Characterization of the binding specificity ofAnguilla anguilla agglutinin (AAA) in comparison toUlex europaeus agglutinin I (UEA-I) |
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Authors: | Stephan E Baldus Juergen Thiele Young-Ok Park Franz-Georg Hanisch Jacques Bara Robert Fischer |
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Institution: | (1) Institute of Pathology, University of Cologne, Joseph-Stelzmann-Str. 9, 50924 Cologne, Germany;(2) Institute of Biochemistry, University of Cologne, Joseph-Stelzmann-Str. 52, 50924 Cologne, Germany;(3) Centre de Recherches Paris Saint-Antoine, 184, rue du Faubourg Saint-Antoine, 75571 Paris Cedex 12, France |
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Abstract: | Using immunochemical and immunohistochemical methods, the binding site ofAnguilla anguilla agglutinin (AAA) was characterized and compared with the related fucose-specific lectin fromUlex europaeus (UEA-I). In solid-phase enzyme-linked immunoassays, the two lectins recognized Fuc1-2Gal-HSA. AAA additionally cross-reacted with neoglycolipids bearing lacto-N-fucopentaose (LNFP) I H type 1] and II Lea] and lactodifucotetraose (LDFT) as glycan moieties. UEA-I, on the other hand, bound to a LDFT-derived neoglycolipid but not to the other neoglycolipids tested. Binding of AAA to gastric mucin was competitively neutralized by Lea-specific monoclonal antibodies. UEA-I binding, on the other hand, was reduced after co-incubation with H type 2- and Ley-specific monoclonal antibodies. According to our results, AAA reacts with fucosylated type 1 chain antigens, whereas UEA-I binds only to the 1-2-fucosylated LDFT-derived neoglycolipid. In immunohistochemical studies, the reactivity of AAA and UEA-I in normal pyloric mucosa from individuals with known Lewis and secretor status was analysed. AAA showed a broad reaction in the superficial pyloric mucosa from secretors and non-secretors, but AAA reactivity was more pronounced in Le(a+b-) individuals. On the other hand, UEA-I stained the superficial pyloric mucosa only from secretor individuals. A staining of deep mucous glands by the lectins was found in all specimens. Both reacted with most human carcinomas of different origin. Slight differences in their binding pattern were observed and may be explained by the different fine-specificities of the lectins. |
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Keywords: | lectin Anguilla anguilla agglutinin carbohydrate antigen tumour-associated antigen |
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