| First Author | Kabra NH | Year | 1999 |
| Journal | J Immunol | Volume | 162 |
| Issue | 5 | Pages | 2766-74 |
| PubMed ID | 10072523 | Mgi Jnum | J:53223 |
| Mgi Id | MGI:1331537 | Doi | 10.4049/jimmunol.162.5.2766 |
| Citation | Kabra NH, et al. (1999) A tailless fas-FADD death-effector domain chimera is sufficient to execute Fas function in T cells but not B cells of MRL-lpr/lpr mice. J Immunol 162(5):2766-74 |
| abstractText | The Fas receptor delivers signals crucial for lymphocyte apoptosis through its cytoplasmic death domain. Several Fas cytoplasmic-associated proteins have been reported and studied in cell lines. So far, only Fas-associated death domain protein (FADD), another death domain-containing molecule has been shown to be essential for Fas signals in vivo. FADD is thought to function by recruiting caspase-8 through its death-effector domain. To test whether FADD is sufficient to deliver Fas signals, we generated transgenic mice expressing a chimera comprised of the Fas extracellular domain and FADD death-effector domain. Expression of this protein in lymphocytes of Fas-deficient MRL-lpr/lpr mice completely diminishes their T cell but not their B cell abnormalities. These results suggest that FADD alone is sufficient for initiation of Fas signaling in primary T cells, but other pathways may operate in B cells. |
