6533b857fe1ef96bd12b42a4

RESEARCH PRODUCT

Antitumor Vaccines Based on Synthetic Mucin Glycopeptides

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The interest in tumor-associated glycoconjugate antigens was particularly initiated by Springer, who published in 1984 that glycoproteins on the outer cell-membrane of epithelial tumor cells have an altered glycosylation consisting of the Thomsen-Friedenreich (T-) antigen and its precursor the TN-antigen structure (Springer 1984). He and his coworkers also had found that monoclonal antibodies induced with glycoproteins from tumor cell membranes showed cross-reactivity to desialylated glycophorin A. It was concluded from these observations that the T-and TN-glycoproteins on the epithelial tumor cells must be structurally related to asialoglycophorin A (Springer et al. 1983) (Fig. 11.1a). Glycophorin A is the major sialoglycoprotein on erythrocytes. In the N-terminal domain it contains cryptic T-antigen structures which are covered by sialylation in the 3′- and 6-position. The glycophorin exists in two blood group specificities M and N, which have identical glycoforms, but differ in two of the total 131 amino acids.