Abstract
Fas (APO-1, CD95), a member of the tumor necrosis factor (TNF) receptor superfamily, is a cell membrane protein that mediates programmed cell death (apoptosis). In an effort to characterize the possible role of Fas-mediated apoptosis in some important physiological processes in livestock, bovine Fas (bFas) cDNA was isolated and its nucleotide sequence determined. The predicted amino acid sequence encodes a 323-amino-acid protein that contains a leader peptide, a transmembrane domain, and three domains of cysteine-rich motif within the extracellular region. At the amino acid level, bFas is 57% and 50% identical to human (hFas) and mouse (mFas), respectively. Its expression is abundant in peripheral blood lymphocytes, lung, spleen, thymus, and ovary, but minimal in heart, liver, and brain. A polyclonal anti-bFas serum raised against the carboxy-terminal half of cysteine-rich motif I recognized a single 46-kD protein in bovine MDBK cells by Western blot analysis. To investigate the apoptotic activity of bFas, MDBK and bFas-transfected L929 cells were exposed to a monoclonal anti-hFas IgM. Unlike other cell culture systems, the antibody failed to trigger cell death in MDBK and bFas transfected L929 cells.
Get full access to this article
View all access options for this article.