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Volumn 30, Issue 3, 2000, Pages 232-240

Role of tissue transglutaminase in celiac disease

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; GLIADIN; GLUTEN; HLA DQ ANTIGEN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE;

EID: 0034120153     PISSN: 02772116     EISSN: None     Source Type: Journal    
DOI: 10.1097/00005176-200003000-00005     Document Type: Review
Times cited : (85)

References (91)
  • 1
    • 0034121187 scopus 로고    scopus 로고
    • Molecular basis of celiac disease
    • in press
    • Sollid LM. Molecular basis of celiac disease. Ann Rev Immunol (in press).
    • Ann Rev Immunol
    • Sollid, L.M.1
  • 2
    • 0027445948 scopus 로고
    • Evidence that gluten sensitivity is an immunologic disease
    • Marsh MN, Ensari A, Morgan S. Evidence that gluten sensitivity is an immunologic disease. Curr Opin Gastroenterol 1993;9:994-1000.
    • (1993) Curr Opin Gastroenterol , vol.9 , pp. 994-1000
    • Marsh, M.N.1    Ensari, A.2    Morgan, S.3
  • 3
    • 0026423260 scopus 로고
    • Celiac sprue
    • Trier JS. Celiac sprue. N Engl J Med 1991;325:1709-19.
    • (1991) N Engl J Med , vol.325 , pp. 1709-1719
    • Trier, J.S.1
  • 4
    • 0030660433 scopus 로고    scopus 로고
    • Genetic contribution of the HLA region to the familial clustering of coeliac disease
    • Petronzelli F, Bonamico M, Ferrante P, et al. Genetic contribution of the HLA region to the familial clustering of coeliac disease. Ann Hum Genet 1997;6:307-17.
    • (1997) Ann Hum Genet , vol.6 , pp. 307-317
    • Petronzelli, F.1    Bonamico, M.2    Ferrante, P.3
  • 6
    • 0030903745 scopus 로고    scopus 로고
    • Invited anniversary review: HLA associated diseases
    • Thorsby E. Invited anniversary review: HLA associated diseases. Hum Immunol 1997;53:1-11.
    • (1997) Hum Immunol , vol.53 , pp. 1-11
    • Thorsby, E.1
  • 7
    • 0027292775 scopus 로고
    • HLA susceptibility genes in celiac disease: Genetic mapping and role in pathogenesis
    • Sollid LM. Thorsby E. HLA susceptibility genes in celiac disease: Genetic mapping and role in pathogenesis. Gastroenterology 1993; 105:910-22.
    • (1993) Gastroenterology , vol.105 , pp. 910-922
    • Sollid, L.M.1    Thorsby, E.2
  • 8
    • 0027319208 scopus 로고
    • Gliadin-specific, HLA-DQ(1*0501,1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients
    • Lundin KEA, Scott H, Hansen T et al. Gliadin-specific, HLA-DQ(1*0501,1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients. J Exp Med 1993;178: 187-96.
    • (1993) J Exp Med , vol.178 , pp. 187-196
    • Lundin, K.E.A.1    Scott, H.2    Hansen, T.3
  • 9
    • 0028556659 scopus 로고
    • T cells from the small intestinal mucosa of a DR4, DQ7/ DQ8 celiac disease patient preferentially recognize gliadin when presented by DQ8
    • Lundin KEA, Scott H, Fausa O, Thorsby E, Sollid LM. T cells from the small intestinal mucosa of a DR4, DQ7/ DQ8 celiac disease patient preferentially recognize gliadin when presented by DQ8. Human Immunology 1994;41:285-91.
    • (1994) Human Immunology , vol.41 , pp. 285-291
    • Lundin, K.E.A.1    Scott, H.2    Fausa, O.3    Thorsby, E.4    Sollid, L.M.5
  • 10
    • 0031775418 scopus 로고    scopus 로고
    • HLA restriction patterns of gliadin- and astrovirus-specific CD4+ T cells isolated in parallel from the small intestine of celiac disease patients
    • Molberg Ø, Lundin KEA, Nilsen EM, et al. HLA restriction patterns of gliadin- and astrovirus-specific CD4+ T cells isolated in parallel from the small intestine of celiac disease patients. Tissue Antigens 1998;52:407-15.
    • (1998) Tissue Antigens , vol.52 , pp. 407-415
    • Molberg, Ø.1    Lundin, K.E.A.2    Nilsen, E.M.3
  • 11
    • 0031891459 scopus 로고    scopus 로고
    • Majority of gliadin-specific T-cell clones from celiac small intestinal mucosa produce interferon- and interleukin-4
    • Troncone R, Gianfrani C, Mazzarella G, et al. Majority of gliadin-specific T-cell clones from celiac small intestinal mucosa produce interferon- and interleukin-4. Dig Dis Sci 1998;43:156-61.
    • (1998) Dig Dis Sci , vol.43 , pp. 156-161
    • Troncone, R.1    Gianfrani, C.2    Mazzarella, G.3
  • 12
    • 13144283626 scopus 로고    scopus 로고
    • Small intestinal T cells of celiac disease patients recognize a natural pepsin fragment of gliadin
    • van de Wal Y, Kooy YC, van Veelen PA, et al. Small intestinal T cells of celiac disease patients recognize a natural pepsin fragment of gliadin. Proc Natl Acad Sci USA 1998;95:10050-4.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10050-10054
    • Van De Wal, Y.1    Kooy, Y.C.2    Van Veelen, P.A.3
  • 13
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • Dieterich W, Ehnis T, Bauer M, et al. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nat Med 1997;3:797-801.
    • (1997) Nat Med , vol.3 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2    Bauer, M.3
  • 14
    • 0031760420 scopus 로고    scopus 로고
    • Autoantibodies to tissue transglutaminase as predictors of celiac disease
    • Dieterich W, Laag E, Schopper H, et al. Autoantibodies to tissue transglutaminase as predictors of celiac disease. Gastroenterology 1998;115:1317-21.
    • (1998) Gastroenterology , vol.115 , pp. 1317-1321
    • Dieterich, W.1    Laag, E.2    Schopper, H.3
  • 15
    • 0031762794 scopus 로고    scopus 로고
    • Tissue transglutaminase autoantibody enzyme-linked immunosorbent assay in detecting celiac disease
    • Sulkanen S, Halttunen T, Laurila K, et al. Tissue transglutaminase autoantibody enzyme-linked immunosorbent assay in detecting celiac disease. Gastroenterology 1998;115:1322-8.
    • (1998) Gastroenterology , vol.115 , pp. 1322-1328
    • Sulkanen, S.1    Halttunen, T.2    Laurila, K.3
  • 16
    • 0020698882 scopus 로고
    • Mechanism and basis for specificity of transglutaminase-catalyzed ∈-γ-glutamyl lysine bond formation
    • Folk JE. Mechanism and basis for specificity of transglutaminase-catalyzed ∈-γ-glutamyl) lysine bond formation. Adv Enzymol Relat Areas Mol Biol 1983;54:1-56.
    • (1983) Adv Enzymol Relat Areas Mol Biol , vol.54 , pp. 1-56
    • Folk, J.E.1
  • 18
    • 0014429064 scopus 로고
    • Mechanism of action of guinea pig liver transglutaminase. V: The hydrolysis reaction
    • Folk JE, Cole PW, Mullooly JP. Mechanism of action of guinea pig liver transglutaminase. V: The hydrolysis reaction. J Biol Chem 1968;243:418-27.
    • (1968) J Biol Chem , vol.243 , pp. 418-427
    • Folk, J.E.1    Cole, P.W.2    Mullooly, J.P.3
  • 19
    • 0028322985 scopus 로고
    • Transglutaminases: Protein cross-linking enzymes in tissues and body fluids
    • Aeschlimann D, Paulsson M. Transglutaminases: Protein cross-linking enzymes in tissues and body fluids. Thromb Haemost 1994; 71:402-15.
    • (1994) Thromb Haemost , vol.71 , pp. 402-415
    • Aeschlimann, D.1    Paulsson, M.2
  • 20
    • 0026612802 scopus 로고
    • Identification of Gln726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes
    • Aeschlimann D, Paulsson M, Mann K. Identification of Gln726 in nidogen as the amine acceptor in transglutaminase-catalyzed cross-linking of laminin-nidogen complexes. J Biol Chem 1992;267: 11316-21.
    • (1992) J Biol Chem , vol.267 , pp. 11316-11321
    • Aeschlimann, D.1    Paulsson, M.2    Mann, K.3
  • 21
    • 0021142637 scopus 로고
    • Structural features of glutamine substrates for transglutaminases: Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme
    • Gorman JJ, Folk JE. Structural features of glutamine substrates for transglutaminases: Role of extended interactions in the specificity of human plasma factor XIIIa and of the guinea pig liver enzyme. J Biol Chem 1984;259:9007-10.
    • (1984) J Biol Chem , vol.259 , pp. 9007-9010
    • Gorman, J.J.1    Folk, J.E.2
  • 22
    • 0029856046 scopus 로고    scopus 로고
    • Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system
    • Kahlem P, Terre C, Green H, Djian P. Peptides containing glutamine repeats as substrates for transglutaminase-catalyzed cross-linking: Relevance to diseases of the nervous system. Proc Natl Acad Sci USA 1996;93:14580-5.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14580-14585
    • Kahlem, P.1    Terre, C.2    Green, H.3    Djian, P.4
  • 23
    • 0026338017 scopus 로고
    • Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues
    • Greenberg CS, Birckbichler PJ, Rice RH. Transglutaminases: Multifunctional cross-linking enzymes that stabilize tissues. FASEB J 1991;5:3071-7.
    • (1991) FASEB J , vol.5 , pp. 3071-3077
    • Greenberg, C.S.1    Birckbichler, P.J.2    Rice, R.H.3
  • 25
    • 0028176166 scopus 로고
    • Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function
    • Nakaoka H, Perez DM, Baek KJ, et al. Gh: A GTP-binding protein with transglutaminase activity and receptor signaling function. Science 1994;264:1593-6.
    • (1994) Science , vol.264 , pp. 1593-1596
    • Nakaoka, H.1    Perez, D.M.2    Baek, K.J.3
  • 26
    • 0032488822 scopus 로고    scopus 로고
    • Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes: Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers
    • Aeschlimann D, Koeller MK, Allen-Hoffmann BL, Mosher DF. Isolation of a cDNA encoding a novel member of the transglutaminase gene family from human keratinocytes: Detection and identification of transglutaminase gene products based on reverse transcription-polymerase chain reaction with degenerate primers. J Biol Chem 1998;273:3452-60.
    • (1998) J Biol Chem , vol.273 , pp. 3452-3460
    • Aeschlimann, D.1    Koeller, M.K.2    Allen-Hoffmann, B.L.3    Mosher, D.F.4
  • 27
    • 0028907482 scopus 로고
    • Isolation and characterization of the human tissue transglutaminase gene promoter
    • Lu S, Saydak M, Gentile V, Stein JP, Davies PJ. Isolation and characterization of the human tissue transglutaminase gene promoter. J Biol Chem 1995;270:9748-56.
    • (1995) J Biol Chem , vol.270 , pp. 9748-9756
    • Lu, S.1    Saydak, M.2    Gentile, V.3    Stein, J.P.4    Davies, P.J.5
  • 28
    • 0030894829 scopus 로고    scopus 로고
    • Regulation of the expression of the tissue transglutaminase gene by DNA methylation
    • Lu S, Davies PA. Regulation of the expression of the tissue transglutaminase gene by DNA methylation. Proc Natl Acad Sci USA 1997;94:4692-7.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 4692-4697
    • Lu, S.1    Davies, P.A.2
  • 29
    • 0031885898 scopus 로고    scopus 로고
    • TNF-α modulates expression of the tissue transglutaminase gene in liver cells
    • Kuncio GS, Tsyganskaya M, Zhu J, et al. TNF-α modulates expression of the tissue transglutaminase gene in liver cells. Am J Physiol 1998;274:1-5.
    • (1998) Am J Physiol , vol.274 , pp. 1-5
    • Kuncio, G.S.1    Tsyganskaya, M.2    Zhu, J.3
  • 30
    • 0032170231 scopus 로고    scopus 로고
    • Properties of purified lens transglutaminase and regulation of its transamidase/crosslinking activity by GTP
    • Murthy SN, Velasco PT, Lorand L. Properties of purified lens transglutaminase and regulation of its transamidase/crosslinking activity by GTP. Exp Eye Res 1998;67:273-81.
    • (1998) Exp Eye Res , vol.67 , pp. 273-281
    • Murthy, S.N.1    Velasco, P.T.2    Lorand, L.3
  • 31
    • 0027405028 scopus 로고
    • Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells
    • Suto N, Ikura K, Sasaki R. Expression induced by interleukin-6 of tissue-type transglutaminase in human hepatoblastoma HepG2 cells. J Biol Chem 1993;268:7469-73.
    • (1993) J Biol Chem , vol.268 , pp. 7469-7473
    • Suto, N.1    Ikura, K.2    Sasaki, R.3
  • 32
    • 0024597647 scopus 로고
    • Differential expression of tissue transglutaminase in human cells: An immunohistochemical study
    • Thomazy V, Fesus L. Differential expression of tissue transglutaminase in human cells: An immunohistochemical study. Cell Tissue Res 1989;255:215-24.
    • (1989) Cell Tissue Res , vol.255 , pp. 215-224
    • Thomazy, V.1    Fesus, L.2
  • 33
    • 0031893826 scopus 로고    scopus 로고
    • Modulation of the in situ activity of tissue transglutaminase by calcium and GTP
    • Zhang J, Lesort M, Guttmann RP, Johnson GV. Modulation of the in situ activity of tissue transglutaminase by calcium and GTP. J Biol Chem 1998;273:2288-95.
    • (1998) J Biol Chem , vol.273 , pp. 2288-2295
    • Zhang, J.1    Lesort, M.2    Guttmann, R.P.3    Johnson, G.V.4
  • 34
    • 0030997651 scopus 로고    scopus 로고
    • Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase
    • Lai TS, Bielawska A, Peoples KA, Hannun YA, Greenberg CS. Sphingosylphosphocholine reduces the calcium ion requirement for activating tissue transglutaminase. J Biol Chem 1997;272: 16295-300.
    • (1997) J Biol Chem , vol.272 , pp. 16295-16300
    • Lai, T.S.1    Bielawska, A.2    Peoples, K.A.3    Hannun, Y.A.4    Greenberg, C.S.5
  • 35
    • 0030450884 scopus 로고    scopus 로고
    • Tissue transglutaminase and factor XIII in cartilage and bone remodeling
    • Aeschlimann D, Mosher D, Paulsson M. Tissue transglutaminase and factor XIII in cartilage and bone remodeling. Semin Thromb Hemost 1996;22:437-43.
    • (1996) Semin Thromb Hemost , vol.22 , pp. 437-443
    • Aeschlimann, D.1    Mosher, D.2    Paulsson, M.3
  • 36
    • 0031228921 scopus 로고    scopus 로고
    • Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development
    • Schittny JC, Paulsson M, Vallan C, et al. Protein cross-linking mediated by tissue transglutaminase correlates with the maturation of extracellular matrices during lung development. Am J Respir Cell Mol Biol 1997;17:334-43.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 334-343
    • Schittny, J.C.1    Paulsson, M.2    Vallan, C.3
  • 37
    • 0026774043 scopus 로고
    • Role of transglutaminase and protein cross-linking in the repair of mucosal stress erosions
    • Wang JY, Johnson LR. Role of transglutaminase and protein cross-linking in the repair of mucosal stress erosions. Am J Physiol 1992;262:19-25.
    • (1992) Am J Physiol , vol.262 , pp. 19-25
    • Wang, J.Y.1    Johnson, L.R.2
  • 38
    • 0029744038 scopus 로고    scopus 로고
    • Induction of "tissue" transglutaminase in HIV pathogenesis: Evidence for high rate of apoptosis of CD4+ T lymphocytes and accessory cells in lymphoid tissues
    • Amendola A, Gougeon ML, Poccia F, et al. Induction of "tissue" transglutaminase in HIV pathogenesis: Evidence for high rate of apoptosis of CD4+ T lymphocytes and accessory cells in lymphoid tissues. Proc Natl Acad Sci USA 1996;93:11057-62.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 11057-11062
    • Amendola, A.1    Gougeon, M.L.2    Poccia, F.3
  • 39
    • 0018864611 scopus 로고
    • Transglutaminase is essential in receptor-mediated endocytosis of 2-macroglobulin and polypeptide hormones
    • Davies PJ, Davies DR, Levitzki A, et al. Transglutaminase is essential in receptor-mediated endocytosis of 2-macroglobulin and polypeptide hormones. Nature 1980;283:162-7.
    • (1980) Nature , vol.283 , pp. 162-167
    • Davies, P.J.1    Davies, D.R.2    Levitzki, A.3
  • 40
    • 0021350904 scopus 로고
    • Transglutaminase and receptor-mediated endocytosis in macrophages and cultured fibroblasts
    • Davies PJ, Murtaugh MP. Transglutaminase and receptor-mediated endocytosis in macrophages and cultured fibroblasts. Mol Cell Biochem 1984;58:69-77.
    • (1984) Mol Cell Biochem , vol.58 , pp. 69-77
    • Davies, P.J.1    Murtaugh, M.P.2
  • 41
    • 0021967851 scopus 로고
    • Possible involvement of transglutaminase in endocytosis and antigen presentation
    • Teshigawara K, Kannagi R, Noro N, Masuda T. Possible involvement of transglutaminase in endocytosis and antigen presentation. Microbiol Immunol 1985;29:737-50.
    • (1985) Microbiol Immunol , vol.29 , pp. 737-750
    • Teshigawara, K.1    Kannagi, R.2    Noro, N.3    Masuda, T.4
  • 42
    • 0019424083 scopus 로고
    • Transglutaminase modifies the carboxy-terminal intracellular region of HLA-A and -B antigens
    • Pober JS, Strominger JL. Transglutaminase modifies the carboxy-terminal intracellular region of HLA-A and -B antigens. Nature 1981;289:819-21.
    • (1981) Nature , vol.289 , pp. 819-821
    • Pober, J.S.1    Strominger, J.L.2
  • 43
    • 0021327593 scopus 로고
    • Induction of tissue transglutaminase in human peripheral blood monocytes
    • Murtaugh MP, Arend WP, Davies PJ. Induction of tissue transglutaminase in human peripheral blood monocytes. J Exp Med 1984; 159:114-25.
    • (1984) J Exp Med , vol.159 , pp. 114-125
    • Murtaugh, M.P.1    Arend, W.P.2    Davies, P.J.3
  • 44
    • 0020655480 scopus 로고
    • Primary amines inhibit the triggering of B lymphocytes to antibody synthesis
    • Julian C, Speck NA, Pierce SK. Primary amines inhibit the triggering of B lymphocytes to antibody synthesis. J Immunol 1983; 130:91-6.
    • (1983) J Immunol , vol.130 , pp. 91-96
    • Julian, C.1    Speck, N.A.2    Pierce, S.K.3
  • 45
    • 0023758164 scopus 로고
    • Implication of transglutaminase in mitogen-induced human lymphocyte blast transformation
    • Metafora S, Peluso G, Ravagnan G, et al. Implication of transglutaminase in mitogen-induced human lymphocyte blast transformation. Adv Exp Med Biol 1988;231-84.
    • (1988) Adv Exp Med Biol , pp. 231-284
    • Metafora, S.1    Peluso, G.2    Ravagnan, G.3
  • 46
    • 0020411865 scopus 로고
    • Enhanced transglutaminase activity associated with macrophage activation. Possible role in Fc-mediated phagocytosis
    • Leu RW, Herriott MJ, Moore PE, Orr GR, Birckbichler PJ. Enhanced transglutaminase activity associated with macrophage activation. Possible role in Fc-mediated phagocytosis. Exp Cell Res 1982;141:191-9.
    • (1982) Exp Cell Res , vol.141 , pp. 191-199
    • Leu, R.W.1    Herriott, M.J.2    Moore, P.E.3    Orr, G.R.4    Birckbichler, P.J.5
  • 47
    • 0040041521 scopus 로고    scopus 로고
    • Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase
    • Murthy SN, Wilson JH, Lukas TJ, Kuret J, Lorand L. Cross-linking sites of the human tau protein, probed by reactions with human transglutaminase. J Neurochem 1998;71:2607-14.
    • (1998) J Neurochem , vol.71 , pp. 2607-2614
    • Murthy, S.N.1    Wilson, J.H.2    Lukas, T.J.3    Kuret, J.4    Lorand, L.5
  • 48
    • 0000831917 scopus 로고
    • Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers
    • Selkoe DJ, Abraham C, Ihara Y. Brain transglutaminase: In vitro crosslinking of human neurofilament proteins into insoluble polymers. Proc Natl Acad Sci USA 1982;79:6070-4.
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 6070-6074
    • Selkoe, D.J.1    Abraham, C.2    Ihara, Y.3
  • 49
    • 0033594894 scopus 로고    scopus 로고
    • Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei
    • Karpuj MV, Garren H, Slunt H, et al. Transglutaminase aggregates huntingtin into nonamyloidogenic polymers, and its enzymatic activity increases in Huntington's disease brain nuclei. Proc Natl Acad Sci USA 1999;46:7388-93.
    • (1999) Proc Natl Acad Sci USA , vol.46 , pp. 7388-7393
    • Karpuj, M.V.1    Garren, H.2    Slunt, H.3
  • 50
    • 0032014092 scopus 로고    scopus 로고
    • Transglutaminase action imitates Huntington's disease: Selective polymerization of Huntingtin containing expanded polyglutamine
    • Kahlem P, Green H, Djian P. Transglutaminase action imitates Huntington's disease: Selective polymerization of Huntingtin containing expanded polyglutamine. Mol Cell 1998;1:595-601.
    • (1998) Mol Cell , vol.1 , pp. 595-601
    • Kahlem, P.1    Green, H.2    Djian, P.3
  • 51
    • 7844246539 scopus 로고    scopus 로고
    • Growth inhibition of human in vitro and mouse in vitro and in vivo mammary tumor models by retinoids in comparison with tamoxifen and the RU-486 antiprogestagen
    • Darro F, Cahen P, Vianna A, et al. Growth inhibition of human in vitro and mouse in vitro and in vivo mammary tumor models by retinoids in comparison with tamoxifen and the RU-486 antiprogestagen. Breast Cancer Res Treat 1998;51:39-55.
    • (1998) Breast Cancer Res Treat , vol.51 , pp. 39-55
    • Darro, F.1    Cahen, P.2    Vianna, A.3
  • 52
    • 0028921610 scopus 로고
    • Prolactin-immunoglobulin G complexes from human serum act as costimulatory ligands causing proliferation of malignant B lymphocytes
    • Walker AM, Montgomery DW, Saraiya S, et al. Prolactin-immunoglobulin G complexes from human serum act as costimulatory ligands causing proliferation of malignant B lymphocytes. Proc Natl Acad Sci USA 1995;92:3278-82.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3278-3282
    • Walker, A.M.1    Montgomery, D.W.2    Saraiya, S.3
  • 53
    • 0028804296 scopus 로고
    • Transglutaminases in Crohn's disease
    • D'Argenio G, Biancone L, Cosenza V, et al. Transglutaminases in Crohn's disease. Gut 1995;37:690-5.
    • (1995) Gut , vol.37 , pp. 690-695
    • D'Argenio, G.1    Biancone, L.2    Cosenza, V.3
  • 54
    • 0033023517 scopus 로고    scopus 로고
    • Tissue transglutaminase: Apoptosis versus autoimmunity
    • Piacentini M, Colizzi V. Tissue transglutaminase: Apoptosis versus autoimmunity. Immunol Today 1999;20:130-4.
    • (1999) Immunol Today , vol.20 , pp. 130-134
    • Piacentini, M.1    Colizzi, V.2
  • 55
    • 0031863698 scopus 로고    scopus 로고
    • Posttranslational protein modifications, apoptosis, and the bypass of tolerance to autoantigens
    • Utz PJ, Anderson P. Posttranslational protein modifications, apoptosis, and the bypass of tolerance to autoantigens. Arthritis Rheum 1998;41:1152-60.
    • (1998) Arthritis Rheum , vol.41 , pp. 1152-1160
    • Utz, P.J.1    Anderson, P.2
  • 56
    • 0032170644 scopus 로고    scopus 로고
    • Deamidation and disulfide bonding in human lens-crystallins
    • Hanson SR, Smith DL, Smith JB. Deamidation and disulfide bonding in human lens-crystallins. Exp Eye Res 1998;67:301-12.
    • (1998) Exp Eye Res , vol.67 , pp. 301-312
    • Hanson, S.R.1    Smith, D.L.2    Smith, J.B.3
  • 57
    • 0032128377 scopus 로고    scopus 로고
    • Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry
    • Lampi KJ, Ma Z, Hanson SR, et al. Age-related changes in human lens crystallins identified by two- dimensional electrophoresis and mass spectrometry. Exp Eye Res 1998;67:31-43.
    • (1998) Exp Eye Res , vol.67 , pp. 31-43
    • Lampi, K.J.1    Ma, Z.2    Hanson, S.R.3
  • 58
    • 0032577588 scopus 로고    scopus 로고
    • The rho-deamidating cytotoxic necrotizing factor 1 from escherichia coli possesses transglutaminase activity: Cysteine 866 and histidine 881 are essential for enzyme activity
    • Schmidt G, Selzer J, Lerm M, Aktories K. The rho-deamidating cytotoxic necrotizing factor 1 from escherichia coli possesses transglutaminase activity: Cysteine 866 and histidine 881 are essential for enzyme activity. J Biol Chem 1998;273:13669-74.
    • (1998) J Biol Chem , vol.273 , pp. 13669-13674
    • Schmidt, G.1    Selzer, J.2    Lerm, M.3    Aktories, K.4
  • 59
    • 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 (Colch) 1985;68:573-9.
    • (1985) Clin Sci (Colch) , vol.68 , pp. 573-579
    • Bruce, S.E.1    Bjarnason, I.2    Peters, T.J.3
  • 60
    • 0024390253 scopus 로고
    • Human serum transglutaminase and coeliac disease: Correlation between serum and muosal activity in an experimental model of rat small bowel enteropathy
    • D'Argenio G, Sorrentini I, Ciacci C, et al. Human serum transglutaminase and coeliac disease: Correlation between serum and muosal activity in an experimental model of rat small bowel enteropathy. Gut 1989;30:950-4.
    • (1989) Gut , vol.30 , pp. 950-954
    • D'Argenio, G.1    Sorrentini, I.2    Ciacci, C.3
  • 62
    • 0040707494 scopus 로고    scopus 로고
    • Gliadin is a preferred substrate for tissue transglutaminase, the autoantigen in coeliac disease
    • Dietrich W, Ehnis T, Bauer M, Riecken EO, Schuppan D. Gliadin is a preferred substrate for tissue transglutaminase, the autoantigen in coeliac disease (abstract). Gastroenterology 1997;A359.
    • (1997) Gastroenterology
    • Dietrich, W.1    Ehnis, T.2    Bauer, M.3    Riecken, E.O.4    Schuppan, D.5
  • 63
    • 0031438699 scopus 로고    scopus 로고
    • Autoantibodies in coeliac disease: Tissue transglutaminase - Guilt by association
    • Sollid LM, Molberg Ø, McAdam S, Lundin KEA. Autoantibodies in coeliac disease: Tissue transglutaminase - guilt by association. Gut 1997;41:851-2.
    • (1997) Gut , vol.41 , pp. 851-852
    • Sollid, L.M.1    Molberg, Ø.2    McAdam, S.3    Lundin, K.E.A.4
  • 64
    • 0014829537 scopus 로고
    • Carrier function in anti-hapten immune responses. II: Specific properties of carrier cells capable of enhancing anti-hapten antibody responses
    • Paul WE, Katz DH, Goidl EA, Benacerraf B. Carrier function in anti-hapten immune responses. II: Specific properties of carrier cells capable of enhancing anti-hapten antibody responses. J Exp Med 1970;132:283-99.
    • (1970) J Exp Med , vol.132 , pp. 283-299
    • Paul, W.E.1    Katz, D.H.2    Goidl, E.A.3    Benacerraf, B.4
  • 65
    • 0030593837 scopus 로고    scopus 로고
    • Production of antiendomysial antibodies after in-vitro gliadin challenge of small intestine biopsy samples from patients with coeliac disease
    • Picarelli A, Maiuri L, Frate A, et al. Production of antiendomysial antibodies after in-vitro gliadin challenge of small intestine biopsy samples from patients with coeliac disease. Lancet 1996;348: 1065-7.
    • (1996) Lancet , vol.348 , pp. 1065-1067
    • Picarelli, A.1    Maiuri, L.2    Frate, A.3
  • 66
    • 0033119202 scopus 로고    scopus 로고
    • In vitro production of endomysial antibodies in cultured duodenal mucosa from patients with celiac disease
    • Vogelsang H, Schwarzenhofer M, Granditsch G, Oberhuber G. In vitro production of endomysial antibodies in cultured duodenal mucosa from patients with celiac disease. Am J Gastroenterol 1999;94:1057-61.
    • (1999) Am J Gastroenterol , vol.94 , pp. 1057-1061
    • Vogelsang, H.1    Schwarzenhofer, M.2    Granditsch, G.3    Oberhuber, G.4
  • 67
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • Molberg Ø, Mcadam SN, Körner R, et al. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat Med 1998;4:713-7.
    • (1998) Nat Med , vol.4 , pp. 713-717
    • Molberg, Ø.1    Mcadam, S.N.2    Körner, R.3
  • 68
    • 2142764316 scopus 로고    scopus 로고
    • Identification of a gliadin T-cell epitope in coeliac disease: General importance of gliadin deamidation for intestinal T-cell recognition
    • Sjöström H, Lundin KEA, Molberg Ø, et al. Identification of a gliadin T-cell epitope in coeliac disease: General importance of gliadin deamidation for intestinal T-cell recognition. Scand J Immunol 1998;48:111-5.
    • (1998) Scand J Immunol , vol.48 , pp. 111-115
    • Sjöström, H.1    Lundin, K.E.A.2    Molberg, Ø.3
  • 69
    • 0032528813 scopus 로고    scopus 로고
    • Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity
    • van de Wal Y, Kooy Y, van Veelen P, et al. Selective deamidation by tissue transglutaminase strongly enhances gliadin-specific T cell reactivity. J Immunol 1998;161:1585-8.
    • (1998) J Immunol , vol.161 , pp. 1585-1588
    • Van De Wal, Y.1    Kooy, Y.2    Van Veelen, P.3
  • 70
    • 0342800420 scopus 로고    scopus 로고
    • The intestinal T cell response to -gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase
    • in press
    • Arentz-Hansen EH, Körner R, Molberg Ø, et al. The intestinal T cell response to -gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase. J Exp Med (in press).
    • J Exp Med
    • Arentz-Hansen, E.H.1    Körner, R.2    Molberg, Ø.3
  • 71
    • 0032802769 scopus 로고    scopus 로고
    • HLA binding and T cell recognition of a tissue transglutaminase-modified gliadin epitope
    • Quarsten H, Molberg Ø, Fugger L, Mcadam SN, Sollid LM. HLA binding and T cell recognition of a tissue transglutaminase-modified gliadin epitope. Eur J Immunol 1999;99:2506-14.
    • (1999) Eur J Immunol , vol.99 , pp. 2506-2514
    • Quarsten, H.1    Molberg, Ø.2    Fugger, L.3    Mcadam, S.N.4    Sollid, L.M.5
  • 74
    • 10244264710 scopus 로고    scopus 로고
    • The peptide binding motif of the disease associated HLA-DQ (1* 0501, 1* 0201) molecule
    • Vartdal F, Johansen BH, Friede T, et al. The peptide binding motif of the disease associated HLA-DQ (1* 0501, 1* 0201) molecule. Eur J Immunol 1996;26:2764-72.
    • (1996) Eur J Immunol , vol.26 , pp. 2764-2772
    • Vartdal, F.1    Johansen, B.H.2    Friede, T.3
  • 75
    • 0029815574 scopus 로고    scopus 로고
    • Peptide binding characteristics of the coeliac disease-associated DQ(1*0501, 1*0201) molecule
    • van de Wal Y, Kooy YC, Drijfhout JW, Amons R, Koning F. Peptide binding characteristics of the coeliac disease-associated DQ(1*0501, 1*0201) molecule. Immunogenetics 1996;44:246-53.
    • (1996) Immunogenetics , vol.44 , pp. 246-253
    • Van De Wal, Y.1    Kooy, Y.C.2    Drijfhout, J.W.3    Amons, R.4    Koning, F.5
  • 76
    • 0028228509 scopus 로고
    • T cells from the peripheral blood of coeliac disease patients recognize gluten antigens when presented by HLA-DR, -DQ, or -DP molecules
    • Gjertsen HA, Sollid LM, Ek J, Thorsby E, Lundin KE. T cells from the peripheral blood of coeliac disease patients recognize gluten antigens when presented by HLA-DR, -DQ, or -DP molecules. Scand J Immunol 1994;39:567-74.
    • (1994) Scand J Immunol , vol.39 , pp. 567-574
    • Gjertsen, H.A.1    Sollid, L.M.2    Ek, J.3    Thorsby, E.4    Lundin, K.E.5
  • 78
    • 0030974902 scopus 로고    scopus 로고
    • Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β
    • Nunes I, Gleizes PE, Metz CN, Rifkin DB. Latent transforming growth factor-beta binding protein domains involved in activation and transglutaminase-dependent cross-linking of latent transforming growth factor-β. J Cell Biol 1997;136:1151-63.
    • (1997) J Cell Biol , vol.136 , pp. 1151-1163
    • Nunes, I.1    Gleizes, P.E.2    Metz, C.N.3    Rifkin, D.B.4
  • 79
    • 0031944290 scopus 로고    scopus 로고
    • Regulation of immune responses by TGF-β
    • Letterio JJ, Roberts AB. Regulation of immune responses by TGF-β. Annu Rev Immunol 1998;16:137-61.
    • (1998) Annu Rev Immunol , vol.16 , pp. 137-161
    • Letterio, J.J.1    Roberts, A.B.2
  • 80
    • 0033578417 scopus 로고    scopus 로고
    • Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II
    • Feng JF, Readon M, Yadav SP, Im MJ. Calreticulin down-regulates both GTP binding and transglutaminase activities of transglutaminase II. Biochemistry 1999;38:10743-9.
    • (1999) Biochemistry , vol.38 , pp. 10743-10749
    • Feng, J.F.1    Readon, M.2    Yadav, S.P.3    Im, M.J.4
  • 81
    • 0032985177 scopus 로고    scopus 로고
    • Identification of common epitopes on gliadin, enterocytes, and calreticulin recognised by antigliadin antibodies of patients with coeliac disease
    • Krupickova S, Tuckova L, Flegelova Z, et al. Identification of common epitopes on gliadin, enterocytes, and calreticulin recognised by antigliadin antibodies of patients with coeliac disease. Gut 1999;44:168-73.
    • (1999) Gut , vol.44 , pp. 168-173
    • Krupickova, S.1    Tuckova, L.2    Flegelova, Z.3
  • 82
    • 0033558097 scopus 로고    scopus 로고
    • A conformation-dependent epitope in Addison's disease and other endocrinological autoimmune diseases maps to a carboxyl-terminal functional domain of human steroid 21-hydroxylase
    • Nikoshkov A, Falorni A, Lajic S, et al. A conformation-dependent epitope in Addison's disease and other endocrinological autoimmune diseases maps to a carboxyl-terminal functional domain of human steroid 21-hydroxylase. J Immunol 1999;162:2422-6.
    • (1999) J Immunol , vol.162 , pp. 2422-2426
    • Nikoshkov, A.1    Falorni, A.2    Lajic, S.3
  • 83
    • 0025816588 scopus 로고
    • Anti-thyroid peroxidase antibodies in sera from healthy subjects and from patients with chronic thyroiditis: Differences in the ability to inhibit thyroid peroxidase activities
    • Kohno Y, Yamaguchi F, Saito K, et al. Anti-thyroid peroxidase antibodies in sera from healthy subjects and from patients with chronic thyroiditis: Differences in the ability to inhibit thyroid peroxidase activities. Clin Exp Immunol 1991;85:459-63.
    • (1991) Clin Exp Immunol , vol.85 , pp. 459-463
    • Kohno, Y.1    Yamaguchi, F.2    Saito, K.3
  • 84
    • 0033574642 scopus 로고    scopus 로고
    • High-resolution autoreactive epitope mapping and structural modeling of the 65 kDa form of human glutamic acid decarboxylase
    • Schwartz HL, Chandonia JM, Kash SF, et al. High-resolution autoreactive epitope mapping and structural modeling of the 65 kDa form of human glutamic acid decarboxylase. J Mol Biol 1999;287: 983-99.
    • (1999) J Mol Biol , vol.287 , pp. 983-999
    • Schwartz, H.L.1    Chandonia, J.M.2    Kash, S.F.3
  • 85
    • 0031759717 scopus 로고    scopus 로고
    • New tool to predict celiac disease on its way to the clinics
    • Sollid LM, Scott H. New tool to predict celiac disease on its way to the clinics. Gastroenterology 1998;115:1584-6.
    • (1998) Gastroenterology , vol.115 , pp. 1584-1586
    • Sollid, L.M.1    Scott, H.2
  • 86
    • 0033011434 scopus 로고    scopus 로고
    • Serum immunoglobulin A from patients with celiac disease inhibits human T84 intestinal crypt epithelial cell differentiation
    • Halttunen T, Maki M. Serum immunoglobulin A from patients with celiac disease inhibits human T84 intestinal crypt epithelial cell differentiation. Gastroenterology 1999;116:566-72.
    • (1999) Gastroenterology , vol.116 , pp. 566-572
    • Halttunen, T.1    Maki, M.2
  • 87
    • 0032775930 scopus 로고    scopus 로고
    • Antibodies to tissue transglutaminase as serologic markers in patients with dermatitis herpetiformis
    • Dieterich W, Laag E, Bruckner-Tuderman L, et al. Antibodies to tissue transglutaminase as serologic markers in patients with dermatitis herpetiformis. J Invest Dermatol 1999;113:133-6.
    • (1999) J Invest Dermatol , vol.113 , pp. 133-136
    • Dieterich, W.1    Laag, E.2    Bruckner-Tuderman, L.3
  • 88
    • 0030615171 scopus 로고    scopus 로고
    • The HLA-A*0201-restricted H-Y antigen contains a posttranslationally modified cysteine that significantly affects T cell recognition
    • Meadows L, Wang W, Den HJ, et al. The HLA-A*0201-restricted H-Y antigen contains a posttranslationally modified cysteine that significantly affects T cell recognition. Immunity 1997;6:273-81.
    • (1997) Immunity , vol.6 , pp. 273-281
    • Meadows, L.1    Wang, W.2    Den, H.J.3
  • 89
    • 0001433072 scopus 로고    scopus 로고
    • An HLA-A2-restricted tyrosinase antigen on melanoma cells results from post-translational modification and suggests a novel pathway for processing of membrane proteins
    • Skipper JC, Hendrickson RC, Gulden PH, et al. An HLA-A2-restricted tyrosinase antigen on melanoma cells results from post-translational modification and suggests a novel pathway for processing of membrane proteins. J Exp Med 1996;183:527-34.
    • (1996) J Exp Med , vol.183 , pp. 527-534
    • Skipper, J.C.1    Hendrickson, R.C.2    Gulden, P.H.3
  • 90
    • 0033555404 scopus 로고    scopus 로고
    • Hepatitis C virus envelope glycoprotein E1 originates in the endoplasmic reticulum and requires cytoplasmic processing for presentation by class I MHC molecules
    • Selby M, Erickson A, Dong C, et al. Hepatitis C virus envelope glycoprotein E1 originates in the endoplasmic reticulum and requires cytoplasmic processing for presentation by class I MHC molecules. J Immunol 1999;162:669-76.
    • (1999) J Immunol , vol.162 , pp. 669-676
    • Selby, M.1    Erickson, A.2    Dong, C.3
  • 91
    • 0033529490 scopus 로고    scopus 로고
    • Isoaspartyl post-translational modification triggers autoimmune responses to self-proteins
    • Mamula MJ, Gee RJ, Elliott JI, et al. Isoaspartyl post-translational modification triggers autoimmune responses to self-proteins. J Biol Chem 1999;274:22321-7.
    • (1999) J Biol Chem , vol.274 , pp. 22321-22327
    • Mamula, M.J.1    Gee, R.J.2    Elliott, J.I.3


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