Caspase-independent Cell Killing by Fas-associated Protein with Death Domain

doi:10.1083/jcb.143.5.1353

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J. Cell Biol., Volume 143, Number 5, November 30, 1998 1353-1360

Caspase-independent Cell Killing by Fas-associated Protein with Death Domain

Atsuo Kawahara,^*^§ Yoshiyuki Ohsawa, Hirotaka Matsumura,^* Yasuo Uchiyama, and Shigekazu Nagata^*^§

^* Department of Genetics and Department of Anatomy, Osaka University Medical School, Yamada-oka, Suita, Osaka 565-0871, Japan; and ^§ Osaka Bioscience Institute, Furuedai, Suita, Osaka 565-0874, Japan

The binding of Fas ligand to Fas recruits caspase 8 to Fas via an adaptor, FADD/MORT1, and activates a caspase cascade leadingto apoptosis. Here, we describe a human Jurkat-derived cell line(JB-6) that is deficient in caspase 8. This cell line was resistantto the apoptosis triggered by Fas engagement. However, the multimerizationof Fas-associated protein with death domain, through the use ofa dimerizing system, killed the JB-6 cells. This killing processwas not accompanied by the activation of caspases or DNA fragmentation.The dying cells showed neither condensation nor fragmentationof cells and nuclei, but the cells and nuclei swelled in a mannersimilar to that seen in necrosis. These results suggested thatFas-associated protein with death domain can kill the cells viatwo pathways, one mediated by caspases and another that does notinvolve them.

Key words: apoptosis; caspase; Fas; Fas-associated protein with death domain; necrosis

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