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Calreticulin--the potential autoantigen in celiac disease
K Karská1, L Tucková, L Steiner
1Department of Immunology and Gnotobiology, Czech Academy of Sciences, Prague.
Biochemical and Biophysical Research Communications
|April 17, 1995
Summary
Gliadin antibodies cross-react with rat calreticulin, a protein found in enterocytes. This suggests a potential molecular mimicry mechanism in celiac disease pathogenesis.
Area of Science:
- Immunology
- Gastroenterology
- Molecular Biology
Background:
- Monoclonal antibodies targeting gliadin exhibit cross-reactivity with rat enterocytes.
- This cross-reactivity suggests shared epitopes between gliadin and enterocyte components.
Purpose of the Study:
- To identify and characterize the enterocyte molecules recognized by antigliadin antibodies.
- To investigate the potential molecular mimicry between gliadin and intestinal proteins in celiac disease.
Main Methods:
- Affinity chromatography using antigliadin antibodies to isolate enterocyte proteins.
- N-terminal amino acid sequencing and Western blot analysis to identify isolated proteins.
- Competitive enzyme-linked immunosorbent assay (ELISA) using synthetic gliadin peptides and anticalreticulin antibodies.
Main Results:
- Two proteins of 62 and 66 kDa were isolated; the 62 kDa protein was identified as rat calreticulin.
- Antigliadin antibodies recognized rat calreticulin.
- Two specific alpha-gliadin peptides inhibited the binding of anticalreticulin antibodies to rat calreticulin.
- A strong correlation (r = 0.827) was found between IgA anticalreticulin and antigliadin antibodies in celiac patients.
Conclusions:
- Rat calreticulin shares epitopes with gliadin, suggesting molecular mimicry.
- This molecular mimicry may contribute to the autoimmune response in celiac disease.
- Calreticulin is a potential target antigen in gliadin-induced enteropathy.