Wheat peptide challenge in coeliac disease
References (25)
Gluten, major histocompatibility complex, and the small intestine
Gastroenterology
(1992)- et al.
Gluten-induced enteropathy. The effect of partially digested gluten
Lancet
(1959) - et al.
In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease
Gastroenterology
(1988) - et al.
Cell-mediated immunity to a synthetic gliadin peptide resembling a sequence from adenovirus 12
Lancet
(1987) Celiac sprue
N Engl J Med
(1991)- et al.
Coeliac disease IV. An investigation into the injurious constituents of wheat in connection with their action on patients with coeliac disease
Acta Paediatr
(1953) - et al.
Evidence for a primary association of celiac disease to a particular HLA-DQ α/β heterodimer
J Exp Med
(1989) - et al.
Gliadin-specific, HLA-DQ(α1*0501,β1*0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients
J Exp Med
(1993) - Ha Gjertsen, Kea Lundin, Lm Sollid, Ja Eriksen, E. Thorsby, T cells recognize a peptide derived from α-gliadin...
- et al.
An in vitro model of gluten sensitive enteropathy. Effect of gliadin on intestinal epithelial cells of patients with gluten sensitivity enteropathy in organ culture
J Clin Invest
(1974)
Coeliac activity of gliadin peptides CT-1 and CT-2
Z Lebensm Unters Forsch
(1986)
Possible role of a human adenovirus in the pathogenesis of coeliac disease
J Exp Med
(1984)
Cited by (243)
The gliadin p31–43 peptide: Inducer of multiple proinflammatory effects
2021, International Review of Cell and Molecular BiologyThe chemistry and biochemistry of wheat
2020, Breadmaking: Improving QualityPossibility of minimizing gluten intolerance by co-consumption of some fruits – A case for positive food synergy?
2019, Trends in Food Science and TechnologyCereals for developing gluten-free products and analytical tools for gluten detection
2014, Journal of Cereal ScienceThe versatile role of gliadin peptides in celiac disease
2013, Clinical BiochemistryA combination of two lactic acid bacteria improves the hydrolysis of gliadin during wheat dough fermentation
2012, Food MicrobiologyCitation Excerpt :They are divided according to their solubility properties into two major groups: gliadins and glutenins, the first one being involved in the celiac disease (Sollid and Khosla, 2005). Several residues of the N-terminus of α-gliadin are immunologically active, e.g., amino acids at position 31–43, 62–75 and 57–89 in the protein (Gerez et al., 2008) causing an inflammatory response of the small intestinal mucosa (Sturgess et al., 1994; Arentz-Hansen et al., 2000; Shan et al., 2002). The large proportion and location of proline (P) residues in these toxic peptides make them extremely resistant to proteolysis (Stepniak et al., 2006), thus specific peptidases are necessary to hydrolyze the cyclic structure of P (Hausch et al., 2002).
Copyright © 1994 Published by Elsevier Ltd.