International Immunology, Vol 9, 201-209, Copyright © 1997 by Oxford University Press
B Fadeel, CJ Thorpe, S Yonehara and F Chiodi
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.
ARTICLES
Anti-Fas IgG1 antibodies recognizing the same epitope of Fas/APO-1 mediate different biological effects in vitro
Microbiology and Tumorbiology Center, Karolinska Institutet, Stockholm, Sweden.
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