메뉴 건너뛰기




Volumn 1762, Issue 1, 2006, Pages 80-93

VSL#3 probiotic preparation has the capacity to hydrolyze gliadin polypeptides responsible for Celiac Sprue

Author keywords

CD3 +; Celiac Sprue; Gliadin; Probiotic; Proteolysis; Wheat flour; Zonulin

Indexed keywords

ANTIBODY; EPITOPE; F ACTIN; GLIADIN; POLYPEPTIDE; PROBIOTIC AGENT;

EID: 29644441042     PISSN: 09254439     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbadis.2005.09.008     Document Type: Article
Times cited : (199)

References (61)
  • 1
    • 0035109676 scopus 로고    scopus 로고
    • Current approaches to diagnosis and treatment of celiac disease: An evolving spectrum
    • A. Fasano, and C. Catassi Current approaches to diagnosis and treatment of celiac disease: an evolving spectrum Gastroenterology 120 2001 636 651
    • (2001) Gastroenterology , vol.120 , pp. 636-651
    • Fasano, A.1    Catassi, C.2
  • 5
    • 29644442157 scopus 로고    scopus 로고
    • The Consequences of obesity and recognition of celiac disease-Two growing concerns worldwide
    • W.F. Balestrieri The Consequences of obesity and recognition of celiac disease-Two growing concerns worldwide Medscape Gastroenterol. 6 2004 1
    • (2004) Medscape Gastroenterol. , vol.6 , pp. 1
    • Balestrieri, W.F.1
  • 6
    • 0041669320 scopus 로고    scopus 로고
    • Celiac disease
    • H.R.P. Green, and B. Jabri Celiac disease Lancet 362 2003 383 391
    • (2003) Lancet , vol.362 , pp. 383-391
    • Green, H.R.P.1    Jabri, B.2
  • 8
    • 0042635667 scopus 로고    scopus 로고
    • Bioactive antinutritional peptides derived from cereal prolamines: A review
    • M. Silano, and M. De Vincenzi Bioactive antinutritional peptides derived from cereal prolamines: a review Nahrung 43 1999 175 184
    • (1999) Nahrung , vol.43 , pp. 175-184
    • Silano, M.1    De Vincenzi, M.2
  • 10
    • 0032740185 scopus 로고    scopus 로고
    • 31-43 amino acid sequence of the a-gliadin induces anti-endomysial antibody production during in vitro challenge
    • A. Picarelli, L. Di Tola, M. Sabbatella, R. Greco, M. Silano, and M. De Vincenzi 31-43 amino acid sequence of the a-gliadin induces anti-endomysial antibody production during in vitro challenge Scand. J. Gastroenterol. 34 1999 1099 1102
    • (1999) Scand. J. Gastroenterol. , vol.34 , pp. 1099-1102
    • Picarelli, A.1    Di Tola, L.2    Sabbatella, M.3    Greco, R.4    Silano, M.5    De Vincenzi, M.6
  • 12
    • 0034771195 scopus 로고    scopus 로고
    • Celiac disease: Antibody recognition against native and selectively deaminated gliadin peptides
    • M. Aleanzi, A.M. Demonte, C. Esper, S. Garcilazo, and M. Waggener Celiac disease: antibody recognition against native and selectively deaminated gliadin peptides Clin. Chem. 47 2001 2023 2028
    • (2001) Clin. Chem. , vol.47 , pp. 2023-2028
    • Aleanzi, M.1    Demonte, A.M.2    Esper, C.3    Garcilazo, S.4    Waggener, M.5
  • 14
    • 0031689618 scopus 로고    scopus 로고
    • Gliadin activates mucosal cell mediated immunità in cultured rectal mucosa from coeliac patients and a subset of their siblings
    • R. Troncone, G. Mazzarella, N. Leone, M. Mayer, M. De Vincenzi, L. Greco, and S. Auricchio Gliadin activates mucosal cell mediated immunità in cultured rectal mucosa from coeliac patients and a subset of their siblings Gut 43 1998 484 489
    • (1998) Gut , vol.43 , pp. 484-489
    • Troncone, R.1    Mazzarella, G.2    Leone, N.3    Mayer, M.4    De Vincenzi, M.5    Greco, L.6    Auricchio, S.7
  • 15
    • 0029963596 scopus 로고    scopus 로고
    • Definition of initial immunologic modifications upon in vitro challenge in the small intestine of celiac patients
    • L. Maiuri, A. Picarelli, and M. Boirivant Definition of initial immunologic modifications upon in vitro challenge in the small intestine of celiac patients Gastroenterology 110 1996 1368 1378
    • (1996) Gastroenterology , vol.110 , pp. 1368-1378
    • Maiuri, L.1    Picarelli, A.2    Boirivant, M.3
  • 17
    • 0034508690 scopus 로고    scopus 로고
    • Human zonulin, a potential modulator of intestinal tight junctions
    • W. Wang, S. Uzzau, S.E. Goldblum, and A. Fasano Human zonulin, a potential modulator of intestinal tight junctions J. Cell. Sci. 113 2000 4435 4440
    • (2000) J. Cell. Sci. , vol.113 , pp. 4435-4440
    • Wang, W.1    Uzzau, S.2    Goldblum, S.E.3    Fasano, A.4
  • 18
    • 0034728821 scopus 로고    scopus 로고
    • Zonulin, a newly discovered modulator of intestinal permeability, and its expression in celiac disease
    • A. Fasano, T. Not, W. Wang, S. Uzzau, I. Berti, A. Tommasini, and S.E. Goldblum Zonulin, a newly discovered modulator of intestinal permeability, and its expression in celiac disease Lancet 335 2000 1518 1519
    • (2000) Lancet , vol.335 , pp. 1518-1519
    • Fasano, A.1    Not, T.2    Wang, W.3    Uzzau, S.4    Berti, I.5    Tommasini, A.6    Goldblum, S.E.7
  • 19
    • 0034254559 scopus 로고    scopus 로고
    • Chlamydia trachomatis infection of epithelial cells induces the activation of caspase-1 and release of mature IL-18
    • H. Lu, C. Shen, and R.C. Brunham Chlamydia trachomatis infection of epithelial cells induces the activation of caspase-1 and release of mature IL-18 J. Immunol. 165 2000 1463 1469
    • (2000) J. Immunol. , vol.165 , pp. 1463-1469
    • Lu, H.1    Shen, C.2    Brunham, R.C.3
  • 21
    • 0031798042 scopus 로고    scopus 로고
    • The sourdough microflora: Interactions between lactic acid bacteria and yeasts
    • M. Gobbetti The sourdough microflora: interactions between lactic acid bacteria and yeasts Trends Food Sci. Technol. 9 1998 267 274
    • (1998) Trends Food Sci. Technol. , vol.9 , pp. 267-274
    • Gobbetti, M.1
  • 23
    • 0036172626 scopus 로고    scopus 로고
    • Probiotics: Potential pharmaceutical applications
    • I.P. Kaur, K. Chopra, and A. Saini Probiotics: potential pharmaceutical applications Eur. J. Pharm. Sci. 15 2002 1 9
    • (2002) Eur. J. Pharm. Sci. , vol.15 , pp. 1-9
    • Kaur, I.P.1    Chopra, K.2    Saini, A.3
  • 24
    • 0032907877 scopus 로고    scopus 로고
    • Probiotics in inflammatory bowel disease: New insight to pathogenesis or a possible therapeutic alternative?
    • P. Gionchetti, and M. Campieri Probiotics in inflammatory bowel disease: new insight to pathogenesis or a possible therapeutic alternative? Gastroenterology 116 1999 1246 1249
    • (1999) Gastroenterology , vol.116 , pp. 1246-1249
    • Gionchetti, P.1    Campieri, M.2
  • 27
    • 0027317945 scopus 로고
    • Electrophoretic characterization of wheat grain allergens from different cultivars involved in bakers' asthma
    • W. Weiss, C. Volgelmeier, and A. Gorg Electrophoretic characterization of wheat grain allergens from different cultivars involved in bakers' asthma Electrophoresis 14 1993 805 816
    • (1993) Electrophoresis , vol.14 , pp. 805-816
    • Weiss, W.1    Volgelmeier, C.2    Gorg, A.3
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K. Laemmli Cleavage of structural proteins during the assembly of the head of bacteriophage T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 33
    • 0029810854 scopus 로고    scopus 로고
    • The proteolytic system of Lactobacillus sanfrancisco CB1: Purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase
    • M. Gobbetti, E. Smacchi, and A. Corsetti The proteolytic system of Lactobacillus sanfrancisco CB1: purification and characterization of a proteinase, a dipeptidase, and an aminopeptidase Appl. Environ. Microbiol. 62 1996 3220 3226
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3220-3226
    • Gobbetti, M.1    Smacchi, E.2    Corsetti, A.3
  • 34
    • 33751330608 scopus 로고
    • The determination of enzyme dissociation constants
    • H. Lineweaver, and D. Burk The determination of enzyme dissociation constants J. Am. Chem. Soc. 56 1934 658 666
    • (1934) J. Am. Chem. Soc. , vol.56 , pp. 658-666
    • Lineweaver, H.1    Burk, D.2
  • 35
    • 4644256651 scopus 로고    scopus 로고
    • Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo
    • J.L. Piper, G.M. Gray, and C. Khosla Effect of prolyl endopeptidase on digestive-resistant gliadin peptides in vivo J. Pharmacol. Exp. Ther. 311 2004 213 219
    • (2004) J. Pharmacol. Exp. Ther. , vol.311 , pp. 213-219
    • Piper, J.L.1    Gray, G.M.2    Khosla, C.3
  • 36
    • 0034849988 scopus 로고    scopus 로고
    • Modification of wheat flour proteins during in vivo digestion of bread dough, crumb and crust: An electrophoretic and immunological study
    • G. Pasini, M. Simonato, M. Giannattasio, A.D.B. Peruffo, and A. Curioni Modification of wheat flour proteins during in vivo digestion of bread dough, crumb and crust: an electrophoretic and immunological study J. Agric. Food Chem. 49 2001 2254 2259
    • (2001) J. Agric. Food Chem. , vol.49 , pp. 2254-2259
    • Pasini, G.1    Simonato, M.2    Giannattasio, M.3    Peruffo, A.D.B.4    Curioni, A.5
  • 37
    • 0037726720 scopus 로고    scopus 로고
    • Innovative approach to low-level gluten determination in foods using a novel sandwich enzyme-linked immunosorbent assay protol
    • I. Valdés, E. Garcia, M. Lorente, and E. Méndez Innovative approach to low-level gluten determination in foods using a novel sandwich enzyme-linked immunosorbent assay protol Eur. J. Gastroenterol. Hepatol. 15 2003 465 474
    • (2003) Eur. J. Gastroenterol. Hepatol. , vol.15 , pp. 465-474
    • Valdés, I.1    Garcia, E.2    Lorente, M.3    Méndez, E.4
  • 38
    • 0042856251 scopus 로고    scopus 로고
    • New strategy for the determination of gliadins in maize-or-based foods matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: Fractionation of gliadins from maize or rice prolamins by acidic treatment
    • A. Hernando, I. Valdes, and E. Mendez New strategy for the determination of gliadins in maize-or-based foods matrix-assisted laser desorption/ionization time-of-flight mass spectrometry: fractionation of gliadins from maize or rice prolamins by acidic treatment J. Mass Spectrom. 38 2003 862 871
    • (2003) J. Mass Spectrom. , vol.38 , pp. 862-871
    • Hernando, A.1    Valdes, I.2    Mendez, E.3
  • 39
    • 0020438607 scopus 로고
    • Effect of gliadin peptides prepared from hexaploid and tetraploid wheat on cultures of intestine from rat fetuses and coeliac children
    • S. Auricchio, G. De Ritis, M. De Vincenzi, P. Occorsio, and V. Silano Effect of gliadin peptides prepared from hexaploid and tetraploid wheat on cultures of intestine from rat fetuses and coeliac children Pediatr. Res. 16 1982 1004 1010
    • (1982) Pediatr. Res. , vol.16 , pp. 1004-1010
    • Auricchio, S.1    De Ritis, G.2    De Vincenzi, M.3    Occorsio, P.4    Silano, V.5
  • 40
    • 0036154310 scopus 로고    scopus 로고
    • Proteolysis by sourdough lactic acid bacteria: Effects on wheat flour protein fractions and gliadin peptides involved in human cereal intolerance
    • R. Di Cagno, M. De Angelis, P. Lavermicocca, M. De Vincenzi, C. Giovannini, M. Faccia, and M. Gobbetti Proteolysis by sourdough lactic acid bacteria: effects on wheat flour protein fractions and gliadin peptides involved in human cereal intolerance Appl. Environ. Microbiol. 68 2002 623 633
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 623-633
    • Di Cagno, R.1    De Angelis, M.2    Lavermicocca, P.3    De Vincenzi, M.4    Giovannini, C.5    Faccia, M.6    Gobbetti, M.7
  • 42
    • 0029899086 scopus 로고    scopus 로고
    • Relation between gliadin structure and coeliac toxicity
    • H. Wieser Relation between gliadin structure and coeliac toxicity Acta Paediatr. 412 1996 3 9
    • (1996) Acta Paediatr. , vol.412 , pp. 3-9
    • Wieser, H.1
  • 44
  • 45
    • 0002256039 scopus 로고
    • Cereal's proteins and celiac disease
    • M. Marsh Blackwell Scientific Publications Oxford
    • P. Shewry, A. Tatham, and D. Kasada Cereal's proteins and celiac disease M. Marsh Coeliac Disease 1992 Blackwell Scientific Publications Oxford 305 348
    • (1992) Coeliac Disease , pp. 305-348
    • Shewry, P.1    Tatham, A.2    Kasada, D.3
  • 47
    • 0036829115 scopus 로고    scopus 로고
    • Host-dependent zonulin secretion causes the impairment of the small intestine barrier function after bacterial exposure
    • R.E. Asmar, P. Panigrahi, P. Bamford, I. Berti, I. Not, G.V. Coppa, C. Catassi, and A. Fasano Host-dependent zonulin secretion causes the impairment of the small intestine barrier function after bacterial exposure Gastroenterology 123 2002 1607 1615
    • (2002) Gastroenterology , vol.123 , pp. 1607-1615
    • Asmar, R.E.1    Panigrahi, P.2    Bamford, P.3    Berti, I.4    Not, I.5    Coppa, G.V.6    Catassi, C.7    Fasano, A.8
  • 48
    • 0015993561 scopus 로고
    • An in vitro model of gluten sensitive enteropathy: Effect of gliadin on intestinal epithelial cells of patients with gluten sensitive enteropathy in organ culture
    • Z.M. Falchuk, R.L. Gebhard, C. Sessoms, and W. Strober An in vitro model of gluten sensitive enteropathy: effect of gliadin on intestinal epithelial cells of patients with gluten sensitive enteropathy in organ culture J. Clin. Investig. 53 1974 487 500
    • (1974) J. Clin. Investig. , vol.53 , pp. 487-500
    • Falchuk, Z.M.1    Gebhard, R.L.2    Sessoms, C.3    Strober, W.4
  • 49
    • 20744433420 scopus 로고    scopus 로고
    • Is prolyl-endopeptidase effective in the detoxification of gliadin peptides in celiac disease?
    • T. Matysiak-Budnik, C. Candalh, and C. Dugave Is prolyl-endopeptidase effective in the detoxification of gliadin peptides in celiac disease? J. Pediatr. Gastroenterol. Nutr. 39 2004 s53
    • (2004) J. Pediatr. Gastroenterol. Nutr. , vol.39 , pp. 53
    • Matysiak-Budnik, T.1    Candalh, C.2    Dugave, C.3
  • 50
    • 11844263978 scopus 로고    scopus 로고
    • Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: Chemical and immunological characterization
    • T. Marti, O. Molberg, Q. Li, G.M. Gray, C. Khosla, and L.M. Sollid Prolyl endopeptidase-mediated destruction of T cell epitopes in whole gluten: chemical and immunological characterization J. Pharmacol. Exp. Ther. 312 2005 19 26
    • (2005) J. Pharmacol. Exp. Ther. , vol.312 , pp. 19-26
    • Marti, T.1    Molberg, O.2    Li, Q.3    Gray, G.M.4    Khosla, C.5    Sollid, L.M.6
  • 52
    • 23644431629 scopus 로고    scopus 로고
    • Gliadin induces increased intestinal permeability, zonulin release, and occludin down-regulation in an ex-vivo human intestinal model of celiac disease
    • S. Drago, R.E. Asmar, C. D'Agate, G. Iacono, M. Di Pierro, C. Catassi, and A. Fasano Gliadin induces increased intestinal permeability, zonulin release, and occludin down-regulation in an ex-vivo human intestinal model of celiac disease Gastroenterology 124 2003 658
    • (2003) Gastroenterology , vol.124 , pp. 658
    • Drago, S.1    Asmar, R.E.2    D'Agate, C.3    Iacono, G.4    Di Pierro, M.5    Catassi, C.6    Fasano, A.7
  • 53
    • 0023754841 scopus 로고
    • Transglutaminase activity along the rat small bowel and cellular location
    • G. D'Argenio, I. Sorrentini, C. Ciacci, and G. Mazzacca Transglutaminase activity along the rat small bowel and cellular location Enzyme 39 1988 227 230
    • (1988) Enzyme , vol.39 , pp. 227-230
    • D'Argenio, G.1    Sorrentini, I.2    Ciacci, C.3    Mazzacca, G.4
  • 55
    • 1642274741 scopus 로고    scopus 로고
    • Functional modulation of enterocytes by gram-positive gram-negative microorganisms
    • J.M. Otte, and D.K. Podolsky Functional modulation of enterocytes by gram-positive gram-negative microorganisms Am. J. Physiol.: Gastrointest. Liver. Physiol. 286 2004 G613 G626
    • (2004) Am. J. Physiol.: Gastrointest. Liver. Physiol. , vol.286
    • Otte, J.M.1    Podolsky, D.K.2
  • 56
    • 7444244435 scopus 로고    scopus 로고
    • Commensal bacteria in the gut: Learning who our friends are
    • Y. Fang, and D.B. Polka Commensal bacteria in the gut: learning who our friends are Curr. Opin. Gastroenterol. 20 2004 565 571
    • (2004) Curr. Opin. Gastroenterol. , vol.20 , pp. 565-571
    • Fang, Y.1    Polka, D.B.2
  • 57
    • 0037214515 scopus 로고    scopus 로고
    • An immunodominant DQ8 restricted gliadin peptide activates small intestinal immune response in in vitro cultured mucosa from HLA-DQ8 positive but not HLA-DQ8 negative celiac patients
    • G. Mazzarella, M. Maglio, F. Paparo, G. Nardone, R. Stefanile, L. Greco, Y. Van de Wal, Y. Kooi, F. Koning, S. Auricchio, and R. Troncone An immunodominant DQ8 restricted gliadin peptide activates small intestinal immune response in in vitro cultured mucosa from HLA-DQ8 positive but not HLA-DQ8 negative celiac patients Gut 52 2005 57 62
    • (2005) Gut , vol.52 , pp. 57-62
    • Mazzarella, G.1    Maglio, M.2    Paparo, F.3    Nardone, G.4    Stefanile, R.5    Greco, L.6    Van De Wal, Y.7    Kooi, Y.8    Koning, F.9    Auricchio, S.10    Troncone, R.11
  • 58
    • 0023698166 scopus 로고
    • Stimulation of mucosal T cells in situ with anti CD3 antibody location of the activated T cells and their distribution within the mucosal micro-environment
    • T. Monk, J.O. Spencer, N. Cerf-Bensussan, and T.T. MacDonald Stimulation of mucosal T cells in situ with anti CD3 antibody location of the activated T cells and their distribution within the mucosal micro-environment Clin. Exp. Immunol. 74 1988 216 222
    • (1988) Clin. Exp. Immunol. , vol.74 , pp. 216-222
    • Monk, T.1    Spencer, J.O.2    Cerf-Bensussan, N.3    MacDonald, T.T.4
  • 59
    • 2342449224 scopus 로고    scopus 로고
    • Colonization and immunomodulation by Lactobacillus reuteri ATCC 55730 in the human gastrointestinal tract
    • N. Valeur, P. Engel, N. Carbajal, E. Connolly, and K. Ladefoged Colonization and immunomodulation by Lactobacillus reuteri ATCC 55730 in the human gastrointestinal tract Appl. Environ. Microbiol. 70 2004 1176 1181
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 1176-1181
    • Valeur, N.1    Engel, P.2    Carbajal, N.3    Connolly, E.4    Ladefoged, K.5
  • 60
    • 2342625255 scopus 로고    scopus 로고
    • Permanent colonization by Lactobacillus casei is hindered by the low rate of cell division in mouse gut
    • Y.K. Lee, P.S. Ho, C.S. Low, H. Arvilommi, and S. Salminen Permanent colonization by Lactobacillus casei is hindered by the low rate of cell division in mouse gut Appl. Environ. Microbiol. 70 2004 670 674
    • (2004) Appl. Environ. Microbiol. , vol.70 , pp. 670-674
    • Lee, Y.K.1    Ho, P.S.2    Low, C.S.3    Arvilommi, H.4    Salminen, S.5
  • 61
    • 2442660453 scopus 로고    scopus 로고
    • Effect of the adaptation to high bile salts concentrations on glycosidic activity, survival at low pH and cross-resistance to bile salts in Bifidobacterium
    • L. Noriega, M. Gueimonde, B. Sànchez, A. Margolles, and C.G. de los Reyes-Gavilàn Effect of the adaptation to high bile salts concentrations on glycosidic activity, survival at low pH and cross-resistance to bile salts in Bifidobacterium Int. J. Food. Microbiol. 94 2004 79 86
    • (2004) Int. J. Food. Microbiol. , vol.94 , pp. 79-86
    • Noriega, L.1    Gueimonde, M.2    Sànchez, B.3    Margolles, A.4    De Los Reyes-Gavilàn, C.G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.