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Involvement of multiple proteases during Fas‐mediated apoptosis in T lymphocytes
Author(s) -
Sek C. Chow,
Marianne Weis,
Georges Kass,
Tim H. Holmström,
John E. Eriksson,
Sten Orrenius
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00370-o
Subject(s) - jurkat cells , apoptosis , proteases , dna fragmentation , microbiology and biotechnology , chromatin , fragmentation (computing) , programmed cell death , serine protease , biology , inhibitor of apoptosis domain , chemistry , protease , t cell , enzyme , caspase , dna , biochemistry , immunology , immune system , ecology
The mechanism of Fas antigen‐mediated apoptosis is at present unclear. We show here that the100,000 × g supernatant from cell lysates prepared from anti‐Fas‐stimulated JURKAT T cells, induces chromatin fragmentation in isolated nuclei with concomitant morphological changes typically seen in apoptosis. The formation of this apoptotic nuclei promoting activity (ANPA) in JURKAT T cells after Fas antigen ligation was blocked by the serine protease inhibitors, TPCK and DCI, and by the interleukin 1‐β‐converting enzyme inhibitor, VAD‐FMK. In addition, chromatin degradation and morphological changes mediated by the ANPA in isolated nuclei were inhibited by TPCK, but not by DCI or VAD‐FMK. These results suggest that Fas‐mediated apoptosis in T cells involves the activation of a cascade of proteases.