Immunochemical characterization of two antigens recognized by new monoclonal antibodies against human colon carcinoma.

Détails

ID Serval
serval:BIB_94B632B9DACC
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Institution
Titre
Immunochemical characterization of two antigens recognized by new monoclonal antibodies against human colon carcinoma.
Périodique
Journal of immunology
Auteur(s)
Girardet C., Vacca A., Schmidt-Kessen A., Schreyer M., Carrel S., Mach J.P.
ISSN
0022-1767
Statut éditorial
Publié
Date de publication
1986
Peer-reviewed
Oui
Volume
136
Numéro
4
Pages
1497-1503
Langue
anglais
Notes
Publication types: Journal Article ; Research Support, Non-U.S. Gov't
Publication Status: ppublish
Résumé
Two different monoclonal antibodies (MAb), called L-D1 and L-C5, were produced after immunization with either intact cells or the methanol phase of glycolipid extracts, respectively, from the same human colon carcinoma line, LoVo. As determined by an antibody-binding radioimmunoassay (RIA) on intact cells, MAb L-D1 and MAb L-C5 were highly reactive with all five colon carcinoma lines tested and with only one out of the 21 cell lines of various tissue origin tested. No reactivity of either MAb was observed with peripheral blood lymphocytes, granulocytes, or erythrocytes from healthy donors of various blood groups. Both MAb were tested in competitive binding experiments with an anti-CEA MAb from our laboratory (CEA 35) and with two previously described anti-colon carcinoma MAb from the Wistar Institute called 1083-17-1A (17-1A) and NS-19.9. In competitive binding experiments, MAb L-D1 was inhibited by MAb 17-1A and reciprocally, whereas MAb L-C5 was not inhibited by any of the other MAb tested. MAb L-D1 precipitated a major protein band with an apparent molecular weight (MW) of 41 kilodaltons (kD); interestingly, MAb 17-1A, which was reported to react with an uncharacterized antigen, precipitated the same protein band of 41 kD. This was confirmed with immunodepletion experiments. Furthermore, after treatment of the colon carcinoma cell line with tunicamycin, both MAb L-D1 and 17-1A precipitated a protein band of 35 kD. This shift of 6 kD suggests that the glycoprotein recognized by these 2 MAb contains two to three N-linked carbohydrate side chains. MAb L-C5 precipitated a group of three to four protein bands ranging from 43 to 53 kD that were not modified by tunicamycin treatment. A preliminary study conducted by using immunoperoxidase labeling on frozen sections of primary colon carcinoma showed that the two new MAb react strongly with these tumors, but also weakly with the normal adjacent mucosa, as did the other anti-colon carcinoma MAb tested.
Mots-clé
Animals, Antibodies, Monoclonal/diagnostic use, Antigen-Antibody Reactions, Antigens, Neoplasm/analysis, Antigens, Neoplasm/immunology, Binding, Competitive, Carcinoma/immunology, Carcinoma/pathology, Cell Extracts/analysis, Cell Fusion/methods, Cell Line, Colonic Neoplasms/immunology, Colonic Neoplasms/pathology, Frozen Sections, Glycolipids, Hematopoietic Stem Cells/immunology, Humans, Intestinal Mucosa/analysis, Intestinal Mucosa/pathology, Mice, Mice, Inbred BALB C, Precipitin Tests, Radioimmunoassay, Tunicamycin/pharmacology
Pubmed
Web of science
Création de la notice
19/11/2009 13:50
Dernière modification de la notice
20/08/2019 15:57
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