Ligation of CD40 rescues Ramos-Burkitt lymphoma B cells from calcium ionophore- and antigen receptor-triggered apoptosis by inhibiting activation of the cysteine protease CPP32/Yama and cleavage of its substrate PARP.

@article{An1996LigationOC,
  title={Ligation of CD40 rescues Ramos-Burkitt lymphoma B cells from calcium ionophore- and antigen receptor-triggered apoptosis by inhibiting activation of the cysteine protease CPP32/Yama and cleavage of its substrate PARP.},
  author={Sungkwan An and Kirstine A Knox},
  journal={FEBS letters},
  year={1996},
  volume={386 2-3},
  pages={115-22}
}
The new and growing family of interleukin-1beta-converting enzyme (ICE) cysteine proteases are now recognised to be major effectors of cellular death by apoptosis. Like other members of this family, the CPP32/Yama proform is activated by processing to its active heterodimeric enzyme or apopain when it likely contributes to the process of apoptosis by cleaving poly(ADP-ribose) polymerase (PARP) and thereby inhibiting much of its DNA repair activity. Apoptosis plays a fundamental role in the… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 29 extracted citations

Inhibition of B cell receptor-mediated apoptosis by IFN.

Journal of immunology • 1999
View 4 Excerpts
Highly Influenced

Similar Papers

Loading similar papers…