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J. Exp. Med.,
Volume 189, Number 6, March 15, 1999 949-956
By
§§
From the * Department of Microbiology, the The sensitivity of primary splenic B cells to Fas-mediated apoptosis is modulated in a receptor-specific fashion. Here we used a differential display strategy to detect cDNAs present in B cells
rendered Fas resistant but absent in those rendered Fas sensitive. This led to the cloning and
characterization of a novel 1.2-kb gene that encodes a Fas apoptosis inhibitory molecule
(FAIM). faim-transfected BAL-17 B lymphoma cells were less sensitive by half or more to Fas-mediated apoptosis than were vector-transfected controls, using Fas ligand-bearing T cells or a
cytotoxic anti-Fas antibody to trigger Fas, and this was associated with inhibition of Fas-
induced poly-ADP ribose polymerase (PARP) cleavage. In primary B cells, the time course of
faim mRNA and FAIM protein expression correlated with the induction of Fas resistance by surface (s)Ig engagement. Thus, FAIM is an inducible effector molecule that mediates Fas resistance produced by sIg engagement in B cells. However, faim is broadly expressed in various tissues and the faim sequence is highly conserved evolutionarily, suggesting that its role extends beyond
lymphocyte homeostasis. As FAIM has no significant regions of homology to other gene products
that modulate Fas killing, it appears to represent a distinct, new class of antiapoptotic protein.
Department of Medicine, and the § Evans Memorial
Department of Clinical Research, Boston University Medical Center, Boston, Massachusetts 02118
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