Anti-Fas IgG1 antibodies recognizing the same epitope of Fas/APO-1 mediate different biological effects in vitro

Fas/APO-1 is a cell surface glycoprotein that mediates programmed cell death or apoptosis when cross-linked with agonistic anti-Fas or anti-APO-1 mAb or the endogenous Fas/APO-1 ligand. In this report, we examined the in vitro biological properties of a panel of anti-human Fas mAb of IgG1 subclass (...

Full description

Saved in:
Bibliographic Details
Published in:International immunology 1997-02, Vol.9 (2), p.201-209
Main Authors: Fadeel, B, Thorpe, C J, Yonehara, S, Chiodi, F
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - pharmacology
Antibody Affinity
Apoptosis - drug effects
Apoptosis - immunology
Binding Sites - immunology
Cross Reactions
Epitope Mapping
Epitopes - immunology
Epitopes - metabolism
Epitopes - pharmacology
fas Receptor - drug effects
fas Receptor - immunology
fas Receptor - physiology
Humans
Immunoglobulin G - classification
Immunoglobulin G - metabolism
Immunoglobulin G - pharmacology
Jurkat Cells
Medicin och hälsovetenskap
Protein Binding - immunology
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Fas/APO-1 is a cell surface glycoprotein that mediates programmed cell death or apoptosis when cross-linked with agonistic anti-Fas or anti-APO-1 mAb or the endogenous Fas/APO-1 ligand. In this report, we examined the in vitro biological properties of a panel of anti-human Fas mAb of IgG1 subclass (ZB4, VB3, WB3 and CBE). We found that anti-Fas clone VB3 induced marked apoptotic cell death in Fas/APO-1-expressing Jurkat cells, although this cell killing was delayed when compared to the cytolytic effect mediated by the prototypic anti-Fas antibody of IgM subclass (clone CH-11). The ZB4 antibody, on the other hand, efficiently blocked apoptosis induced by CH-11. The WB3 and CBE clones neither induced or inhibited apoptosis. These antibodies were all found to recognize one and the same linear site on the Fas/APO-1 molecule, despite their different biological effects. The ability of these anti-Fas mAb to induce or inhibit apoptosis appeared to correlate with their relative affinity for the Fas/APO-1 molecule. These results provide further evidence for the potential of anti-Fas antibodies of the IgG1 subclass to elicit signals via the Fas/APO-1 molecule.
ISSN:0953-8178
1460-2377
1460-2377
DOI:10.1093/intimm/9.2.201