yeoh, SY1    Alkarkhi, AF2    Ramli, SB3
  • 42
    • 44949153575 scopus 로고    scopus 로고
    • Effect of microbial transglutaminase on spaghetti quality
    • Aalami M, Leelavathi K. Effect of microbial transglutaminase on spaghetti quality. J Food Sci. 2008;73:C306-C312.
    • (2008) J Food Sci , vol.73 , pp. C306-C312
    • Aalami, M1    Leelavathi, K.2
  • 43
    • 78651108998 scopus 로고    scopus 로고
    • Emulsifying properties of the transglutaminase-treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates
    • Hu X, Ren J, Zhao M, et al. Emulsifying properties of the transglutaminase-treated crosslinked product between peanut protein and fish (Decapterus maruadsi) protein hydrolysates. J Sci Food Agric. 2011;91:578-585.
    • (2011) J Sci Food Agric , vol.91 , pp. 578-585
    • Hu, X1    Ren, J2    Zhao, M3
  • 44
    • 80053183936 scopus 로고    scopus 로고
    • Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions
    • Hong GP, Min SG, Chin KB. Emulsion properties of pork myofibrillar protein in combination with microbial transglutaminase and calcium alginate under various pH conditions. Meat Sci. 2012;90:185-193.
    • (2012) Meat Sci , vol.90 , pp. 185-193
    • Hong, GP1    Min, SG2    Chin, KB.3
  • 45
    • 49649095219 scopus 로고    scopus 로고
    • Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein
    • Xiong YL, Agyare KK, Addo K. Hydrolyzed wheat gluten suppresses transglutaminase-mediated gelation but improves emulsification of pork myofibrillar protein. Meat Sci. 2008;80:535-544.
    • (2008) Meat Sci , vol.80 , pp. 535-544
    • Xiong, YL1    Agyare, KK2    Addo, K.3
  • 46
    • 85047688442 scopus 로고    scopus 로고
    • Detoxification of gluten by means of enzymatic treatment
    • Wieser H, Koehler P. Detoxification of gluten by means of enzymatic treatment. J AOAC Int. 2012;95:356-363.
    • (2012) J AOAC Int , vol.95 , pp. 356-363
    • Wieser, H1    Koehler, P.2
  • 47
    • 84905002264 scopus 로고    scopus 로고
    • Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten
    • Heredia-Sandoval NG, Islas-Rubio AR, Cabrera-Chávez F, et al. Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten. Food Funct. 2014;5:1813-1818.
    • (2014) Food Funct , vol.5 , pp. 1813-1818
    • Heredia-Sandoval, NG1    Islas-Rubio, AR2    Cabrera-Chávez, F3
  • 48
    • 34147143558 scopus 로고    scopus 로고
    • Celiac-related properties of chemically and enzymatically modified gluten proteins
    • Berti C, Roncoroni L, Falini ML, et al. Celiac-related properties of chemically and enzymatically modified gluten proteins. J Agric Food Chem. 2007;55:2482-2488.
    • (2007) J Agric Food Chem , vol.55 , pp. 2482-2488
    • Berti, C1    Roncoroni, L2    Falini, ML3
  • 49
    • 66149145935 scopus 로고    scopus 로고
    • Bovine milk caseins and transglutaminase-treated cereal prolamines are differentially recognized by IgA of celiac disease patients according to age
    • Cabrera-Chávez F, Rouzaud-Sández O, Sotelo-Cruz N, et al. Bovine milk caseins and transglutaminase-treated cereal prolamines are differentially recognized by IgA of celiac disease patients according to age. J Agric Food Chem. 2009;57:3754-3759.
    • (2009) J Agric Food Chem , vol.57 , pp. 3754-3759
    • Cabrera-Chávez, F1    Rouzaud-Sández, O2    Sotelo-Cruz, N3
  • 50
    • 84866356187 scopus 로고    scopus 로고
    • Immunological effects of transglutaminase-treated gluten in coeliac disease
    • Elli L, Roncoroni L, Hils M, et al. Immunological effects of transglutaminase-treated gluten in coeliac disease. Hum Immunol. 2012;73:992-997.
    • (2012) Hum Immunol , vol.73 , pp. 992-997
    • Elli, L1    Roncoroni, L2    Hils, M3
  • 51
    • 40549118791 scopus 로고    scopus 로고
    • Transglutaminase treatment of wheat and maize prolamines of bread increase the serum IgA reactivity of celiac disease patients
    • Cabrera-Chávez F, Rouzaud-Sández O, Sotelo-Cruz N, et al. Transglutaminase treatment of wheat and maize prolamines of bread increase the serum IgA reactivity of celiac disease patients. J Agric Food Chem. 2008;56:1387-1391.
    • (2008) J Agric Food Chem , vol.56 , pp. 1387-1391
    • Cabrera-Chávez, F1    Rouzaud-Sández, O2    Sotelo-Cruz, N3
  • 52
    • 50949126267 scopus 로고    scopus 로고
    • Immunoreactivity of antibodies against transglutaminase-deamidated gliadins in adult celiac disease
    • Falini ML, Elli L, Caramanico R, et al. Immunoreactivity of antibodies against transglutaminase-deamidated gliadins in adult celiac disease. Dig Dis Sci. 2008;53: 2697-2701.
    • (2008) Dig Dis Sci , vol.53 , pp. 2697-2701
    • Falini, ML1    Elli, L2    Caramanico, R3
  • 53
    • 84905002264 scopus 로고    scopus 로고
    • Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten
    • Heredia-Sandoval NG, Islas-Rubio AR, Cabrera-Chávez F, et al. Transamidation of gluten proteins during the bread-making process of wheat flour to produce breads with less immunoreactive gluten. Food Funct. 2014;5:1813-1818.
    • (2014) Food Funct , vol.5 , pp. 1813-1818
    • Heredia-Sandoval, NG1    Islas-Rubio, AR2    Cabrera-Chávez, F3
  • 54
    • 84864707488 scopus 로고    scopus 로고
    • Determination of microbial transglutaminase in meat and meat products. Food Addit Contam Part A
    • Kaufmann A, Koppel R, Widmer M. Determination of microbial transglutaminase in meat and meat products. Food Addit Contam Part A. Chem Anal Control Expo Risk Assess. 2012;29:1364-1373.
    • (2012) Chem Anal Control Expo Risk Assess , vol.29 , pp. 1364-1373
    • Kaufmann, A1    Koppel, R2    Widmer, M.3
  • 55
    • 78751699186 scopus 로고    scopus 로고
    • Zonulin and its regulation of intestinal barrier function: the biological door to inflammation, autoimmunity, and cancer
    • Fasano A. Zonulin and its regulation of intestinal barrier function: the biological door to inflammation, autoimmunity, and cancer. Physiol Rev. 2011;91:151-175.
    • (2011) Physiol Rev , vol.91 , pp. 151-175
    • Fasano, A.1
  • 56
    • 84873716991 scopus 로고    scopus 로고
    • Regulation of intestinal epithelial permeability by tight junctions
    • Suzuki T. Regulation of intestinal epithelial permeability by tight junctions. Cell Mol Life Sci. 2013;70:631-659.
    • (2013) Cell Mol Life Sci , vol.70 , pp. 631-659
    • Suzuki, T.1
  • 57
    • 84865017585 scopus 로고    scopus 로고
    • Intestinal permeability in coeliac disease: insight into mechanisms and relevance to pathogenesis
    • Heyman M, Abed J, Lebreton C, et al. Intestinal permeability in coeliac disease: insight into mechanisms and relevance to pathogenesis. Gut. 2012;61:1355-1364.
    • (2012) Gut , vol.61 , pp. 1355-1364
    • Heyman, M1    Abed, J2    Lebreton, C3
  • 58
    • 79952326609 scopus 로고    scopus 로고
    • Divergence of gut permeability and mucosal immune gene expression in two gluten-associated conditions: celiac disease and gluten sensitivity
    • Sapone A, Lammers KM, Casolaro V, et al. Divergence of gut permeability and mucosal immune gene expression in two gluten-associated conditions: celiac disease and gluten sensitivity. BMC Med. 2011;9:23-34.
    • (2011) BMC Med , vol.9 , pp. 23-34
    • Sapone, A1    Lammers, KM2    Casolaro, V3
  • 59
    • 79953892338 scopus 로고    scopus 로고
    • Synthetic surfactant food additives can cause intestinal barrier dysfunction
    • Csáki KF. Synthetic surfactant food additives can cause intestinal barrier dysfunction. Med Hypotheses. 2011;76:676-681.
    • (2011) Med Hypotheses , vol.76 , pp. 676-681
    • Csáki, KF.1
  • 60
    • 8444239269 scopus 로고    scopus 로고
    • Do surface-active lipids in food increase the intestinal permeability to toxic substances and allergenic agents?
    • llbäck NG, Nyblom M, Carlfors J, et al. Do surface-active lipids in food increase the intestinal permeability to toxic substances and allergenic agents? Med Hypotheses. 2004;63:724-730.
    • (2004) Med Hypotheses , vol.63 , pp. 724-730
    • llbäck, NG1    Nyblom, M2    Carlfors, J3
  • 61
    • 84875236506 scopus 로고    scopus 로고
    • Hypothesis: increased consumption of emulsifiers as an explanation for the rising incidence of Crohn's disease
    • Roberts CL, Rushworth SL, Richman E, et al. Hypothesis: increased consumption of emulsifiers as an explanation for the rising incidence of Crohn's disease. J Crohns Colitis. 2013;7:338-341.
    • (2013) J Crohns Colitis , vol.7 , pp. 338-341
    • Roberts, CL1    Rushworth, SL2    Richman, E3
  • 62
    • 0042834268 scopus 로고    scopus 로고
    • þ T cell transendothelial migration
    • þ T cell transendothelial migration. J Immunol. 2003;171:3179-3186.
    • (2003) J Immunol , vol.171 , pp. 3179-3186
    • Mohan, K1    Pinto, D2    Issekutz, B.3
  • 63
    • 0036073298 scopus 로고    scopus 로고
    • Histone cross-linking by transglutaminase
    • Kim JH, Nam KH, Kwon OS, et al. Histone cross-linking by transglutaminase. Biochem Biophys Res Commun. 2002;24:1453-1457.
    • (2002) Biochem Biophys Res Commun , vol.24 , pp. 1453-1457
    • Kim, JH1    Nam, KH2    Kwon, OS3
  • 64
    • 12444326818 scopus 로고    scopus 로고
    • Tissue transglutaminase-mediated formation and cleavage of histamine-gliadin complexes: biological effects and implications for celiac disease
    • Qiao S-W, Piper J, Haraldsen G, et al. Tissue transglutaminase-mediated formation and cleavage of histamine-gliadin complexes: biological effects and implications for celiac disease. J Immunol. 2005;174:1657-1663.
    • (2005) J Immunol , vol.174 , pp. 1657-1663
    • Qiao, S-W1    Piper, J2    Haraldsen, G3
  • 65
    • 0021712890 scopus 로고
    • Human mononuclear leukocyte transglutaminase activity is enhanced by streptococcal erythrogenic toxin and a staphylococcal mitogenic factor associated with toxic shock syndrome
    • Zettergren JG, Leifer MJ, Nakashima H, et al. Human mononuclear leukocyte transglutaminase activity is enhanced by streptococcal erythrogenic toxin and a staphylococcal mitogenic factor associated with toxic shock syndrome. Biochim Biophys Acta. 1984;802:385-389.
    • (1984) Biochim Biophys Acta , vol.802 , pp. 385-389
    • Zettergren, JG1    Leifer, MJ2    Nakashima, H3
  • 66
    • 79957624284 scopus 로고    scopus 로고
    • Immobilization of alkaline phosphatase on magnetic particles by site-specific and covalent cross-linking catalyzed by microbial transglutaminase
    • Moriyama K, Sung K, Goto M, et al. Immobilization of alkaline phosphatase on magnetic particles by site-specific and covalent cross-linking catalyzed by microbial transglutaminase. J Biosci Bioeng. 2011;111:650-653.
    • (2011) J Biosci Bioeng , vol.111 , pp. 650-653
    • Moriyama, K1    Sung, K2    Goto, M3
  • 67
    • 84865462532 scopus 로고    scopus 로고
    • Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides
    • Lebreton C, Menard S, Abed J, et al. Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides. Gastroenterology. 2012;143:698-707.
    • (2012) Gastroenterology , vol.143 , pp. 698-707
    • Lebreton, C1    Menard, S2    Abed, J3
  • 68
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: nature's biological glues
    • 1
    • Griffin M1, Casadio R, Bergamini CM. Transglutaminases: nature's biological glues. Biochem J. 2002;368:377-396.
    • (2002) Biochem J , vol.368 , pp. 377-396
    • Griffin, M1    Casadio, R2    Bergamini, CM.3
  • 69
    • 84906100336 scopus 로고    scopus 로고
    • Enzymes in Bakery: Current and Future Trends
    • I Muzzalupo, ed. Rijieka, Croatia: InTech
    • Miguel ASM, Martins-Meyer TS, Figueiredo EVDC, et al. Enzymes in Bakery: Current and Future Trends. In: I Muzzalupo, ed. Food Industry. Rijieka, Croatia: InTech; 2013:287-321. doi:10.5772/55834.
    • (2013) Food Industry , pp. 287-321
    • Miguel, ASM1    Martins-Meyer, TS2    Figueiredo, EVDC3
  • 70
    • 84896530100 scopus 로고    scopus 로고
    • Transglutaminase-based chemo-enzymatic conjugation approach yields homogeneous antibody-drug conjugates
    • Dennler P, Chiotellis A, Fischer E, et al. Transglutaminase-based chemo-enzymatic conjugation approach yields homogeneous antibody-drug conjugates. Bioconjug Chem. 2014;25:569-578.
    • (2014) Bioconjug Chem , vol.25 , pp. 569-578
    • Dennler, P1    Chiotellis, A2    Fischer, E3
  • 71
    • 84902117764 scopus 로고    scopus 로고
    • How T cells taste gluten in celiac disease
    • Jabri B, Chen X, Sollid LM. How T cells taste gluten in celiac disease. Nat Struct Mol Biol. 2014;21:429-431.
    • (2014) Nat Struct Mol Biol , vol.21 , pp. 429-431
    • Jabri, B1    Chen, X2    Sollid, LM.3
  • 72
    • 84881152184 scopus 로고    scopus 로고
    • Celiac disease and autoimmunity: review and controversies
    • Denham JM, Hill ID. Celiac disease and autoimmunity: review and controversies. Curr Allergy Asthma Rep. 2013;13:347-353.
    • (2013) Curr Allergy Asthma Rep , vol.13 , pp. 347-353
    • Denham, JM1    Hill, ID.2
  • 73
    • 84864613463 scopus 로고    scopus 로고
    • The incidence and risk of celiac disease in a healthy US adult population
    • Riddle MS, Murray JA, Porter CD. The incidence and risk of celiac disease in a healthy US adult population. Am J Gastroenterol. 2012;107:1248-1255.
    • (2012) Am J Gastroenterol , vol.107 , pp. 1248-1255
    • Riddle, MS1    Murray, JA2    Porter, CD.3
  • 74
    • 84885143794 scopus 로고    scopus 로고
    • The rising incidence of celiac disease in Scotland
    • White LE, Merrick VM, Bannerman E, et al. The rising incidence of celiac disease in Scotland. Pediatrics 2013;132:e924-e931. doi:10.1542/peds.2013-0932.
    • (2013) Pediatrics , vol.132 , pp. e924-e931
    • White, LE1    Merrick, VM2    Bannerman, E3
  • 75
    • 9844265402 scopus 로고    scopus 로고
    • High incidence and prevalence of adult coeliac disease. Augmented diagnostic approach
    • Collin P, Reunala T, Rasmussen M, et al. High incidence and prevalence of adult coeliac disease. Augmented diagnostic approach. Scand J Gastroenterol. 1997;32: 1129-1133.
    • (1997) Scand J Gastroenterol , vol.32 , pp. 1129-1133
    • Collin, P1    Reunala, T2    Rasmussen, M3
  • 76
    • 58449124695 scopus 로고    scopus 로고
    • Regional variation in celiac disease risk within Sweden revealed by the nationwide prospective incidence register
    • Olsson C, Stenlund H, Hörnell O, et al. Regional variation in celiac disease risk within Sweden revealed by the nationwide prospective incidence register. Acta Paediatr. 2009;98:337-342.
    • (2009) Acta Paediatr , vol.98 , pp. 337-342
    • Olsson, C1    Stenlund, H2    Hörnell, O3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.