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Volumn 109, Issue 5, 2014, Pages 748-756

Novel role of the serine protease inhibitor elafin in gluten-related disorders

Author keywords

[No Author keywords available]

Indexed keywords

ELAFIN; GLIADIN; GLUTEN; PROTEIN GLUTAMINE GAMMA GLUTAMYLTRANSFERASE 2; PROTEIN ZO1;

EID: 84899919523     PISSN: 00029270     EISSN: 15720241     Source Type: Journal    
DOI: 10.1038/ajg.2014.48     Document Type: Article
Times cited : (55)

References (46)
  • 1
    • 79952340540 scopus 로고    scopus 로고
    • Editorial: Can gluten contribute to irritable bowel syndrome
    • Verdu EF. Editorial: can gluten contribute to irritable bowel syndrome. Am J Gastroenterol 2011; 106: 516-8.
    • (2011) Am J Gastroenterol , vol.106 , pp. 516-518
    • Verdu, E.F.1
  • 2
    • 67349226415 scopus 로고    scopus 로고
    • Between celiac disease and irritable bowel syndrome: The "no man's land" of gluten sensitivity
    • Verdu EF, Armstrong D, Murray JA. Between celiac disease and irritable bowel syndrome: the "no man's land" of gluten sensitivity. Am J Gastroenterol 2009; 104: 1587-94.
    • (2009) Am J Gastroenterol , vol.104 , pp. 1587-1594
    • Verdu, E.F.1    Armstrong, D.2    Murray, J.A.3
  • 3
    • 79952362194 scopus 로고    scopus 로고
    • Gluten causes gastrointestinal symptoms in subjects without celiac disease: A double-blind randomized placebo-controlled trial
    • Biesiekierski JR, Newnham ED, Irving PM et al. Gluten causes gastrointestinal symptoms in subjects without celiac disease: a double-blind randomized placebo-controlled trial. Am J Gastroenterol 2011; 106: 508-14.
    • (2011) Am J Gastroenterol , vol.106 , pp. 508-514
    • Biesiekierski, J.R.1    Newnham, E.D.2    Irving, P.M.3
  • 4
    • 84871135111 scopus 로고    scopus 로고
    • The Oslo definitions for coeliac disease and related terms
    • Ludvigsson JF, Leffler DA, Bai JC et al. The Oslo definitions for coeliac disease and related terms. Gut 2013; 62: 43-52.
    • (2013) Gut , vol.62 , pp. 43-52
    • Ludvigsson, J.F.1    Leffler, D.A.2    Bai, J.C.3
  • 5
    • 84856207904 scopus 로고    scopus 로고
    • The copolymer P(HEMA-co-SS) binds gluten and reduces immune response in gluten-sensitized mice and human tissues
    • Pinier M, Fuhrmann G, Galipeau HJ et al. The copolymer P(HEMA-co-SS) binds gluten and reduces immune response in gluten-sensitized mice and human tissues. Gastroenterology 2012; 142: 316-25.
    • (2012) Gastroenterology , vol.142 , pp. 316-325
    • Pinier, M.1    Fuhrmann, G.2    Galipeau, H.J.3
  • 6
    • 67651171674 scopus 로고    scopus 로고
    • Systematic review: Adherence to a glutenfree diet in adult patients with coeliac disease
    • Hall N, Rubin G, Charnock A. Systematic review: adherence to a glutenfree diet in adult patients with coeliac disease. Aliment Pharmacol Ther 2009; 30: 315-30.
    • (2009) Aliment Pharmacol Ther , vol.30 , pp. 315-330
    • Hall, N.1    Rubin, G.2    Charnock, A.3
  • 7
    • 0642365206 scopus 로고    scopus 로고
    • Celiac diet: Its impact on quality of life
    • Lee A, Newman JM. Celiac diet: its impact on quality of life. J Am Diet Assoc 2003; 103: 1533-5.
    • (2003) J Am Diet Assoc , vol.103 , pp. 1533-1535
    • Lee, A.1    Newman, J.M.2
  • 8
    • 54049096811 scopus 로고    scopus 로고
    • Gluten-free and regular foods: A cost comparison
    • Stevens L, Rashid M. Gluten-free and regular foods: a cost comparison. Can J Diet Pract Res 2008; 69: 147-50.
    • (2008) Can J Diet Pract Res , vol.69 , pp. 147-150
    • Stevens, L.1    Rashid, M.2
  • 9
    • 0242303668 scopus 로고    scopus 로고
    • Perceptions of health-related quality of life of men and women living with coeliac disease
    • Hallert C, Sandlund O, Broqvist M. Perceptions of health-related quality of life of men and women living with coeliac disease. Scand J Caring Sci 2003; 17: 301-7.
    • (2003) Scand J Caring Sci , vol.17 , pp. 301-307
    • Hallert, C.1    Sandlund, O.2    Broqvist, M.3
  • 10
    • 0036148651 scopus 로고    scopus 로고
    • Living with coeliac disease: Controlled study of the burden of illness
    • Hallert C, Granno C, Hulten S et al. Living with coeliac disease: controlled study of the burden of illness. Scand J Gastroenterol 2002; 37: 39-42.
    • (2002) Scand J Gastroenterol , vol.37 , pp. 39-42
    • Hallert, C.1    Granno, C.2    Hulten, S.3
  • 11
    • 81355138867 scopus 로고    scopus 로고
    • Impact of coeliac disease on dietary habits and quality of life
    • Black J, Orfila C. Impact of coeliac disease on dietary habits and quality of life. J Hum Nutr Diet 2011; 24: 582-7.
    • (2011) J Hum Nutr Diet , vol.24 , pp. 582-587
    • Black, J.1    Orfila, C.2
  • 12
    • 0027406841 scopus 로고
    • Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin
    • Ying QL, Simon SR. Kinetics of the inhibition of human leukocyte elastase by elafin, a 6-kilodalton elastase-specific inhibitor from human skin. Biochemistry 1993; 32: 1866-74.
    • (1993) Biochemistry , vol.32 , pp. 1866-1874
    • Ying, Q.L.1    Simon, S.R.2
  • 13
    • 0035141593 scopus 로고    scopus 로고
    • Kinetics of the inhibition of proteinase 3 by elafin
    • Ying QL, Simon SR. Kinetics of the inhibition of proteinase 3 by elafin. Am J Respir Cell Mol Biol 2001; 24: 83-9.
    • (2001) Am J Respir Cell Mol Biol , vol.24 , pp. 83-89
    • Ying, Q.L.1    Simon, S.R.2
  • 14
    • 30344465763 scopus 로고    scopus 로고
    • SLPI and elafin: One glove, many fingers
    • Williams S, Brown T, Roghanian A et al. SLPI and elafin: one glove, many fingers. Clin Sci 2006; 110: 21-35.
    • (2006) Clin Sci , vol.110 , pp. 21-35
    • Williams, S.1    Brown, T.2    Roghanian, A.3
  • 15
    • 33947654353 scopus 로고    scopus 로고
    • Attenuated induction of epithelial and leukocyte serine antiproteases elafin and secretory leukocyte protease inhibitor in Crohn's disease
    • Schmid M, Fellermann K, Fritz P et al. Attenuated induction of epithelial and leukocyte serine antiproteases elafin and secretory leukocyte protease inhibitor in Crohn's disease. J Leukoc Biol 2007; 81: 907-15.
    • (2007) J Leukoc Biol , vol.81 , pp. 907-915
    • Schmid, M.1    Fellermann, K.2    Fritz, P.3
  • 16
    • 40649084134 scopus 로고    scopus 로고
    • Real-time PCR quantification analysis of five mucosal transcripts in patients with Crohn's disease
    • Eriksson A, Jennische E, Flach CF et al. Real-time PCR quantification analysis of five mucosal transcripts in patients with Crohn's disease. Eur J Gastroenterol Hepatol 2008; 20: 290-6.
    • (2008) Eur J Gastroenterol Hepatol , vol.20 , pp. 290-296
    • Eriksson, A.1    Jennische, E.2    Flach, C.F.3
  • 17
    • 84868288692 scopus 로고    scopus 로고
    • Food-grade bacteria expressing elafin protect against inflammation and restore colon homeostasis
    • Motta JP, Bermudez-Humaran LG, Deraison C et al. Food-grade bacteria expressing elafin protect against inflammation and restore colon homeostasis. Sci Transl Med 2012; 4: 158ra144.
    • (2012) Sci Transl Med , vol.4
    • Motta, J.P.1    Bermudez-Humaran, L.G.2    Deraison, C.3
  • 18
    • 0029050246 scopus 로고
    • The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope
    • Steinert PM, Marekov LN. The proteins elafin, filaggrin, keratin intermediate filaments, loricrin, and small proline-rich proteins 1 and 2 are isodipeptide cross-linked components of the human epidermal cornified cell envelope. J Biol Chem 1995; 270: 17702-11.
    • (1995) J Biol Chem , vol.270 , pp. 17702-17711
    • Steinert, P.M.1    Marekov, L.N.2
  • 19
    • 79958145057 scopus 로고    scopus 로고
    • Secretory leukocyte protease inhibitor (SLPI) is, like its homologue trappin-2 (pre-elafin), a transglutaminase substrate
    • Baranger K, Zani M, Labas V et al. Secretory leukocyte protease inhibitor (SLPI) is, like its homologue trappin-2 (pre-elafin), a transglutaminase substrate. PloS ONE 2011; 6: e20976.
    • (2011) PloS ONE , vol.6
    • Baranger, K.1    Zani, M.2    Labas, V.3
  • 20
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • Kristiansen C, Madsen L, Fugger L 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
    • Kristiansen, C.1    Madsen, L.2    Fugger, L.3
  • 21
    • 77956916373 scopus 로고    scopus 로고
    • Transglutaminase 2: A multi-functional protein in multiple subcellular compartments
    • Park D, Choi SS, Ha K. Transglutaminase 2: a multi-functional protein in multiple subcellular compartments. Amino Acids 2010; 39: 619-31.
    • (2010) Amino Acids , vol.39 , pp. 619-631
    • Park, D.1    Choi, S.S.2    Ha, K.3
  • 22
    • 77954376606 scopus 로고    scopus 로고
    • Celiac disease serology in patients with Different pretest probabilities: Is biopsy avoidable?
    • Sugai E, Moreno ML, Hwang HJ et al. Celiac disease serology in patients with Different pretest probabilities: Is biopsy avoidable? World J Gastroenterol 2010; 16: 3144-52.
    • (2010) World J Gastroenterol , vol.16 , pp. 3144-3152
    • Sugai, E.1    Moreno, M.L.2    Hwang, H.J.3
  • 23
    • 77951629788 scopus 로고    scopus 로고
    • Dynamics of celiac disease-specific serology aft er initiation of a gluten-free diet and use in the assessment of compliance with treatment
    • Sugai E, Nachman F, Vaquez H et al. Dynamics of celiac disease-specific serology aft er initiation of a gluten-free diet and use in the assessment of compliance with treatment. Dig Liver Dis 2010; 42: 352-8.
    • (2010) Dig Liver Dis , vol.42 , pp. 352-358
    • Sugai, E.1    Nachman, F.2    Vaquez, H.3
  • 24
    • 0000918165 scopus 로고
    • Approaches and limits for accurate mass characterization of large biomolecules
    • Zubarev RA, Demirev PA, Haakansson P et al. Approaches and limits for accurate mass characterization of large biomolecules. Anal Chem 1995; 67: 3793-8.
    • (1995) Anal Chem , vol.67 , pp. 3793-3798
    • Zubarev, R.A.1    Demirev, P.A.2    Haakansson, P.3
  • 25
    • 9644294268 scopus 로고    scopus 로고
    • A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice
    • Marietta E, Black K, Camilleri M et al. A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice. J Clin Invest 2004; 114: 1090-7.
    • (2004) J Clin Invest , vol.114 , pp. 1090-1097
    • Marietta, E.1    Black, K.2    Camilleri, M.3
  • 26
    • 32044441878 scopus 로고    scopus 로고
    • Gliadin stimulation of murine macrophage inflammatory gene expression and intestinal permeability are MyD88-dependent: Role of the innate immune response in Celiac disease
    • Thomas KE, Sapone A, Fasano A et al. Gliadin stimulation of murine macrophage inflammatory gene expression and intestinal permeability are MyD88-dependent: role of the innate immune response in Celiac disease. J Immunol 2006; 176: 2512-21.
    • (2006) J Immunol , vol.176 , pp. 2512-2521
    • Thomas, K.E.1    Sapone, A.2    Fasano, A.3
  • 27
    • 80054738919 scopus 로고    scopus 로고
    • Sensitization to gliadin induces moderate enteropathy and insulitis in nonobese diabetic-DQ8 mice
    • Galipeau HJ, Rulli NE, Jury J et al. Sensitization to gliadin induces moderate enteropathy and insulitis in nonobese diabetic-DQ8 mice. J Immunol 2011; 187: 4338-46.
    • (2011) J Immunol , vol.187 , pp. 4338-4346
    • Galipeau, H.J.1    Rulli, N.E.2    Jury, J.3
  • 28
    • 68149094492 scopus 로고    scopus 로고
    • Host responses to intestinal microbial antigens in gluten-sensitive mice
    • Natividad JM, Huang X, Slack E et al. Host responses to intestinal microbial antigens in gluten-sensitive mice. PLoS ONE 2009; 4: e6472.
    • (2009) PLoS ONE , vol.4
    • Natividad, J.M.1    Huang, X.2    Slack, E.3
  • 29
    • 38349112856 scopus 로고    scopus 로고
    • Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice
    • Verdu EF, Huang X, Natividad J et al. Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice. Am J Physiol Gastrointest Liver Physiol 2008; 294: G217-25.
    • (2008) Am J Physiol Gastrointest Liver Physiol , vol.294
    • Verdu, E.F.1    Huang, X.2    Natividad, J.3
  • 30
    • 84856714131 scopus 로고    scopus 로고
    • Increased bacterial translocation in glutensensitive mice is independent of small intestinal paracellular permeability defect
    • Silva MA, Jury J, Sanz Y et al. Increased bacterial translocation in glutensensitive mice is independent of small intestinal paracellular permeability defect. Dig Dis Sci 2012; 57: 38-47.
    • (2012) Dig Dis Sci , vol.57 , pp. 38-47
    • Silva, M.A.1    Jury, J.2    Sanz, Y.3
  • 31
    • 4043143473 scopus 로고    scopus 로고
    • Intraepithelial lymphocytes in the villous tip: Do they indicate potential coeliac disease?
    • Biagi F, Luinetti O, Campanella J et al. Intraepithelial lymphocytes in the villous tip: do they indicate potential coeliac disease? J Clin Pathol 2004; 57: 835-9.
    • (2004) J Clin Pathol , vol.57 , pp. 835-839
    • Biagi, F.1    Luinetti, O.2    Campanella, J.3
  • 32
    • 79953209715 scopus 로고    scopus 로고
    • Modifying the protease, antiprotease pattern by elafin overexpression protects mice from colitis
    • Motta JP, Magne L, Descamps D et al. Modifying the protease, antiprotease pattern by elafin overexpression protects mice from colitis. Gastroenterology 2011; 140: 1272-82.
    • (2011) Gastroenterology , vol.140 , pp. 1272-1282
    • Motta, J.P.1    Magne, L.2    Descamps, D.3
  • 33
    • 0030787339 scopus 로고    scopus 로고
    • Tridegin, a new peptidic inhibitor of factor XIIIa, from the blood-sucking leech Haementeria ghilianii
    • Finney S, Seale L, Sawyer RT et al. Tridegin, a new peptidic inhibitor of factor XIIIa, from the blood-sucking leech Haementeria ghilianii. Biochem J 1997; 324: 797-805.
    • (1997) Biochem J , vol.324 , pp. 797-805
    • Finney, S.1    Seale, L.2    Sawyer, R.T.3
  • 35
    • 84877579141 scopus 로고    scopus 로고
    • Increasing incidence of celiac disease in a North American population
    • Ludvigsson JF, Rubio-Tapia A, van Dyke CT et al. Increasing incidence of celiac disease in a North American population. Am J Gastroenterol 2013; 108: 818-24.
    • (2013) Am J Gastroenterol , vol.108 , pp. 818-824
    • Ludvigsson, J.F.1    Rubio-Tapia, A.2    Van Dyke, C.T.3
  • 36
    • 72949102295 scopus 로고    scopus 로고
    • Tissue-mediated control of immunopathology in coeliac disease
    • Jabri B, Sollid LM. Tissue-mediated control of immunopathology in coeliac disease. Nat Rev Immunol 2009; 9: 858-70.
    • (2009) Nat Rev Immunol , vol.9 , pp. 858-870
    • Jabri, B.1    Sollid, L.M.2
  • 37
    • 84866121549 scopus 로고    scopus 로고
    • Role of transglutaminase 2 in celiac disease pathogenesis
    • Klöck C, DiRaimondo TR, Khosla C. Role of transglutaminase 2 in celiac disease pathogenesis. Semin Immunopathol 2012; 34: 513-22.
    • (2012) Semin Immunopathol , vol.34 , pp. 513-522
    • Klöck, C.1    Diraimondo, T.R.2    Khosla, C.3
  • 38
    • 84856467615 scopus 로고    scopus 로고
    • Activation and inhibition of transglutaminase 2 in mice
    • Dafik L, Albertelli M, Stamnaes J et al. Activation and inhibition of transglutaminase 2 in mice. PloS ONE 2012; 7: e30642.
    • (2012) PloS ONE , vol.7
    • Dafik, L.1    Albertelli, M.2    Stamnaes, J.3
  • 39
    • 0034843270 scopus 로고    scopus 로고
    • Enterocytic CYP3A4 in a paediatric population: Developmental changes and the effect of coeliac disease and cystic fibrosis
    • Johnson TN, Tanner MS, Taylor CJ et al. Enterocytic CYP3A4 in a paediatric population: developmental changes and the effect of coeliac disease and cystic fibrosis. Br J Clin Pharmacol 2001; 51: 451-60.
    • (2001) Br J Clin Pharmacol , vol.51 , pp. 451-460
    • Johnson, T.N.1    Tanner, M.S.2    Taylor, C.J.3
  • 40
    • 0030053064 scopus 로고    scopus 로고
    • Decreased intestinal CYP3A in celiac disease: Reversal aft er successful gluten-free diet: A potential source of interindividual variability in first-pass drug metabolism
    • Lang CC, Brown RM, Kinirons MT et al. Decreased intestinal CYP3A in celiac disease: reversal aft er successful gluten-free diet: a potential source of interindividual variability in first-pass drug metabolism. Clin Pharmacol Ther 1996; 59: 41-6.
    • (1996) Clin Pharmacol Ther , vol.59 , pp. 41-46
    • Lang, C.C.1    Brown, R.M.2    Kinirons, M.T.3
  • 41
    • 80053351926 scopus 로고    scopus 로고
    • SLPI and trappin-2 as therapeutic agents to target airway serine proteases in inflammatory lung diseases: Current and future directions
    • Zani ML, Tanga A, Saidi A et al. SLPI and trappin-2 as therapeutic agents to target airway serine proteases in inflammatory lung diseases: current and future directions. Biochem Soc Trans 2011; 39: 1441-6.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1441-1446
    • Zani, M.L.1    Tanga, A.2    Saidi, A.3
  • 42
    • 28244491162 scopus 로고    scopus 로고
    • Elafin and its precursor trappin-2 still inhibit neutrophil serine proteinases when they are covalently bound to extracellular matrix proteins by tissue transglutaminase
    • Guyot N, Zani M, Maurel M et al. Elafin and its precursor trappin-2 still inhibit neutrophil serine proteinases when they are covalently bound to extracellular matrix proteins by tissue transglutaminase. Biochemistry 2005; 44: 15610-8.
    • (2005) Biochemistry , vol.44 , pp. 15610-15618
    • Guyot, N.1    Zani, M.2    Maurel, M.3
  • 43
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • Shan L, Molberg Ø, Parrot I et al. Structural basis for gluten intolerance in celiac sprue. Science 2002; 297: 2275-9.
    • (2002) Science , vol.297 , pp. 2275-2279
    • Shan, L.1    Parrot, I.2
  • 44
    • 84859632755 scopus 로고    scopus 로고
    • TG2, a novel extracellular protein with multiple functions
    • Wang Z, Griffin M. TG2, a novel extracellular protein with multiple functions. Amino Acids 2012; 42: 939-49.
    • (2012) Amino Acids , vol.42 , pp. 939-949
    • Wang, Z.1    Griffin, M.2
  • 45
    • 84857059735 scopus 로고    scopus 로고
    • Role of the endogenous elastase inhibitor, elafin, in cardiovascular injury: From epithelium to endothelium
    • Alam SR, Newby DE, Henriksen PA. Role of the endogenous elastase inhibitor, elafin, in cardiovascular injury: from epithelium to endothelium. Biochem Pharmacol 2012; 83: 695-704.
    • (2012) Biochem Pharmacol , vol.83 , pp. 695-704
    • Alam, S.R.1    Newby, D.E.2    Henriksen, P.A.3
  • 46
    • 79952389800 scopus 로고    scopus 로고
    • Co-adjuvant effects of retinoic acid and IL-15 induce inflammatory immunity to dietary antigens
    • DePaolo RW, Abadie V, Tang F et al. Co-adjuvant effects of retinoic acid and IL-15 induce inflammatory immunity to dietary antigens. Nature 2011; 471: 220-4.
    • (2011) Nature , vol.471 , pp. 220-224
    • Depaolo, R.W.1    Abadie, V.2    Tang, F.3


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