메뉴 건너뛰기




Volumn 93, Issue 4, 2013, Pages 479-488

Selective inhibition of the gliadin-specific, cell-mediated immune response by transamidation with microbial transglutaminase

Author keywords

Celiac disease; Enterocytes; T lymphocytes

Indexed keywords

CASPASE 3; GAMMA INTERFERON; GLIADIN; GLUTEN; INTERLEUKIN 10; MESSENGER RNA; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 84875661766     PISSN: 07415400     EISSN: 19383673     Source Type: Journal    
DOI: 10.1189/jlb.0412182     Document Type: Article
Times cited : (33)

References (44)
  • 1
    • 64949090387 scopus 로고    scopus 로고
    • Coeliac disease
    • Di Sabatino, A., Corazza, G. R. (2009) Coeliac disease. Lancet 373, 1480-1493.
    • (2009) Lancet , vol.373 , pp. 1480-1493
    • Di Sabatino, A.1    Corazza, G.R.2
  • 5
    • 2142650113 scopus 로고    scopus 로고
    • Effect of a gluten-free diet on gastrointestinal symptoms in celiac disease
    • Murray, J. A., Watson, T., Clearman, B., Mitros, F. (2004) Effect of a gluten-free diet on gastrointestinal symptoms in celiac disease. Am. J. Clin. Nutr. 79, 669-673.
    • (2004) Am. J. Clin. Nutr. , vol.79 , pp. 669-673
    • Murray, J.A.1    Watson, T.2    Clearman, B.3    Mitros, F.4
  • 9
    • 7444226234 scopus 로고    scopus 로고
    • Comparative biochemical analysis of three bacterial prolyl endopeptidases: Implications for coeliac sprue
    • Shan, L., Marti, T., Sollid, L. M., Gray, G. M., Khosla, C. (2004) Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem. J. 383, 311-318.
    • (2004) Biochem. J. , vol.383 , pp. 311-318
    • Shan, L.1    Marti, T.2    Sollid, L.M.3    Gray, G.M.4    Khosla, C.5
  • 10
    • 33846962165 scopus 로고    scopus 로고
    • Oral proteases: A new approach to managing coeliac disease
    • Cerf-Bensussan, N., Matysiak-Budnik, T., Cellier, C., Heyman, M. (2007) Oral proteases: a new approach to managing coeliac disease. Gut 56, 157-160.
    • (2007) Gut , vol.56 , pp. 157-160
    • Cerf-Bensussan, N.1    Matysiak-Budnik, T.2    Cellier, C.3    Heyman, M.4
  • 13
    • 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. (1993) Primary structure of microbial transglutaminase from Streptoverticillium sp. Strain s-8112. J. Biol. Chem. 668, 11565-11572.
    • (1993) J. Biol. Chem. , vol.668 , pp. 11565-11572
    • Kanaji, T.1    Ozaki, H.2    Takao, T.3    Kawajiri, H.4    Ide, H.5    Motoki, M.6    Shimonishi, Y.7
  • 14
    • 2442610049 scopus 로고    scopus 로고
    • Properties and applications of microbial transglutaminase
    • Yokoyama, K., Nio, N., Kikuchi, Y. (2004) Properties and applications of microbial transglutaminase. Appl. Microbiol. Biotechnol. 64, 447-454.
    • (2004) Appl. Microbiol. Biotechnol. , vol.64 , pp. 447-454
    • Yokoyama, K.1    Nio, N.2    Kikuchi, Y.3
  • 17
    • 0000398463 scopus 로고
    • RP-HPLC and capillary electrophoresis of subunits from glutenin isolated by SDS and osborne fractionation
    • Weegels, P. L., Hamer, R. J., Schofield, J. D. (1995) RP-HPLC and capillary electrophoresis of subunits from glutenin isolated by SDS and osborne fractionation. J. Cereal Sci. 22, 211-224.
    • (1995) J. Cereal Sci. , vol.22 , pp. 211-224
    • Weegels, P.L.1    Hamer, R.J.2    Schofield, J.D.3
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 0016481865 scopus 로고
    • Direct estimation of lysine in corn meals by the ninhydrin color reaction
    • Beckwith, A. C., Paulis, J. W., Wall, J. S. (1975) Direct estimation of lysine in corn meals by the ninhydrin color reaction. J. Agr. Food Chem. 23, 194-196.
    • (1975) J. Agr. Food Chem. , vol.23 , pp. 194-196
    • Beckwith, A.C.1    Paulis, J.W.2    Wall, J.S.3
  • 20
    • 34249877687 scopus 로고    scopus 로고
    • Phase 2 enzymes induction by conjugated linoleic acid improves lupus-associated oxidative stress
    • Bergamo, P., Maurano, F., Rossi, M. (2007) Phase 2 enzymes induction by conjugated linoleic acid improves lupus-associated oxidative stress. Free Radic. Biol. Med. 43, 71-79.
    • (2007) Free Radic. Biol. Med. , vol.43 , pp. 71-79
    • Bergamo, P.1    Maurano, F.2    Rossi, M.3
  • 21
    • 0033364256 scopus 로고    scopus 로고
    • The histopathology of coeliac disease: Time for a standardized report scheme for pathologists
    • Oberhuber, G., Granditsch, G., Vogelsang, H. (1999) The histopathology of coeliac disease: time for a standardized report scheme for pathologists. Eur. J. Gastroenterol. Hepatol. 11, 1185-1194.
    • (1999) Eur. J. Gastroenterol. Hepatol. , vol.11 , pp. 1185-1194
    • Oberhuber, G.1    Granditsch, G.2    Vogelsang, H.3
  • 24
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using real-time quantitative PCR and the 2γ+CT method
    • Livak, K. J., Schmittgen, T. D. (2001) Analysis of relative gene expression data using real-time quantitative PCR and the 2γ+CT method. Methods 25, 402-428.
    • (2001) Methods , vol.25 , pp. 402-428
    • Livak, K.J.1    Schmittgen, T.D.2
  • 26
    • 2542588613 scopus 로고    scopus 로고
    • Direct gliadin cytotoxicity as a cofactor in the pathogenesis of celiac disease
    • Elli, L., Dolfini, E., Bardella, M. T. (2004) Direct gliadin cytotoxicity as a cofactor in the pathogenesis of celiac disease. Int. Arch. Allergy Immunol. 134, 88.
    • (2004) Int. Arch. Allergy Immunol. , vol.134 , pp. 88
    • Elli, L.1    Dolfini, E.2    Bardella, M.T.3
  • 29
    • 0035019083 scopus 로고    scopus 로고
    • T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase
    • Molberg, O., McAdam, S., Lundin, K. E., Kristiansen, C., Arentz-Hansen, H., Kett, K., Sollid, L. M. (2001) T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase. Eur. J. Immunol. 31, 1317-1323.
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1317-1323
    • Molberg, O.1    McAdam, S.2    Lundin, K.E.3    Kristiansen, C.4    Arentz-Hansen, H.5    Kett, K.6    Sollid, L.M.7
  • 30
    • 0021969767 scopus 로고
    • Human jejunal transglutaminase: Demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease
    • Bruce, S. E., Bjarnason, I., Peters, T. J. (1985) Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease. Clin. Sci. (Lond). 68, 573-579.
    • (1985) Clin. Sci. (Lond). , vol.68 , pp. 573-579
    • Bruce, S.E.1    Bjarnason, I.2    Peters, T.J.3
  • 31
    • 2342424238 scopus 로고    scopus 로고
    • Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides
    • Fleckenstein, B., Qiao, S. W., Larsen, M. R., Jung, G., Roepstorff, P., Sollid, L. M. (2004) Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides. J. Biol. Chem. 279, 17607-17616.
    • (2004) J. Biol. Chem. , vol.279 , pp. 17607-17616
    • Fleckenstein, B.1    Qiao, S.W.2    Larsen, M.R.3    Jung, G.4    Roepstorff, P.5    Sollid, L.M.6
  • 35
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: Dissecting a complex inflammatory disorder
    • Sollid, L. M. (2002) Coeliac disease: dissecting a complex inflammatory disorder. Nat. Rev. Immunol. 9, 647-655.
    • (2002) Nat. Rev. Immunol. , vol.9 , pp. 647-655
    • Sollid, L.M.1
  • 36
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • Wieser, H. (2007) Chemistry of gluten proteins. Food Microbiol. 24, 115-119.
    • (2007) Food Microbiol. , vol.24 , pp. 115-119
    • Wieser, H.1
  • 38
    • 0034234573 scopus 로고    scopus 로고
    • IL-10 gene expression is controlled by the transcription factors Sp1 and Sp3
    • Tone, M., Powell, M. J., Tone, Y., Thompson, S. A., Waldmann, H. (2000) IL-10 gene expression is controlled by the transcription factors Sp1 and Sp3. J. Immunol. 165, 286-291.
    • (2000) J. Immunol. , vol.165 , pp. 286-291
    • Tone, M.1    Powell, M.J.2    Tone, Y.3    Thompson, S.A.4    Waldmann, H.5
  • 39
    • 40949102111 scopus 로고    scopus 로고
    • Post-transcriptional control of cytokine production
    • Anderson, P. (2008) Post-transcriptional control of cytokine production. Nat. Immunol. 9, 353-359.
    • (2008) Nat. Immunol. , vol.9 , pp. 353-359
    • Anderson, P.1
  • 40
    • 34249678457 scopus 로고    scopus 로고
    • TH1 cells control themselves by producing interleukin-10
    • O'Garra, A., Vieira, P. (2007) TH1 cells control themselves by producing interleukin-10. Nat. Rev. Immunol. 7, 425-428.
    • (2007) Nat. Rev. Immunol. , vol.7 , pp. 425-428
    • O'Garra, A.1    Vieira, P.2
  • 43
    • 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. (2008) The propensity for deamidation and transamidation of peptides by transglutaminase 2 is dependent on substrate affinity and reaction conditions. Biochim. Biophys. Acta 1784, 1804-1811.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 1804-1811
    • Stamnaes, J.1    Fleckenstein, B.2    Sollid, L.M.3
  • 44
    • 0026317501 scopus 로고
    • Clonal analysis of sucrase-isomaltase expression in the human colon adenocarcinoma Caco-2 cells
    • Beaulieu, J-F., Quaroni, A. (1991) Clonal analysis of sucrase-isomaltase expression in the human colon adenocarcinoma Caco-2 cells. Biochem. J. 280, 599-608.
    • (1991) Biochem. J. , vol.280 , pp. 599-608
    • Beaulieu, J.-F.1    Quaroni, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.