메뉴 건너뛰기




Volumn 190, Issue 12, 2013, Pages 5981-5991

Transglutaminase 2-specific autoantibodies in celiac disease target clustered, N-terminal epitopes not displayed on the surface of cells

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; EPITOPE; FIBRONECTIN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2;

EID: 84879108452     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1300183     Document Type: Article
Times cited : (68)

References (48)
  • 1
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • DOI 10.1038/nm0797-797
    • Dieterich, W., T. Ehnis, M. Bauer, P. Donner, U. Volta, E. O. Riecken, and D. Schuppan. 1997. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nat. Med. 3: 797-801. (Pubitemid 27298728)
    • (1997) Nature Medicine , vol.3 , Issue.7 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2    Bauer, M.3    Donner, P.4    Volta, U.5    Riecken, E.O.6    Schuppan, D.7
  • 3
    • 77957724427 scopus 로고    scopus 로고
    • Update on serologic testing in celiac disease
    • Leffler, D. A., and D. Schuppan. 2010. Update on serologic testing in celiac disease. Am. J. Gastroenterol. 105: 2520-2524.
    • (2010) Am. J. Gastroenterol. , vol.105 , pp. 2520-2524
    • Leffler, D.A.1    Schuppan, D.2
  • 4
    • 84855414559 scopus 로고    scopus 로고
    • European Society for Pediatric Gastroenterology, Hepatology, and Nutrition guidelines for the diagnosis of coeliac disease
    • ESPGHAN Working Group on Coeliac Disease Diagnosis; ESPGHAN Gastroenterology Committee; European Society for Pediatric Gastroenterology, Hepatology, and Nutrition
    • Husby, S., S. Koletzko, I. R. Korponay-Szabó, M. L. Mearin, A. Phillips, R. Shamir, R. Troncone, K. Giersiepen, D. Branski, C. Catassi, et al ESPGHAN Working Group on Coeliac Disease Diagnosis; ESPGHAN Gastroenterology Committee; European Society for Pediatric Gastroenterology, Hepatology, and Nutrition. 2012. European Society for Pediatric Gastroenterology, Hepatology, and Nutrition guidelines for the diagnosis of coeliac disease. J. Pediatr. Gastroenterol. Nutr. 54: 136-160.
    • (2012) J. Pediatr. Gastroenterol. Nutr. , vol.54 , pp. 136-160
    • Husby, S.1    Koletzko, S.2    Korponay-Szabó, I.R.3    Mearin, M.L.4    Phillips, A.5    Shamir, R.6    Troncone, R.7    Giersiepen, K.8    Branski, D.9    Catassi, C.10
  • 6
    • 0032528813 scopus 로고    scopus 로고
    • Cutting edge: Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • van deWal, Y., Y. Kooy, P. van Veelen, S. Peña, L. Mearin, G. Papadopoulos, and F. Koning. 1998. Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity. J. Immunol. 161: 1585-1588. (Pubitemid 28387571)
    • (1998) Journal of Immunology , vol.161 , Issue.4 , pp. 1585-1588
    • Van De, W.Y.1    Kooy, Y.2    Van Veelen, P.3    Pena, S.4    Mearin, L.5    Papadopoulos, G.6    Koning, F.7
  • 7
    • 0031438699 scopus 로고    scopus 로고
    • Autoantibodies in coeliac disease: Tissue transglutaminase guilt by association?
    • Sollid, L. M., O. Molberg, S. McAdam, and K. E. Lundin. 1997. Autoantibodies in coeliac disease: tissue transglutaminase - guilt by association? Gut 41: 851-852. (Pubitemid 28023192)
    • (1997) Gut , vol.41 , Issue.6 , pp. 851-852
    • Sollid, L.M.1    Molberg, O.2    Mcadam, S.3    Lundin, K.E.A.4
  • 9
    • 0037317032 scopus 로고    scopus 로고
    • Transglutaminases: Crosslinking enzymes with pleiotropic functions
    • DOI 10.1038/nrm1014
    • Lorand, L., and R. M. Graham. 2003. Transglutaminases: crosslinking enzymes with pleiotropic functions. Nat. Rev. Mol. Cell Biol. 4: 140-156. (Pubitemid 36172696)
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , Issue.2 , pp. 140-156
    • Lorand, L.1    Graham, R.M.2
  • 10
    • 0028176166 scopus 로고
    • Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka, H., D. M. Perez, K. J. Baek, T. Das, A. Husain, K. Misono, M. J. Im, and R. M. Graham. 1994. Gh: a GTP-binding protein with transglutaminase activity and receptor signaling function. Science 264: 1593-1596.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3    Das, T.4    Husain, A.5    Misono, K.6    Im, M.J.7    Graham, R.M.8
  • 11
    • 0023644524 scopus 로고
    • Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity
    • Achyuthan, K. E., and C. S. Greenberg. 1987. Identification of a guanosine triphosphate-binding site on guinea pig liver transglutaminase. Role of GTP and calcium ions in modulating activity. J. Biol. Chem. 262: 1901-1906.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1901-1906
    • Achyuthan, K.E.1    Greenberg, C.S.2
  • 12
    • 0034635503 scopus 로고    scopus 로고
    • 2+ and GTP binding on tissue transglutaminase tertiary structure
    • DOI 10.1074/jbc.275.6.3915
    • Di Venere, A., A. Rossi, F. De Matteis, N. Rosato, A. F. Agrò, and G. Mei. 2000. Opposite effects of Ca(2+) and GTP binding on tissue transglutaminase tertiary structure. J. Biol. Chem. 275: 3915-3921. (Pubitemid 30094616)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.6 , pp. 3915-3921
    • Di, V.A.1    Rossi, A.2    De Matteis, F.3    Rosato, N.4    Finazzi, A.A.5    Mei, G.6
  • 13
    • 0037022619 scopus 로고    scopus 로고
    • Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity
    • DOI 10.1073/pnas.042454899
    • Liu, S., R. A. Cerione, and J. Clardy. 2002. Structural basis for the guanine nucleotide-binding activity of tissue transglutaminase and its regulation of transamidation activity. Proc. Natl. Acad. Sci. USA 99: 2743-2747. (Pubitemid 34240531)
    • (2002) Proceedings of the National Academy of Sciences of the United States of America , vol.99 , Issue.5 , pp. 2743-2747
    • Liu, S.1    Cerione, R.A.2    Clardy, J.3
  • 14
    • 38549156658 scopus 로고    scopus 로고
    • Transglutaminase 2 undergoes a large conformational change upon activation
    • Pinkas, D. M., P. Strop, A. T. Brunger, and C. Khosla. 2007. Transglutaminase 2 undergoes a large conformational change upon activation. PLoS Biol. 5: e327.
    • (2007) PLoS Biol. , vol.5
    • Pinkas, D.M.1    Strop, P.2    Brunger, A.T.3    Khosla, C.4
  • 15
    • 79955692581 scopus 로고    scopus 로고
    • Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes
    • Zemskov, E. A., I. Mikhailenko, R. C. Hsia, L. Zaritskaya, and A. M. Belkin. 2011. Unconventional secretion of tissue transglutaminase involves phospholipid-dependent delivery into recycling endosomes. PLoS ONE 6: e19414.
    • (2011) PLoS ONE , vol.6
    • Zemskov, E.A.1    Mikhailenko, I.2    Hsia, R.C.3    Zaritskaya, L.4    Belkin, A.M.5
  • 16
    • 0034695929 scopus 로고    scopus 로고
    • Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin
    • Akimov, S. S., D. Krylov, L. F. Fleischman, and A. M. Belkin. 2000. Tissue transglutaminase is an integrin-binding adhesion coreceptor for fibronectin. J. Cell Biol. 148: 825-838.
    • (2000) J. Cell Biol. , vol.148 , pp. 825-838
    • Akimov, S.S.1    Krylov, D.2    Fleischman, L.F.3    Belkin, A.M.4
  • 17
    • 0025948793 scopus 로고
    • Elimination from peripheral lymphoid tissues of self-reactive B lymphocytes recognizing membrane-bound antigens
    • Hartley, S. B., J. Crosbie, R. Brink, A. B. Kantor, A. Basten, and C. C. Goodnow. 1991. Elimination from peripheral lymphoid tissues of self-reactive B lymphocytes recognizing membrane-bound antigens. Nature 353: 765-769. (Pubitemid 21912617)
    • (1991) Nature , vol.353 , Issue.6346 , pp. 765-769
    • Hartley, S.B.1    Crosbie, J.2    Brink, R.3    Kantor, A.B.4    Basten, A.5    Goodnow, C.C.6
  • 20
    • 84862782326 scopus 로고    scopus 로고
    • High abundance of plasma cells secreting transglutaminase 2-specific IgA autoantibodies with limited somatic hypermutation in celiac disease intestinal lesions
    • Di Niro, R., L. Mesin, N. Y. Zheng, J. Stamnaes, M. Morrissey, J. H. Lee, M. Huang, R. Iversen, M. F. du Pré, S. W. Qiao, et al. 2012. High abundance of plasma cells secreting transglutaminase 2-specific IgA autoantibodies with limited somatic hypermutation in celiac disease intestinal lesions. Nat. Med. 18: 441-445.
    • (2012) Nat. Med. , vol.18 , pp. 441-445
    • Di Niro, R.1    Mesin, L.2    Zheng, N.Y.3    Stamnaes, J.4    Morrissey, M.5    Lee, J.H.6    Huang, M.7    Iversen, R.8    Du Pré, M.F.9    Qiao, S.W.10
  • 21
    • 0034747685 scopus 로고    scopus 로고
    • Gene disruption of tissue transglutaminase
    • De Laurenzi, V., and G. Melino. 2001. Gene disruption of tissue transglutaminase. Mol. Cell. Biol. 21: 148-155.
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 148-155
    • De Laurenzi, V.1    Melino, G.2
  • 23
    • 0037039447 scopus 로고    scopus 로고
    • High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: Implications for Celiac Sprue
    • DOI 10.1021/bi011715x
    • Piper, J. L., G. M. Gray, and C. Khosla. 2002. High selectivity of human tissue transglutaminase for immunoactive gliadin peptides: implications for celiac sprue. Biochemistry 41: 386-393. (Pubitemid 34049414)
    • (2002) Biochemistry , vol.41 , Issue.1 , pp. 386-393
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 24
    • 63849240274 scopus 로고    scopus 로고
    • Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen
    • Smith, K., L. Garman, J. Wrammert, N. Y. Zheng, J. D. Capra, R. Ahmed, and P. C. Wilson. 2009. Rapid generation of fully human monoclonal antibodies specific to a vaccinating antigen. Nat. Protoc. 4: 372-384.
    • (2009) Nat. Protoc. , vol.4 , pp. 372-384
    • Smith, K.1    Garman, L.2    Wrammert, J.3    Zheng, N.Y.4    Capra, J.D.5    Ahmed, R.6    Wilson, P.C.7
  • 25
    • 17844391272 scopus 로고    scopus 로고
    • Chemistry and biology of dihydroisoxazole derivatives: Selective inhibitors of human transglutaminase 2
    • DOI 10.1016/j.chembiol.2005.02.007
    • Choi, K., M. Siegel, J. L. Piper, L. Yuan, E. Cho, P. Strnad, B. Omary, K. M. Rich, and C. Khosla. 2005. Chemistry and biology of dihydroisoxazole derivatives: selective inhibitors of human transglutaminase 2. Chem. Biol. 12: 469-475. (Pubitemid 40588922)
    • (2005) Chemistry and Biology , vol.12 , Issue.4 , pp. 469-475
    • Choi, K.1    Siegel, M.2    Piper, J.L.3    Yuan, L.4    Cho, E.5    Strnad, P.6    Omary, B.7    Rich, K.M.8    Khosla, C.9
  • 26
    • 33847033626 scopus 로고    scopus 로고
    • Surface expression of transglutaminase 2 by dendritic cells and its potential role for uptake and presentation of gluten peptides to T cells
    • Ráki, M., K. W. Schjetne, J. Stamnaes, O. Molberg, F. L. Jahnsen, T. B. Issekutz, B. Bogen, and L. M. Sollid. 2007. Surface expression of transglutaminase 2 by dendritic cells and its potential role for uptake and presentation of gluten peptides to T cells. Scand. J. Immunol. 65: 213-220.
    • (2007) Scand. J. Immunol. , vol.65 , pp. 213-220
    • Ráki, M.1    Schjetne, K.W.2    Stamnaes, J.3    Molberg, O.4    Jahnsen, F.L.5    Issekutz, T.B.6    Bogen, B.7    Sollid, L.M.8
  • 27
    • 0037128650 scopus 로고    scopus 로고
    • Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis
    • DOI 10.1084/jem.20011299
    • Sárdy, M., S. Kárpáti, B. Merkl, M. Paulsson, and N. Smyth. 2002. Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. J. Exp. Med. 195: 747-757. (Pubitemid 34259719)
    • (2002) Journal of Experimental Medicine , vol.195 , Issue.6 , pp. 747-757
    • Sardy, M.1    Karpati, S.2    Merkl, B.3    Paulsson, M.4    Smyth, N.5
  • 29
    • 0021148016 scopus 로고
    • Anti-Jo-1 antibody: A marker for myositis with interstitial lung disease
    • Bernstein, R. M., S. H. Morgan, J. Chapman, C. C. Bunn, M. B. Mathews, M. Turner-Warwick, and G. R. Hughes. 1984. Anti-Jo-1 antibody: a marker for myositis with interstitial lung disease. Br. Med. J. (Clin. Res. Ed.) 289: 151-152. (Pubitemid 14010319)
    • (1984) British Medical Journal , vol.289 , Issue.6438 , pp. 151-152
    • Bernstein, R.M.1    Morgan, S.H.2    Chapman, J.3
  • 31
    • 34047130607 scopus 로고    scopus 로고
    • Mutagenesis of the catalytic triad of tissue transglutaminase abrogates coeliac disease serum IgA autoantibody binding
    • DOI 10.1136/gut.2006.092908
    • Byrne, G., F. Ryan, J. Jackson, C. Feighery, and J. Kelly. 2007. Mutagenesis of the catalytic triad of tissue transglutaminase abrogates coeliac disease serum IgA autoantibody binding. Gut 56: 336-341. (Pubitemid 46579760)
    • (2007) Gut , vol.56 , Issue.3 , pp. 336-341
    • Byrne, G.1    Ryan, F.2    Jackson, J.3    Feighery, C.4    Kelly, J.5
  • 33
    • 0028928017 scopus 로고
    • The fibronectinbinding domain of transglutaminase
    • Jeong, J. M., S. N. Murthy, J. T. Radek, and L. Lorand. 1995. The fibronectinbinding domain of transglutaminase. J. Biol. Chem. 270: 5654-5658.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5654-5658
    • Jeong, J.M.1    Murthy, S.N.2    Radek, J.T.3    Lorand, L.4
  • 34
    • 21244479796 scopus 로고    scopus 로고
    • 2-terminal beta-sandwich domain of tissue transglutaminase
    • DOI 10.1074/jbc.M503323200
    • Hang, J., E. A. Zemskov, L. Lorand, and A. M. Belkin. 2005. Identification of a novel recognition sequence for fibronectin within the NH2-terminal betasandwich domain of tissue transglutaminase. J. Biol. Chem. 280: 23675-23683. (Pubitemid 40884849)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.25 , pp. 23675-23683
    • Hang, J.1    Zemskov, E.A.2    Lorand, L.3    Belkin, A.M.4
  • 35
    • 0032747129 scopus 로고    scopus 로고
    • Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal beta-sandwich domain
    • Gaudry, C. A., E. Verderio, D. Aeschlimann, A. Cox, C. Smith, and M. Griffin. 1999. Cell surface localization of tissue transglutaminase is dependent on a fibronectin-binding site in its N-terminal beta-sandwich domain. J. Biol. Chem. 274: 30707-30714.
    • (1999) J. Biol. Chem. , vol.274 , pp. 30707-30714
    • Gaudry, C.A.1    Verderio, E.2    Aeschlimann, D.3    Cox, A.4    Smith, C.5    Griffin, M.6
  • 36
  • 37
    • 80052713226 scopus 로고    scopus 로고
    • Reactivity of the Nterminal region of fibronectin protein to transglutaminase 2 and factor XIIIA
    • Hoffmann, B. R., D. S. Annis, and D. F. Mosher. 2011. Reactivity of the Nterminal region of fibronectin protein to transglutaminase 2 and factor XIIIA. J. Biol. Chem. 286: 32220-32230.
    • (2011) J. Biol. Chem. , vol.286 , pp. 32220-32230
    • Hoffmann, B.R.1    Annis, D.S.2    Mosher, D.F.3
  • 38
    • 67650513329 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans are receptors for the cellsurface trafficking and biological activity of transglutaminase-2
    • Scarpellini, A., R. Germack, H. Lortat-Jacob, T. Muramatsu, E. Billett, T. Johnson, and E. A. Verderio. 2009. Heparan sulfate proteoglycans are receptors for the cellsurface trafficking and biological activity of transglutaminase-2. J. Biol. Chem. 284: 18411-18423.
    • (2009) J. Biol. Chem. , vol.284 , pp. 18411-18423
    • Scarpellini, A.1    Germack, R.2    Lortat-Jacob, H.3    Muramatsu, T.4    Billett, E.5    Johnson, T.6    Verderio, E.A.7
  • 39
    • 0035469864 scopus 로고    scopus 로고
    • Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin
    • Akimov, S. S., and A. M. Belkin. 2001. Cell surface tissue transglutaminase is involved in adhesion and migration of monocytic cells on fibronectin. Blood 98: 1567-1576.
    • (2001) Blood , vol.98 , pp. 1567-1576
    • Akimov, S.S.1    Belkin, A.M.2
  • 40
    • 77950942385 scopus 로고    scopus 로고
    • Transglutaminase 2 is expressed and active on the surface of human monocyte-derived dendritic cells and macrophages
    • Hodrea, J., M. A. Demény, G. Majai, Z. Sarang, I. R. Korponay-Szabó, and L. Fésüs. 2010. Transglutaminase 2 is expressed and active on the surface of human monocyte-derived dendritic cells and macrophages. Immunol. Lett. 130: 74-81.
    • (2010) Immunol. Lett. , vol.130 , pp. 74-81
    • Hodrea, J.1    Demény, M.A.2    Majai, G.3    Sarang, Z.4    Korponay-Szabó, I.R.5    Fésüs, L.6
  • 42
    • 0034887356 scopus 로고    scopus 로고
    • Autoantibodies from patients with coeliac disease recognize distinct functional domains of the autoantigen tissue transglutaminase
    • DOI 10.1046/j.1365-2249.2001.01584.x
    • Seissler, J., U. Wohlrab, C. Wuensche, W. A. Scherbaum, and B. O. Boehm. 2001. Autoantibodies from patients with coeliac disease recognize distinct functional domains of the autoantigen tissue transglutaminase. Clin. Exp. Immunol. 125: 216-221. (Pubitemid 32758431)
    • (2001) Clinical and Experimental Immunology , vol.125 , Issue.2 , pp. 216-221
    • Seissler, J.1    Wohlrab, U.2    Wuensche, C.3    Scherbaum, W.A.4    Boehm, B.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.