The pathogenesis of coeliac disease

被引：80

作者：

Dewar, D

Pereira, SP

Ciclitira, PJ

机构：

[1] St Thomas Hosp, Rayne Inst, Dept Gastroenterol, London SE1 7EH, England

[2] UCL, Sch Med, Inst Hepatol, London WC1E 6HX, England

来源：

INTERNATIONAL JOURNAL OF BIOCHEMISTRY & CELL BIOLOGY | 2004年 / 36卷 / 01期

关键词：

coeliac disease; pathogenesis; gluten; epitope; HLA-DQ2; tissue transglutaminase;

D O I：

10.1016/S1357-2725(03)00239-5

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Coeliac disease is a chronic enteropathy caused by intolerance to gluten proteins. The true prevalence of this condition is greater than previously thought, with increasing numbers of 'silent' cases being diagnosed. Untreated coeliac disease is associated with significant morbidity and increased mortality. There have been a number of advances in our understanding of the pathogenesis of coeliac disease, in particular the mechanisms whereby gluten epitopes are processed, become modified by tissue transglutaminase (tTG) and then interact with HLA restricted T cells. An improved. understanding of the immune response to gluten is likely to lead to the development of novel strategies for the treatment of coeliac disease. (C) 2003 Elsevier Ltd. All rights reserved.

引用

收藏

页码：17 / 24

页数：8

相关论文

共 25 条

[1] The intestinal T cell response to α-gliadin in adult celiac disease is focused on a single deamidated glutamine targeted by tissue transglutaminase [J].

Arentz-Hansen, H ;

Körner, R ;

Molberg, O ;

Quarsten, H ;

Vader, W ;

Kooy, YMC ;

Lundin, KEA ;

Koning, F ;

Roepstorff, P ;

Sollid, LM ;

McAdam, SN .

JOURNAL OF EXPERIMENTAL MEDICINE, 2000, 191 (04) :603-612

[2] Celiac lesion T cells recognize epitopes that cluster in regions of gliadins rich in proline residues [J].

Arentz-Hansen, H ;

McAdam, SN ;

Molberg, O ;

Fleckenstein, B ;

Lundin, KEA ;

Jorgensen, TJD ;

Jung, G ;

Roepstorff, P ;

Sollid, LM .

GASTROENTEROLOGY, 2002, 123 (03) :803-809

[3] Treatment of experimental encephalomyelitis with a peptide analogue of myelin basic protein [J].

Brocke, S ;

Gijbels, K ;

Allegretta, M ;

Ferber, I ;

Piercy, C ;

Blankenstein, T ;

Martin, R ;

Utz, U ;

Karin, N ;

Mitchell, D ;

Veromaa, T ;

Waisman, A ;

Gaur, A ;

Conlon, P ;

Ling, N ;

Fairchild, PJ ;

Wraith, DC ;

OGarra, A ;

Fathman, CG ;

Steinman, L .

NATURE, 1996, 379 (6563) :343-346

[4] Refractory sprue, coeliac disease, and enteropathy-associated T-cell lymphoma [J].

Cellier, C ;

Delabesse, E ;

Helmer, C ;

Patey, N ;

Matuchansky, C ;

Jabri, B ;

Macintyre, E ;

Cerf-Bensussan, N ;

Brousse, N .

LANCET, 2000, 356 (9225) :203-208

[5] Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function [J].

Clemente, MG ;

De Virgiliis, S ;

Kang, JS ;

Macatagney, R ;

Musu, MP ;

Di Pierro, MR ;

Drago, S ;

Congia, M ;

Fasano, A .

GUT, 2003, 52 (02) :218-223

[6] Mortality in patients with coeliac disease and their relatives:: a cohort study [J].

Corrao, G ;

Corazza, GR ;

Bagnardi, V ;

Brusco, G ;

Ciacci, C ;

Cottone, M ;

Guidetti, CS ;

Usai, P ;

Cesari, P ;

Pelli, MA ;

Loperfido, S ;

Volta, U ;

Calabró, A ;

Certo, M .

LANCET, 2001, 358 (9279) :356-361

[7] Increased expression of mRNA for matrix metalloproteinases-1 and -3 and tissue inhibitor of metalloproteinases-1 in intestinal biopsy specimens from patients with coeliac disease [J].

Daum, S ;

Bauer, U ;

Foss, HD ;

Schuppan, D ;

Stein, H ;

Riecken, EO ;

Ullrich, R .

GUT, 1999, 44 (01) :17-25

[8] CTLA-4 gene polymorphism is associated with predisposition to coeliac disease [J].

Djilali-Saiah, I ;

Schmitz, J ;

Harfouch-Hammoud, E ;

Mougenot, JF ;

Bach, JF ;

Caillat-Zucman, S .

GUT, 1998, 43 (02) :187-189

[9] Investigation of the putative immunodominant T cell epitopes in coeliac disease [J].

Ellis, HJ ;

Pollock, EL ;

Engel, W ;

Fraser, JS ;

Rosen-Bronson, S ;

Wieser, H ;

Ciclitira, PJ .

GUT, 2003, 52 (02) :212-217

[10]

FRASER JS, IN PRESS GUT