Western Immunoblotting of Cereal Proteins with Monoclonal Antibodies to Wheat Gliadin to Investigate Coeliac Disease

1988 ◽  
Vol 85 (3) ◽  
pp. 346-350 ◽  
Author(s):  
A.R. Freedman ◽  
G. Galfre ◽  
E. Gal ◽  
H.J. Ellis ◽  
P.J. Ciclitira
Keyword(s):  
Monoclonal Antibodies ◽  
Coeliac Disease ◽  
Western Immunoblotting ◽  
Wheat Gliadin ◽  
Cereal Proteins

TOXICITY OF WHEAT GLIADIN FRACTIONS IN CŒLIAC DISEASE

The Lancet ◽  
1973 ◽  
Vol 301 (7816) ◽  
pp. 1363-1364 ◽  
Author(s):  
R.R.W. Townley ◽  
H.J. Cornell ◽  
P.S. Bhathal ◽  
J.D. Mitchell
Keyword(s):  
Coeliac Disease ◽  
Wheat Gliadin

Chromosomal control of wheat gliadin protein epitopes: analysis with specific monoclonal antibodies

1991 ◽  
Vol 82 (1) ◽  
pp. 44-53 ◽  
Author(s):  
J. H. Skerritt ◽  
O. Martinuzzi ◽  
E. V. Metakovsky
Keyword(s):  
Monoclonal Antibodies ◽  
Wheat Gliadin ◽  
Gliadin Protein

scholarly journals Evaluation of a gluten free product containing wheat gliadin in patients with coeliac disease.

BMJ ◽  
1984 ◽  
Vol 289 (6437) ◽  
pp. 83-83 ◽  
Author(s):  
P J Ciclitira ◽  
H J Ellis ◽  
N L Fagg
Keyword(s):  
Coeliac Disease ◽  
Free Product ◽  
Gluten Free ◽  
Wheat Gliadin

Coeliac Disease: A Rapid Method to Test Wheat Sensitivity

PEDIATRICS ◽  
1956 ◽  
Vol 17 (5) ◽  
pp. 699-699
Keyword(s):  
Celiac Disease ◽  
Coeliac Disease ◽  
Rapid Method ◽  
Tolerance Test ◽  
Skin Tests ◽  
Objective Criterion ◽  
Wheat Sensitivity ◽  
Wheat Gliadin

Skin tests have not proven reliable as a means of determining gastrointestinal sensitivity to wheat. In view of the implication of wheat gliadin in the pathogenesis of celiac disease it becomes desirable to have a convenient, objective criterion of gastrointestinal sensitivity to gliadin. The authors propose a gliadin tolerance test. The patient is given a test dosage of gliadin and the level of glutamine is determined in the blood afterwards at 1, 2, 3, 4, and 5-hour intervals. Normal patients do not show an increase of the glutamine in the blood of more than 50 per cent while children with coeliac disease who do not tolerate gliadin show increases greater than 50 per cent and up to fourfold increases.

Relation of antigenic structure of cereal proteins to their toxicity in coeliac patients

1985 ◽  
Vol 53 (1) ◽  
pp. 39-45 ◽  
Author(s):  
P. J. Ciclitira ◽  
H. J. Ellis ◽  
D. J. Evans ◽  
E. S. Lennox
Keyword(s):  
Coeliac Disease ◽  
Competitive Inhibition ◽  
Double Diffusion ◽  
Cross Reactivity ◽  
Antigenic Structure ◽  
Partial Identity ◽  
Cereal Proteins

1. Unfractionated gliadin and its α-, β-, γ- and ω-gliadin subfractions were used as rabbit immunogens. The antisera were characterized by (1) Ouchterlony double diffusion, (2) binding of 125I-labelled gliadin subfractions, (3) inhibition by several gliadin subfractions of binding between γgliadin antiserum and 125I-labeIled γgliadin.2. Double diffusion showed identical cross-reactivity between the antisera and the gliadin subfractions with the exception of ω-gliadin. Precipitin lines of partial identity with gliadin were observed against rye secalins and barley hordeins but not oat avenins or maize zeins.3. Binding was observed between unfractionated 125I-labelledα-, β-, γ- and ω-gliadins and all the antisera. There was binding of 125I-labelled ω-gliadin to the ω-gliadin antiserum but poor binding of 125I-labelled ω-gliadin to unfractionated α-, β- and γ-gliadin antisera. Competitive inhibition of binding between 125I-labelled γ-gliadin and γ-gliadin antiserum diluted 1:250 (v/v) demonstrated similar competition between α-, β- and γ-gliadins and this antiserum but poor competition between ω-gliadin, wheat glutenins, albumins and globulins, rye secalins, barley hordeins and oat avenins.4. These findings suggest that there is a good correlation between the antigenic structure of gliadin proteins and their toxicity to patients with coeliac disease.

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