Fernando G. Ghirdo, Eduardo Arranz Sanz
Storage proteins from wheat kernels are the base of a wide variety ofhomemade and industrial food products. Nonetheless, for a group ofindividuals (celiac disease (CD) patients), these proteins are toxic.Gliadins and glutenins from wheat, as well as their counterparts inbarley and rye, also called prolamins, are evolutionary related, andpresent a high degree of homology.Polyclonal and monoclonal antibodies raised against prolamins have beena very useful tool to characterise structural and conformational features ofprolamins, and particularly, for gluten analysis based on immunochemicaltechniques. Complete adherence to a gluten-free diet is required to recoverthe normal histology of the small intestine in CD patients. To this end, theuse of certified gluten-free products is mandatory.Aqueous solvents such as 60-70% ethanol, have been used forextraction of prolamins from flours and food. This method is notselective and, therefore, results in complex mixtures of proteins whichtogether with their low solubility in aqueous solutions, high degree ofhomology, and consequently crossreactivity, produce some drawbacksin gluten analysis by immunoassays. Prolamins drive an exacerbated immune response in intestinalmucosa of CD patients. T lymphocytes are a central piece in CDpathogenesis. However, new insights in the knowledge of innateimmunity point out to some gliadin peptides which can also producestructural changes in the intestine as well as inflammatory reactions.
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