Human ICE/CED-3 Protease Nomenclature

Alnemri, Emad S.; Livingston, David J.; Nicholson, Donald W.; Salvesen, Guy S.; Thornberry, Nancy A.; Wong, Winnie W.; Yuan, Junying

doi:10.1016/s0092-8674(00)81334-3

Cited by 2,194 publications

(1,232 citation statements)

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“…Caspase is a nomenclature of ICE/CED-3 family of cysteinproteinases (Alnemri et al, 1996). Three subfamilies of caspase have been documented and are known as the ICE-, CPP32-and ICH-1-subfamilies.…”

Section: Discussionmentioning

confidence: 99%

“…The ICE gene shows close similarity to the ced-3 death gene derived from Caenorhabditis elegans (Yuan et al, 1993). Ten genes have been identi®ed as ICE/CED-3 homologue and these were recently termed the`caspase' family (Alnemri et al, 1996). Among caspases, an essential role of caspase 3 (CPP32/Yama/Apopain) in Fasmediated apoptosis has been reported (FernandesAlnemri et al, 1994;Hasegawa et al, 1996;Suzuki et al, 1997b).…”

Section: Introductionmentioning

confidence: 99%

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Resistance to Fas-mediated apoptosis: activation of Caspase 3 is regulated by cell cycle regulator p21WAF1 and IAP gene family ILP

Suzuki¹,

Tsutomi²,

Akahane³

et al. 1998

Oncogene

323

277

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The death receptor Fas transduces apoptotic death signaling mediated by caspases. In the present study, human hepatoma HepG2 cells showed the Fas-mediated apoptosis mediated by caspase, especially caspase 3, only in the presence of actinomycin D. Interestingly, cytosolic proteins extracted from intact HepG2 cells induced caspase 3 inactivation. Our results reveal that this inactivation was triggered by the direct inhibition of activated caspase 3 by IAP gene family ILP. In addition, a 53 kDa protein was co-immunoprecipitated with antihuman caspase 3 antibody from intact HepG2 cells. This protein was a complex-protein of procaspase 3 and the cell cycle regulator p21 WAF1 (p21). P21 bound to only procaspase 3, but not to activated caspase 3. We also demonstrate that p21 protein-loaded HepG2 cells resist to Fas-mediated apoptosis even in the presence of actinomycin D. Here we report that caspase 3 inactivation for the resistance to Fas-mediated apoptosis is induced by a procaspase 3/p21 complex formation and direct inhibition of activated caspase 3 by ILP.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Resistance to Fas-mediated apoptosis: activation of Caspase 3 is regulated by cell cycle regulator p21WAF1 and IAP gene family ILP

Suzuki¹,

Tsutomi²,

Akahane³

et al. 1998

Oncogene

323

277

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“…The induction of apoptosis by diverse stimuli is associated with activation of aspartate-speci®c cysteine proteases (caspases) (Martin and Green, 1995) and cleavage of PARP (Kaufmann et al, 1993), PKCd (Emoto et al, 1995;Ghayur et al, 1996) and other proteins (Widman et al, 1998). Caspases exist in cells as catalytically inactive zymogens composed of three di erent subunits: a prodomain and two catalytic subdomains (Alnemri et al, 1996). Activation of procaspases generally requires cleavage after speci®c Asp residues (Cohen, 1997;Nicholson and Thornberry, 1997).…”

Section: Introductionmentioning

confidence: 99%

Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3

et al. 2000

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The release of mitochondrial cytochrome c by genotoxic stress induces the formation of a cytosolic complex with Apaf-1 (mammalian CED4 homolog) and thereby the activation of procaspase-3 (cas-3) and procaspase-9 (cas-9). Here we demonstrate that heat-shock protein 27 (Hsp27) inhibits cytochrome c (cyt c)-dependent activation of cas-3. Hsp27 had no e ect on cyt c release, Apaf-1 and cas-9 activation. By contrast, our results show that Hsp27 associates with cas-3, but not Apaf-1 or cas-9, and inhibits activation of cas-3 by cas-9-mediated proteolysis. Furthermore, the present results demonstrate that immunodepletion of Hsp27 depletes cas-3. Importantly, treatment of cells with DNA damaging agents dissociates the Hsp27/cas-3 complex and relieves inhibition of cas-3 activation. These ®ndings de®ne a novel function for Hsp27 and provide the ®rst evidence that a heat shock protein represses cas-3 activation.

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“…Apoptosis can be induced by a variety of stimuli, including depletion of growth factors, hormones, heat shock, genotoxins and crosslinking of death factor receptors (reviewed by Thompson, 1995). Apoptotic signal transduction pathways activated by various treatments converge into a common pathway, which is driven by ICE family proteases (reviewed by Martin and Green, 1995), now called caspases (Alnemri et al, 1996), and negatively regulated by anti-cell death proteins such as the Bcl-2 family (reviewed by Thompson, 1995) and the IAP family (Clem and Miller, 1994;Hay et al, 1995). Caspase-1 (ICE)-like and caspase-3 (CPP32/Yama)-like proteases are implicated in apoptosis, because their tetrapeptide competitive inhibitors prevent apoptosis induced by a variety of stimuli (reviewed by Martin and Green, 1995).…”

Section: Introductionmentioning

confidence: 99%

Evidence against a functional site for Bcl-2 downstream of caspase cascade in preventing apoptosis

et al. 1997

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Apoptotic cell death is driven by ICE family proteases (caspases) and negatively regulated by Bcl-2 family proteins. Although it has been shown that Bcl-2 exerts anti-apoptotic activity by blocking a step(s) leading to the activation of caspases, a role for Bcl-2 and Bcl-x L downstream of the caspase cascade has remained unclear. Here, we show that puri®ed active caspase-3 (CPP32/Yama/apopain) and caspase-1 (ICE) induces apoptosis when microinjected into the cytoplasm of cells, con®rming our recent observations, and that the apoptosis is not at all prevented by Bcl-2 and Bcl-x L , which are overexpressed more than su ciently to prevent Fas-mediated and overexpressed procaspase-1-mediated apoptosis. Thus, Bcl-2 and Bcl-x L do not act downstream of the caspase cascade.

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Human ICE/CED-3 Protease Nomenclature

Cited by 2,194 publications

References 0 publications

Resistance to Fas-mediated apoptosis: activation of Caspase 3 is regulated by cell cycle regulator p21WAF1 and IAP gene family ILP

Resistance to Fas-mediated apoptosis: activation of Caspase 3 is regulated by cell cycle regulator p21WAF1 and IAP gene family ILP

Hsp27 functions as a negative regulator of cytochrome c-dependent activation of procaspase-3

Evidence against a functional site for Bcl-2 downstream of caspase cascade in preventing apoptosis

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