1997
DOI: 10.1038/40901
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Abstract: The inhibitor-of-apoptosis (IAP) family of genes has an evolutionarily conserved role in regulating programmed cell death in animals ranging from insects to humans. Ectopic expression of human IAP proteins can suppress cell death induced by a variety of stimuli, but the mechanism of this inhibition was previously unknown. Here we show that human X-chromosome-linked IAP directly inhibits at least two members of the caspase family of cell-death proteases, caspase-3 and caspase-7. As the caspases are highly conse… Show more

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Cited by 1,753 publications
(1,290 citation statements)
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“…These results suggest the direct inhibition of caspase 3 by ILP. Our ®ndings, therefore, are con®rmed with a previous report (Deveraux et al, 1997).…”
Section: Caspase 3-inactivation By Ilpsupporting
confidence: 91%
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“…These results suggest the direct inhibition of caspase 3 by ILP. Our ®ndings, therefore, are con®rmed with a previous report (Deveraux et al, 1997).…”
Section: Caspase 3-inactivation By Ilpsupporting
confidence: 91%
“…Among Bcl-2 family members, Bcl-2 and Bcl-xL suppress the apoptotic death signaling (Tsujimoto et al, 1984;Vaux et al, 1988;Tsujimoto, 1989;Boise et al, 1993), whereas those expressions were not encountered in intact HepG2 cells (data not shown). IAPs also prevent the apoptotic death signaling, and especially ILP can suppress it by direct inhibition of caspase 3 (Deveraux et al, 1997). In the present study, ILP expression was encountered in intact HepG2 cells, and its expression was down regulated by treatment with actinomycin D. These results led us to the possible involvement of ILP in the resistance of Fas-mediated apoptosis in the absence of actinomycin D.…”
Section: Discussionsupporting
confidence: 55%
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“…31 It has been shown previously that XIAP binds to activated caspase-3 or to a catalytically inactive caspase-3 with an active conformation, but does not bind to the proenzyme. 32,33 We do not believe, that the turnover of mature caspase-3 in our system involves XIAP-induced proteasomal degradation, since our studies demonstrate a requirement for an intact catalytic site. Furthermore, in our experiments, proteasome inhibitors (MG132, lactacystin) failed to stabilize active caspase-3 complexes in HeLa cells, possibly reflecting a cell-specific difference in the mode of degradation (unpublished data).…”
Section: Discussionmentioning
confidence: 86%
“…In addition to pro-and antiapoptotic bcl-2 molecules (Reed, 1998), a second gene family of inhibitor of apoptosis (IAP) has been recently identified (Crook et al, 1993). Highly evolutionarily conserved from viruses to mammalian cells (Crook et al, 1993;Ambrosini et al, 1997), IAP proteins target a downstream step in apoptosis by inhibiting the terminal effector caspase-3 and -7 (Deveraux et al, 1997;Tamm et al, 1998), and by interfering with processing/activation of the pinnacle caspase, caspase-9.…”
mentioning
confidence: 99%