monoclonal antibody 16d10 to the c-terminal domain of the feto-acinar pancreatic protein binds to membrane of human pancreatic tumoral soj-6 cells and inhibits the growth of tumor xenografts
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ID: 165437
2004
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Abstract
Feto-acinar pancreatic protein (FAPP) characterized by mAbJ28 reactivity is a specific component associated with ontogenesis and behaves as an oncodevelopment-associated antigen. We attempted to determine whether pancreatic tumoral SOJ-6 cells are expressed at their surface FAPP antigens and to examine if specific antibodies directed against these FAPP epitopes could decrease the growth of pancreatic tumors in a mice model. For this purpose, we used specific antibodies against either the whole FAPP, the O-glycosylated C-terminal domain, or the N-terminal domain of the protein. Our results indicate that SOJ-6 cells expressed at their surface a 32-kDa peptide corresponding to the C-terminal domain of the FAPP. Furthermore, we show, by using endoproteinase Lys-C or geldanamycin, a drug able to impair the FAPP secretion, that this 32-kDa peptide expressed on the SOJ-6 cell surface comes from the degradation of the FAPP. Finally, an in vivo prospective study using a preventative tumor model in nude mice indicates that targeting this peptide by the use of mAb16D10 inhibits the growth of SOJ-6 xenografts. The specificity of mAb16D10 for pancreatic tumors and the possibility to obtain recombinant structures of mucin-like peptides recognized by mAb16D10 and mAbJ28 are promising tools in immunologic approaches to cure pancreatic cancers.
| Reference Key |
panicot-dubois2004neoplasia:monoclonal
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| Authors | ;Laurence Panicot-Dubois;Muriel Aubert;Cécile Franceschi;Eric Mas;Françoise Silvy;Christian Crotte;Jean-Paul Bernard;Dominique Lombardo;Marie-Odile Sadoulet |
| Journal | ACS chemical neuroscience |
| Year | 2004 |
| DOI |
10.1593/neo.04298
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| URL | |
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