Gliadins bind to reticulin in a lectin-like manner.
It has previously been reported that gliadins bind to reticulin in tissue sections. Three lines of evidence are reported in this study which indicate that the gliadins bind to reticulins because they are lectins which bind to sugars expressed on glycoproteins in reticulin and other sites. First, immunofluorescence studies on tissue sections showed that although gliadin binding is largely confined to areas rich in reticulin, it is, nonetheless, also seen in one or two other sites devoid of reticulin. Second, by using fluorescein-labelled lectins of known specificity, it has been shown that the areas to which gliadins bind in tissue sections (including those sites devoid of reticulin) are rich in particular sugars. Third, it has been shown that one of these sugars, alpha-D-mannose, partially inhibited gliadin binding to tissue sections.
D000818:Animals; D002352:Carrier Proteins; D002446:Celiac Disease / Q000276:immunology; D003874:Dermatitis Herpetiformis / Q000276:immunology; D005455:Fluorescent Antibody Technique; D005903:Gliadin / Q000276:immunology / Q000378:metabolism*; D000882:Haplorhini; D006801:Humans; D007421:Intestine, Small / Q000276:immunology; D037102:Lectins / Q000276:immunology / Q000378:metabolism*; D037241:Mannose-Binding Lectins; D010940:Plant Proteins / Q000378:metabolism*; D051381:Rats; D012155:Reticulin / Q000276:immunology / Q000378:metabolism*; D012867:Skin / Q000276:immunology
D002352:Carrier Proteins; D037102:Lectins; D037241:Mannose-Binding Lectins; D010940:Plant Proteins; D012155:Reticulin; D005903:Gliadin