Author(s): Smorodin EP, Kurtenkov OA, Sergeyev BL, Branovets JS, Izotova JG,
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Abstract Changes in the glycosylation in cancer may lead to an aberrant expression of A, B incompatible or xenogeneic blood group related antigens. To characterize the specificity of IgG antibodies to A, B, and related glycans in sera of gastrointestinal cancer patients, serum probes and affinity-isolated antibodies were analyzed in the indirect and competitive ELISA using a set of homogenous polyacrylamide (PAA) glycoconjugates. Monoreactive antibodies recognizing A(di) (I) and cross-reactive antibodies to A(di)/B(di)/B(tri) (II) or A(di)/A(tri)/Fs(di)/Core5 (III) were affinity-isolated on A(di)-PAA-Sepharose. The population I showed a higher affinity to A(di)-PAA than cross-reactive antibodies. The antibodies II were more specific to B(di) and may belong to the core alpha-Gal reactive antibodies but are also capable of recognizing A(di). The antibodies III were more specific to A(tri); they agglutinated A-erythrocytes and belong to anti-A isoantibodies reactive to xenogeneic oligosaccharides. The purified antibody samples were non- or faintly reactive to Tn. The IC(50) values of PAA glycoconjugates ranged from 6 × 10(-8) to 7 × 10(-6) M. No or weak binding of antibodies to the unrelated antigens used in the detection of polyreactivity (ferritin, casein, and DNA) was observed.
This article was published in J Immunoassay Immunochem
and referenced in Journal of Clinical & Cellular Immunology