메뉴 건너뛰기




Volumn 1690, Issue 3, 2004, Pages 220-230

Deamidation and cross-linking of gliadin peptides by transglutaminases and the relation to celiac disease

Author keywords

Celiac disease; Cross linking; Deamidation; Gliadin peptide; Mucosal protein; Transglutaminase

Indexed keywords

AMINE; EPITOPE; GLIADIN; MONOCLONAL ANTIBODY; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 7044233640     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2004.06.009     Document Type: Article
Times cited : (66)

References (40)
  • 2
    • 0034121187 scopus 로고    scopus 로고
    • Molecular basis of celiac disease
    • L.M. Sollid Molecular basis of celiac disease Annu. Rev. Immunol. 18 2000 53 81
    • (2000) Annu. Rev. Immunol. , vol.18 , pp. 53-81
    • Sollid, L.M.1
  • 4
    • 0034066695 scopus 로고    scopus 로고
    • In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope
    • R.P. Anderson, P. Degano, A.J. Godkin, D.P. Jewell, and A.V. Hill In vivo antigen challenge in celiac disease identifies a single transglutaminase- modified peptide as the dominant A-gliadin T-cell epitope Nat. Med. 6 2000 337 342
    • (2000) Nat. Med. , vol.6 , pp. 337-342
    • Anderson, R.P.1    Degano, P.2    Godkin, A.J.3    Jewell, D.P.4    Hill, A.V.5
  • 11
    • 0032528813 scopus 로고    scopus 로고
    • Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • Y. van de Wal, Y. Kooy, P. van Veelen, S. Pena, L. Mearin, G. Papadopoulos, and F. Koning Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity J. Immunol. 161 1998 1585 1588
    • (1998) J. Immunol. , vol.161 , pp. 1585-1588
    • Van De Wal, Y.1    Kooy, Y.2    Van Veelen, P.3    Pena, S.4    Mearin, L.5    Papadopoulos, G.6    Koning, F.7
  • 12
    • 0035019083 scopus 로고    scopus 로고
    • T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase
    • Ø. Molberg, S. McAdam, K.E. Lundin, C. Kristiansen, E.H. Arentz-Hansen, K. Kett, and L.M. Sollid T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase Eur. J. Immunol. 31 2001 1317 1323
    • (2001) Eur. J. Immunol. , vol.31 , pp. 1317-1323
    • Molberg Ø1    McAdam, S.2    Lundin, K.E.3    Kristiansen, C.4    Arentz-Hansen, E.H.5    Kett, K.6    Sollid, L.M.7
  • 13
    • 2342424238 scopus 로고    scopus 로고
    • Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides
    • B. Fleckenstein, S.W. Qiao, M.R. Larsen, G. Jung, P. Roepstorff, and L.M. Sollid Molecular characterization of covalent complexes between tissue transglutaminase and gliadin peptides J. Biol. Chem. 279 2004 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
  • 14
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for celiac sprue
    • J.L. Piper, G.M. Gray, and C. Khosla High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: implications for celiac sprue Biochemistry 41 2002 386 393
    • (2002) Biochemistry , vol.41 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 16
    • 0036901574 scopus 로고    scopus 로고
    • Transglutaminases: Nature's biological glues
    • M. Griffin, R. Casadio, and C.M. Bergamini Transglutaminases: nature's biological glues Biochem. J. 368 2002 377 396
    • (2002) Biochem. J. , vol.368 , pp. 377-396
    • Griffin, M.1    Casadio, R.2    Bergamini, C.M.3
  • 17
    • 0031438699 scopus 로고    scopus 로고
    • Autoantibodies in coeliac disease: Tissue transglutaminase-guilt by association?
    • L.M. Sollid, O. Molberg, S. McAdam, and K.E. Lundin Autoantibodies in coeliac disease: tissue transglutaminase-guilt by association? Gut 41 1997 851 852
    • (1997) Gut , vol.41 , pp. 851-852
    • Sollid, L.M.1    Molberg, O.2    McAdam, S.3    Lundin, K.E.4
  • 19
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • G. Köhler, and C. Milstein Continuous cultures of fused cells secreting antibody of predefined specificity Nature 256 1975 495 497
    • (1975) Nature , vol.256 , pp. 495-497
    • Köhler, G.1    Milstein, C.2
  • 20
    • 0020327743 scopus 로고
    • Theory and methods for immunization in culture and monoclonal antibody production
    • C.L. Reading Theory and methods for immunization in culture and monoclonal antibody production J. Immunol. Methods 53 1982 261 291
    • (1982) J. Immunol. Methods , vol.53 , pp. 261-291
    • Reading, C.L.1
  • 21
    • 0014737384 scopus 로고
    • Determination of submicro quantities of ammonia
    • A. Levitzki Determination of submicro quantities of ammonia Anal. Biochem. 33 1970 335 340
    • (1970) Anal. Biochem. , vol.33 , pp. 335-340
    • Levitzki, A.1
  • 22
    • 0035988899 scopus 로고    scopus 로고
    • Gliadin is a good substrate of several transglutaminases: Possible implication in the pathogenesis of coeliac disease
    • H. Skovbjerg, O. Norén, D. Anthonsen, J. Moller, and H. Sjöström Gliadin is a good substrate of several transglutaminases: possible implication in the pathogenesis of coeliac disease Scand. J. Gastroenterol. 37 2002 812 817
    • (2002) Scand. J. Gastroenterol. , vol.37 , pp. 812-817
    • Skovbjerg, H.1    Norén, O.2    Anthonsen, D.3    Moller, J.4    Sjöström, H.5
  • 23
    • 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 reactions
    • B. Fleckenstein, O. Molberg, S.W. Qiao, D.G. Schmid, F. von der Mulbe, K. Elgstoen, G. Jung, and L.M. Sollid Gliadin T cell epitope selection by tissue transglutaminase in celiac disease. Role of enzyme specificity and pH influence on the transamidation versus deamidation reactions J. Biol. Chem. 277 2002 34109 34116
    • (2002) J. Biol. Chem. , vol.277 , pp. 34109-34116
    • Fleckenstein, B.1    Molberg, O.2    Qiao, S.W.3    Schmid, D.G.4    Von Der Mulbe, F.5    Elgstoen, K.6    Jung, G.7    Sollid, L.M.8
  • 25
    • 0021969767 scopus 로고
    • Human jejunal transglutaminase: Demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease
    • S.E. Bruce, I. Bjarnason, and T.J. Peters Human jejunal transglutaminase: demonstration of activity, enzyme kinetics and substrate specificity with special relation to gliadin and coeliac disease Clin. Sci. 68 1985 573 579
    • (1985) Clin. Sci. , vol.68 , pp. 573-579
    • Bruce, S.E.1    Bjarnason, I.2    Peters, T.J.3
  • 26
    • 0031916924 scopus 로고    scopus 로고
    • Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig
    • C.F. Deacon, T.E. Hughes, and J.J. Holst Dipeptidyl peptidase IV inhibition potentiates the insulinotropic effect of glucagon-like peptide 1 in the anesthetized pig Diabetes 47 1998 764 769
    • (1998) Diabetes , vol.47 , pp. 764-769
    • Deacon, C.F.1    Hughes, T.E.2    Holst, J.J.3
  • 27
    • 85006173213 scopus 로고
    • Purification and characterization of a tissue-type transglutaminase from red sea bream (Pagrus major)
    • H. Yasueda, Y. Kumazawa, and M. Motoki Purification and characterization of a tissue-type transglutaminase from red sea bream (Pagrus major) Biosci. Biotechnol. Biochem. 58 1994 2041 2045
    • (1994) Biosci. Biotechnol. Biochem. , vol.58 , pp. 2041-2045
    • Yasueda, H.1    Kumazawa, Y.2    Motoki, M.3
  • 29
    • 0032948280 scopus 로고    scopus 로고
    • Anti-tissue transglutaminase, anti-endomysium and anti-R1-reticulin autoantibodies-the antibody trinity of coeliac disease
    • R.J. Lock, J.E. Gilmour, and D.J. Unsworth Anti-tissue transglutaminase, anti-endomysium and anti-R1-reticulin autoantibodies-the antibody trinity of coeliac disease Clin. Exp. Immunol. 116 1999 258 262
    • (1999) Clin. Exp. Immunol. , vol.116 , pp. 258-262
    • Lock, R.J.1    Gilmour, J.E.2    Unsworth, D.J.3
  • 33
    • 0035424309 scopus 로고    scopus 로고
    • Post-translational protein modifications in antigen recognition and autoimmunity
    • H.A. Doyle, and M.J. Mamula Post-translational protein modifications in antigen recognition and autoimmunity Trends Immunol. 22 2001 443 449
    • (2001) Trends Immunol. , vol.22 , pp. 443-449
    • Doyle, H.A.1    Mamula, M.J.2
  • 34
    • 0032806274 scopus 로고    scopus 로고
    • Duration of exposure to gluten and risk for autoimmune disorders in patients with celiac disease. SIGEP Study Group for Autoimmune Disorders in Celiac Disease
    • A. Ventura, G. Magazzu, and L. Greco Duration of exposure to gluten and risk for autoimmune disorders in patients with celiac disease. SIGEP Study Group for Autoimmune Disorders in Celiac Disease Gastroenterology 117 1999 297 303
    • (1999) Gastroenterology , vol.117 , pp. 297-303
    • Ventura, A.1    Magazzu, G.2    Greco, L.3
  • 35
    • 0034823195 scopus 로고    scopus 로고
    • Duration of gluten exposure in adult coeliac disease does not correlate with the risk for autoimmune disorders
    • G.C. Sategna, E. Solerio, N. Scaglione, G. Aimo, and G. Mengozzi Duration of gluten exposure in adult coeliac disease does not correlate with the risk for autoimmune disorders Gut 49 2001 502 505
    • (2001) Gut , vol.49 , pp. 502-505
    • Sategna, G.C.1    Solerio, E.2    Scaglione, N.3    Aimo, G.4    Mengozzi, G.5
  • 36
    • 0141593569 scopus 로고    scopus 로고
    • Early infant feeding and risk of developing type 1 diabetes-associated autoantibodies
    • A.G. Ziegler, S. Schmied, D. Huber, M. Hummel, and E. Bonifacio Early infant feeding and risk of developing type 1 diabetes-associated autoantibodies JAMA 290 2003 1721 1728
    • (2003) JAMA , vol.290 , pp. 1721-1728
    • Ziegler, A.G.1    Schmied, S.2    Huber, D.3    Hummel, M.4    Bonifacio, E.5
  • 37
    • 0036399648 scopus 로고    scopus 로고
    • Regression of autoimmunity and abnormal glucose homeostasis in an adolescent boy with silent coeliac disease
    • P. Banin, R. Perretta, E. Ravaioli, V. De Sanctis, and V Regression of autoimmunity and abnormal glucose homeostasis in an adolescent boy with silent coeliac disease Acta Paediatr. 91 2002 1141 1143
    • (2002) Acta Paediatr. , vol.91 , pp. 1141-1143
    • Banin, P.1    Perretta, R.2    Ravaioli, E.3    De Sanctis, V.4
  • 39
    • 0036186436 scopus 로고    scopus 로고
    • Coeliac disease and secondary autoimmunity
    • D. Schuppan, and R. Ciccocioppo Coeliac disease and secondary autoimmunity Dig. Liver Dis. 34 2002 13 15
    • (2002) Dig. Liver Dis. , vol.34 , pp. 13-15
    • Schuppan, D.1    Ciccocioppo, R.2
  • 40
    • 0031863698 scopus 로고    scopus 로고
    • Posttranslational protein modifications, apoptosis, and the bypass of tolerance to autoantigens
    • P.J. Utz, and P. Anderson Posttranslational protein modifications, apoptosis, and the bypass of tolerance to autoantigens Arthritis Rheum. 41 1998 1152 1160
    • (1998) Arthritis Rheum. , vol.41 , pp. 1152-1160
    • Utz, P.J.1    Anderson, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.