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Volumn 62, Issue 30, 2014, Pages 7604-7611

Microbial transglutaminase treatment in pasta-production does not affect the immunoreactivity of gliadin with celiac disease patients' sera

Author keywords

celiac disease; gliadin; microbial transglutaminase; pasta

Indexed keywords

AMINO ACIDS; DISEASES; PATIENT TREATMENT;

EID: 84905284806     PISSN: 00218561     EISSN: 15205118     Source Type: Journal    
DOI: 10.1021/jf501275c     Document Type: Article
Times cited : (19)

References (41)
  • 1
    • 84866077437 scopus 로고    scopus 로고
    • Epidemiology and clinical presentations of celiac disease
    • Reilly, N. R.; Green, P. H. R. Epidemiology and clinical presentations of celiac disease Semin. Immunopathol. 2012, 34, 473-478
    • (2012) Semin. Immunopathol. , vol.34 , pp. 473-478
    • Reilly, N.R.1    Green, P.H.R.2
  • 3
    • 70649092298 scopus 로고    scopus 로고
    • Celiac disease: From pathogenesis to novel therapies
    • Schuppan, D.; Junker, Y.; Barisani, D. Celiac disease: from pathogenesis to novel therapies Gastroenterology 2009, 137, 1912-1933
    • (2009) Gastroenterology , vol.137 , pp. 1912-1933
    • Schuppan, D.1    Junker, Y.2    Barisani, D.3
  • 6
    • 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, L. M. 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, J.1    Fleckenstein, B.2    Sollid, L.M.3
  • 9
    • 0034771195 scopus 로고    scopus 로고
    • Celiac disease: Antibody recognition against native and selectively deamidated gliadin peptides
    • Aleanzi, M.; Demonte, A. M.; Esper, C.; Garcilazo, S.; Waggener, M. Celiac disease: Antibody recognition against native and selectively deamidated gliadin peptides Clin. Chem. 2001, 47, 2023-2208
    • (2001) Clin. Chem. , vol.47 , pp. 2023-2208
    • Aleanzi, M.1    Demonte, A.M.2    Esper, C.3    Garcilazo, S.4    Waggener, M.5
  • 10
    • 16244399156 scopus 로고    scopus 로고
    • What are the sensitivity and specificity of serologic tests for celiac disease? Do sensitivity and specificity vary in different populations?
    • Hill, I. D. What are the sensitivity and specificity of serologic tests for celiac disease? Do sensitivity and specificity vary in different populations? Gastroenterology 2005, 128, S25-S32
    • (2005) Gastroenterology , vol.128
    • Hill, I.D.1
  • 11
    • 84856610721 scopus 로고    scopus 로고
    • Contribution of celiac disease autoantibodies to the disease process
    • Lindfors, K.; Kaukinen, K. Contribution of celiac disease autoantibodies to the disease process Exp. Rev. Clin. Immunol 2012, 8, 151-154
    • (2012) Exp. Rev. Clin. Immunol , vol.8 , pp. 151-154
    • Lindfors, K.1    Kaukinen, K.2
  • 12
    • 77956191748 scopus 로고    scopus 로고
    • Transglutaminase 2-targeted autoantibodies in celiac disease: Pathogenetic players in addition to diagnostic tools?
    • Lindfors, K.; Mäki, M.; Kaukinen, K. Transglutaminase 2-targeted autoantibodies in celiac disease: Pathogenetic players in addition to diagnostic tools? Autoimmun. Rev. 2010, 9, 744-749
    • (2010) Autoimmun. Rev. , vol.9 , pp. 744-749
    • Lindfors, K.1    Mäki, M.2    Kaukinen, K.3
  • 13
    • 84859630491 scopus 로고    scopus 로고
    • Autoantibodies from patients with celiac disease inhibit transglutaminase 2 binding to heparin/heparan sulfate and interfere with intestinal epithelial cell adhesion
    • Teesalu, K.; Panarina, M.; Uibo, O.; Uibo, R.; Utt, M. Autoantibodies from patients with celiac disease inhibit transglutaminase 2 binding to heparin/heparan sulfate and interfere with intestinal epithelial cell adhesion Amino Acids 2012, 42, 1055-1064
    • (2012) Amino Acids , vol.42 , pp. 1055-1064
    • Teesalu, K.1    Panarina, M.2    Uibo, O.3    Uibo, R.4    Utt, M.5
  • 15
    • 0027223075 scopus 로고
    • Primary structure of microbial transglutaminase from Streptoverticillium sp. Strain s-8112
    • Kanaji, T.; Ozaki, H.; Takao, T.; Kawajiri, H.; Ide, H.; Motoki, M.; Shimonishi, Y. Primary structure of microbial transglutaminase from Streptoverticillium sp. Strain s-8112 J. Biol. Chem. 1993, 268, 11565-11572
    • (1993) J. Biol. Chem. , vol.268 , pp. 11565-11572
    • Kanaji, T.1    Ozaki, H.2    Takao, T.3    Kawajiri, H.4    Ide, H.5    Motoki, M.6    Shimonishi, Y.7
  • 16
    • 0035531318 scopus 로고    scopus 로고
    • Transglutaminase: Its utilization in the food industry
    • Kuraishi, C.; Yamazaki, K.; Susa, Y. Transglutaminase: Its utilization in the food industry Food Rev. Int. 2001, 17, 221-2456
    • (2001) Food Rev. Int. , vol.17 , pp. 221-2456
    • Kuraishi, C.1    Yamazaki, K.2    Susa, Y.3
  • 17
    • 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. (Praha). 2014, 59, 241-250
    • (2014) Folia Microbiol. (Praha). , vol.59 , pp. 241-250
    • Kieliszek, M.1    Misiewicz, A.2
  • 20
  • 21
    • 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.; Sjöström, H. Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease Biochim. Biophys. Acta 2004, 1690, 220-230
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 220-230
    • Skovbjerg, H.1    Koch, C.2    Anthonsen, D.3    Sjöström, H.4
  • 24
    • 84905286099 scopus 로고    scopus 로고
    • Bundesinstitut für Risikobewertung. Transglutaminase in Fleischerzeugnissen.
    • Bundesinstitut für Risikobewertung. Transglutaminase in Fleischerzeugnissen. 2011, 52, 1-6.
    • (2011) , vol.52 , pp. 1-6
  • 25
    • 40549118791 scopus 로고    scopus 로고
    • Transglutaminase treatment of wheat and maize prolamins of bread increases the serum IgA reactivity of celiac disease patients
    • Cabrera-Chávez, F.; Rouzaud-Sández, O.; Sotelo-Cruz, N.; Calderón de la Barca, A. M. Transglutaminase treatment of wheat and maize prolamins of bread increases 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, F.1    Rouzaud-Sández, O.2    Sotelo-Cruz, N.3    Calderón De La Barca, A.M.4
  • 26
    • 66149145935 scopus 로고    scopus 로고
    • Bovine milk caseins and transglutaminase-treated cereal prolamins are differentially recognized by IgA of celiac disease patients according to their age
    • Cabrera-Chávez, F.; Rouzaud-Sández, O.; Sotelo-Cruz, N.; Calderón de la Barca, A. M. Bovine milk caseins and transglutaminase-treated cereal prolamins are differentially recognized by IgA of celiac disease patients according to their age J. Agric. Food Chem. 2009, 57, 3754-3759
    • (2009) J. Agric. Food Chem. , vol.57 , pp. 3754-3759
    • Cabrera-Chávez, F.1    Rouzaud-Sández, O.2    Sotelo-Cruz, N.3    Calderón De La Barca, A.M.4
  • 28
    • 84890081865 scopus 로고    scopus 로고
    • 7 th ed. The Ministry of Health and Welfare Reproduced by Japan Food Additives Association: Tokyo, Japan
    • Japan's Specifications and Standards for Food Additives, 7 th ed.; The Ministry of Health and Welfare Reproduced by Japan Food Additives Association: Tokyo, Japan; pp 19-35.
    • Japan's Specifications and Standards for Food Additives , pp. 19-35
  • 29
    • 84893758056 scopus 로고
    • Formation of ε-(γ-glutamyl)lysine cross-link in cured horse mackerel meat induced by drying
    • Kumazawa, Y.; Seguro, K.; Takamura, M.; Motoki, M. Formation of ε-(γ-glutamyl)lysine cross-link in cured horse mackerel meat induced by drying J. Food Sci. 1993, 58, 1062-1064
    • (1993) J. Food Sci. , vol.58 , pp. 1062-1064
    • Kumazawa, Y.1    Seguro, K.2    Takamura, M.3    Motoki, M.4
  • 30
    • 0031696005 scopus 로고    scopus 로고
    • Quantitative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography
    • Wieser, H.; Antes, S.; Seilmeier, W. Quantitative determination of gluten protein types in wheat flour by reversed-phase high-performance liquid chromatography Cereal Chem. 1998, 75, 644-650
    • (1998) Cereal Chem. , vol.75 , pp. 644-650
    • Wieser, H.1    Antes, S.2    Seilmeier, W.3
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 1970, 227, 508-585
    • (1970) Nature , vol.227 , pp. 508-585
    • Laemmli, U.K.1
  • 32
    • 84988074679 scopus 로고
    • Improved silver staining of plant protein, RNA & DNA in PAA gels
    • Blum, H.; Beier, H.; G, H. J. Improved silver staining of plant protein, RNA & DNA in PAA gels Electrophoresis 1987, 8, 93-99
    • (1987) Electrophoresis , vol.8 , pp. 93-99
    • Blum, H.1    Beier, H.2
  • 33
    • 0028139777 scopus 로고
    • Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions
    • Sakamoto, H.; Kumazawa, Y.; Motoki, M. Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions J. Food Sci. 1994, 59, 866-871
    • (1994) J. Food Sci. , vol.59 , pp. 866-871
    • Sakamoto, H.1    Kumazawa, Y.2    Motoki, M.3
  • 34
    • 84986465415 scopus 로고
    • Gel strength enhancement by addition of microbial transglutaminase during onshore Surimi manutacture
    • Sakamoto, H.; Kumazawa, Y.; Toiguchi, S.; Seguro, K.; Soeda, T.; Motoki, M. Gel strength enhancement by addition of microbial transglutaminase during onshore Surimi manutacture J. Food Sci. 1995, 60, 300-304
    • (1995) J. Food Sci. , vol.60 , pp. 300-304
    • Sakamoto, H.1    Kumazawa, Y.2    Toiguchi, S.3    Seguro, K.4    Soeda, T.5    Motoki, M.6
  • 36
    • 0036751964 scopus 로고    scopus 로고
    • Effects of tranglutaminse on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends
    • Basman, A.; Köksel, H.; NG, P. K. W. Effects of tranglutaminse on SDS-PAGE patterns of wheat, soy, and barley proteins and their blends J. Food Sci. 2002, 67, 2654-2658
    • (2002) J. Food Sci. , vol.67 , pp. 2654-2658
    • Basman, A.1    Köksel, H.2    Ng, P.K.W.3
  • 37
    • 65249091991 scopus 로고    scopus 로고
    • A quantitative analysis of transglutaminase 2-mediated deamidation of gluten peptides: Implications for the T-cell response in celiac disease
    • Dørum, S.; Qiao, S.-W.; Sollid, L. M.; Fleckenstein, B. A quantitative analysis of transglutaminase 2-mediated deamidation of gluten peptides: Implications for the T-cell response in celiac disease J. Proteome Res. 2009, 8, 1748-1755
    • (2009) J. Proteome Res. , vol.8 , pp. 1748-1755
    • Dørum, S.1    Qiao, S.-W.2    Sollid, L.M.3    Fleckenstein, B.4
  • 39
    • 65649142511 scopus 로고    scopus 로고
    • Correlation analysis of celiac sprue tissue transglutaminase and deamidated gliadin IgG/IgA
    • Marietta, E.-V.; Rashtak, S.; Murray, J. A. Correlation analysis of celiac sprue tissue transglutaminase and deamidated gliadin IgG/IgA World J. Gastroenterol. 2009, 15, 845-848
    • (2009) World J. Gastroenterol. , vol.15 , pp. 845-848
    • Marietta, E.-V.1    Rashtak, S.2    Murray, J.A.3
  • 41
    • 84877576026 scopus 로고    scopus 로고
    • American college of gastroenterology clinical guideline: Diagnosis and management of celiac disease
    • Rubio-Tapia, A.; Hill, I. D.; Kelly, C. P.; Calderwood, A. H.; Murray, J. A. American college of gastroenterology clinical guideline: Diagnosis and management of celiac disease Am. J. Gastroenterol. 2013, 108, 656-677
    • (2013) Am. J. Gastroenterol. , vol.108 , pp. 656-677
    • Rubio-Tapia, A.1    Hill, I.D.2    Kelly, C.P.3    Calderwood, A.H.4    Murray, J.A.5


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