The oncofetal J28 epitope involves fucosylated O-linked oligosaccharide structures of the fetoacinar pancreatic protein.

The fetoacinar pancreatic protein (FAP), characterized by the mAb J28, is an oncofetal form of bile salt dependent lipase (BSDL), the expression of which is related to pancreatic differentiation and neoplastic processes. Because the J28 epitope, recognized by mAb J28, is suggested to be dependent upon carbohydrates, we have attempted to gain information about the structure of this epitope. Indeed, treatment of FAP with sodium periodate abolished the reactivity of the protein to mAb J28, which demonstrates the implication of oligosaccharides in the structure of the J28 epitope. FAP offers both O-linked and N-linked carbohydrate structures, of which, as we have determined, one is involved. Peptides obtained after cyanogen bromide cleavage were desialylated then separated by affinity chromatography on an immobilized peanut agglutinin agarose column. The peptide retained on this column carried out the reactivity with the mAb J28. Although some differences in amino acid analysis were observed, the N-terminal sequence of this peptide correlates with that of the C-terminal part of the enzyme. Carbohydrate analysis of the peptide bearing the J28 epitope revealed fucose, galactose, N-acetylgalactosamine, N-acetylglucosamine, and N-acetylneuraminic acid. The competition observed between mAb J28 and Ulex europaeus I lectin for binding to the J28 epitope suggested that fucose residue alpha (1-2) linked to a galactose residue was implicated in the structure of the J28 epitope. Alternatively, the loss of the mAb J28 reactivity upon treatment of FAP either with bovine kidney or bovine epididymis fucosidase was observed indicating that fucose residues linked at the alpha (1-2) and alpha (1-6) positions may be involved in the establishment of the structure of the J28 epitope. These observations suggest that mAb J28 recognized a particular fucosylated O-linked oligosaccharide structure located at the mucin-like extended C-terminal part of FAP.