| First Author | Cao H | Year | 1996 |
| Journal | Biochem Biophys Res Commun | Volume | 227 |
| Issue | 1 | Pages | 266-72 |
| PubMed ID | 8858135 | Mgi Jnum | J:35779 |
| Mgi Id | MGI:83224 | Doi | 10.1006/bbrc.1996.1499 |
| Citation | Cao H, et al. (1996) Regulation of tumor necrosis factor-and Fas-mediated apoptotic cell death by a novel cDNA TR2L. Biochem Biophys Res Commun 227(1):266-72 |
| abstractText | A novel cDNA, TR2L, isolated from murine NIH 3T3 fibroblasts, was found to modulate tumor necrosis factor (TNF)-mediated apoptosis in murine L929 fibrosarcoma cells. The full-length cDNA (853 bp) encodes a predicted coding region of 56 amino acids (6.3 kD), with 53.6% identity to the C-terminus of rat transcriptional activator FE65. When expressed stably in L929 cells, TR2L protein inhibited TNF cytotoxic response. In contrast, TR2L enhanced anti-Fas antibodies/actinomycin D (ActD)-mediated L929 apoptosis. Alteration of TR2L function occurred by tagging this protein with a 6xHis fragment to the N-terminus (designated 6xH-TR2L). L929 cells which stably expressed 6xH-TR2L acquired a significantly enhanced TNF apoptotic response and increased genomic DNA fragmentation compared to control cells. Enhanced cell death also occurred in these 6xH-TR2L-expressing cells under serum starvation conditions. In contrast, the anti-Fas/ActD-mediated apoptosis was blocked by the 6xH-TR2L protein. Functional role of TR2L protein in regulation of cancer cell susceptibility to TNF-and Fas ligand-mediated apoptosis is suggested. |
