Monoclonal Antibodies Reactive with the neu Oncogene Product Inhibit the Neoplastic Properties of neu-Transformed Cells

Author(s):  
Jeffrey A. Drebin ◽  
Victoria C. Link ◽  
Mark I. Greene
1991 ◽  
Vol 11 (3) ◽  
pp. 1745-1750 ◽  
Author(s):  
D H Yu ◽  
K Scorsone ◽  
M C Hung

The adenovirus type 5 early region 1A (E1A) gene was introduced into neu-transformed B104-1-1 cells. Cells that expressed E1A possessed reduced transforming activity in vitro and reduced tumorigenicity in nude mice. These results demonstrate that the E1A gene products can act negatively to suppress the transformed phenotype in neu-transformed cells.


1993 ◽  
Vol 8 (4) ◽  
pp. 233-239 ◽  
Author(s):  
I. Garcia De Palazzo ◽  
A. Klein-Szanto ◽  
L. M. Weiner

Selected murine monoclonal antibodies (MAb) have been shown to inhibit relevant tumor growth in vitro and in animal models. Recently, bispecific antibodies (BsMAb) have been developed which target cytolytic effector cells via one antibody binding site and tumor antigen by the other specificity. For example, the BsMAb 2B1 possesses specificity for c-erbB-2 and Fcγ RIII, the low affinity Fcγ receptor expressed by polymorphonuclear leukocytes (PMN), macrophages and large granular lymphocytes (LGL). The human homologue of the rat neu oncogene, c-erbB-2, has been demonstrated to be amplified in breast, gastrointestinal, lung and ovarian carcinomas. Tumor expression of c-erbB-2 has been shown to be an important prognostic indicator in breast and ovarian carcinomas. The restricted expression of the c-erbB-2 protooncogene product in normal human tissues and the wide distribution of c-erbB-2 expression in such tumors may justify attempts to use an appropriately constructed BsM Ab in clinical trials. In this report we have addressed this issue by immunohistochemically evaluating the expression of c-erbB-2 oncogene product in a variety of malignant tumors utilizing 2B1 and the anti-c-erbB-2 monovalent parent of 2B1, 520C9. Among the studied neoplasms, c-erbB-2 expression was detected in 49% of primary carcinomas stained with 520C9 and in 39% of those stained with 2B1. In the group of metastatic tumors, c-erbB-2 oncoprotein was detected in 52% of cases by 520C9 and in 41% by 2B1. Our results indicate that immunocytochemistry using bispecific monoclonal 2B1 is a reliable method for the detection of c-erbB-2 expression, and that this BsMAb detects c-erbB-2 expression in tumors nearly as well as its anti-c-erbB-2 monovalent parent antibody.


Virology ◽  
1985 ◽  
Vol 142 (1) ◽  
pp. 44-58 ◽  
Author(s):  
Alt Zantema ◽  
Jack A.M. Fransen ◽  
Arja Davis-Olivier ◽  
Frans C.S. Ramaekers ◽  
G. Peter Vooijs ◽  
...  

1985 ◽  
Vol 22 (6) ◽  
pp. 691-701 ◽  
Author(s):  
R. F. TIEBOUT ◽  
E. A. M. STRICKER ◽  
F. OOSTERHOF ◽  
D. J. M. HEEMSTRA ◽  
W. P. ZEIJLEMAKER

1991 ◽  
Vol 11 (3) ◽  
pp. 1745-1750
Author(s):  
D H Yu ◽  
K Scorsone ◽  
M C Hung

The adenovirus type 5 early region 1A (E1A) gene was introduced into neu-transformed B104-1-1 cells. Cells that expressed E1A possessed reduced transforming activity in vitro and reduced tumorigenicity in nude mice. These results demonstrate that the E1A gene products can act negatively to suppress the transformed phenotype in neu-transformed cells.


1989 ◽  
Vol 108 (6) ◽  
pp. 2401-2408 ◽  
Author(s):  
J R Glenney ◽  
L Zokas

We have previously reported the production of monoclonal antibodies directed against phosphotyrosine, which is the modification induced by many oncogene products and growth factor receptors. One of these antiphosphotyrosine antibodies (py20) was used in affinity chromatography to isolate phosphotyrosine (PY)-containing proteins from Rous sarcoma virus-transformed chick embryo fibroblasts (RSV-CEFs). Mice were immunized with these PY-proteins for the production of monoclonal antibodies to individual substrates. Fifteen antibodies were generated in this way to antigens with molecular masses of 215, 76, 60, and 22 kD. Antibodies to individual substrates were used to analyze the subcellular location in normal and RSV-CEFs. Antibodies to the 215- and 76-kD antigen stained focal contacts when used in immunofluorescence microscopy while anti-22-kD protein antibodies resulted in punctate staining concentrated in the margins of cells and in parallel arrays. Both distributions were altered in transformed cells. When cells were extracted with nonionic detergent under conditions that stabilize the cytoskeleton, 50% of the 76-kD protein and greater than 90% of the 22-kD protein fractionated with the cytoskeleton. This study offers a new approach to both the identification of membrane skeletal proteins in fibroblasts and changes that occur upon transformation by an activated tyrosine kinase.


1987 ◽  
Vol 31 (10) ◽  
pp. 959-966 ◽  
Author(s):  
Hidenori Suzuki ◽  
Yuichi Okubo ◽  
Mayumi Moriyama ◽  
Manami Sasaki ◽  
Yoshiko Matsumoto ◽  
...  

Author(s):  
James E. Crandall ◽  
Linda C. Hassinger ◽  
Gerald A. Schwarting

Cell surface glycoconjugates are considered to play important roles in cell-cell interactions in the developing central nervous system. We have previously described a group of monoclonal antibodies that recognize defined carbohydrate epitopes and reveal unique temporal and spatial patterns of immunoreactivity in the developing main and accessory olfactory systems in rats. Antibody CC2 reacts with complex α-galactosyl and α-fucosyl glycoproteins and glycolipids. Antibody CC1 reacts with terminal N-acetyl galactosamine residues of globoside-like glycolipids. Antibody 1B2 reacts with β-galactosyl glycolipids and glycoproteins. Our light microscopic data suggest that these antigens may be located on the surfaces of axons of the vomeronasal and olfactory nerves as well as on some of their target neurons in the main and accessory olfactory bulbs.


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