Abstract
The bcl-2 family of genes code for proteins that contain anti-apoptotic or pro-apoptotic activity. The human bfl-1 gene contains an open reading frame for a 175-amino acid Bcl-2 family protein. Among the various Bcl-2 family members, the Bfl-1 protein shares the highest homology with the mouse A1 protein. These two proteins share three conserved domains, Bcl homology (BH)1, BH2, and BH3, with other Bcl-2 family proteins. Unlike other Bcl-2 family members, Bfl-1 contains a Gln-rich NH2-terminal region and lacks an NH (19K homology) domain 1. We demonstrate that the Bfl-1 protein suppresses apoptosis induced by the p53 tumor suppressor protein in a manner similar to other Bcl-2 family members such as Bcl-2, Bcl-XL and EBV-BHRF1. In addition, the bfl-1 gene cooperates efficiently with the Ela oncogene in transformation of primary rodent epithelial cells. Our results suggest that the human bfl-1 gene may play an important role in carcinogenesis.
Footnotes
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↵1 This research was supported by Grants CA-33616 and CA-31719 from the National Cancer Institute.
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↵2 C. D-E. and T. S. contributed equally to this work.
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↵3 To whom requests for reprints should be addressed, at Saint Louis University School of Medicine, Health Sciences Center, 3681 Park Ave., St. Louis, MO 63110-2592. Phone: (314) 577-8416; Fax: (314) 577-8406.
- Received May 28, 1996.
- Accepted July 17, 1996.
- ©1996 American Association for Cancer Research.
Volume 56, Issue 17
