Expression of the Baculovirus <i>p35</i> Gene Inhibits Mammalian Neural Cell Death

Rabizadeh, Shahrooz; LaCount, Douglas; Friesen, Paul D.; Bredesen, Dale E.

doi:10.1111/j.1471-4159.1993.tb07477.x

Cited by 191 publications

(103 citation statements)

References 18 publications

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“…The first IAP family member identified was p35, a baculoviral protein that suppresses apoptosis in a number of cell types (including cells of the CNS) and under a variety of conditions (Rabizadeh et al, 1993;Hisahara et al, 2000). Subsequent studies demonstrated that several IAPs exist and function by binding to the inactive pro-caspase and therefore, inhibiting its processing to the active form (Hay et al, 1994;Hay et al, 1995;Hay, 2000).…”

Section: The Caspase-3 Apoptotic Cascadementioning

confidence: 99%

“…A second potential step to target in the caspase-3 apoptotic cascade involves the events that are upstream of caspase-3, but downstream of the cytochrome c release, in particular the family of inhibitor of apoptosis proteins Duckett et al, 1998;Ekert et al, 1999;Ekert et al, 2001). The first identified IAP family member was p35, a baculoviral protein that suppresses apoptosis in a number of cell types (including cells of the CNS) and under a variety of conditions (Rabizadeh et al, 1993;Simons et al, 1999;Xu et al, 1999;Eberhardt et al, 2000;Hisahara et al, 2000;Kugler et al, 2000;Korhonen et al, 2001). Subsequent studies demonstrated that several IAPs exist and function by binding to the inactive pro-caspase, therefore, inhibiting its processing to the active form (Hay et al, 1994;Hay et al, 1995;Hay, 2000).…”

Section: Therapeutic Interventions: Delivery Of Anti-apoptotic Genes mentioning

confidence: 99%

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Apoptotic Cell Death Following Traumatic Injury to the Central Nervous System

Springer¹

2002

BMB Reports

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Apoptotic cell death is a fundamental and highly regulated biological process in which a cell is instructed to actively participate in its own demise. This process of cellular suicide is activated by developmental and environmental cues and normally plays an essential role in eliminating superfluous, damaged, and senescent cells of many tissue types. In recent years, a number of experimental studies have provided evidence of widespread neuronal and glial apoptosis following injury to the central nervous system (CNS). These studies indicate that injury-induced apoptosis can be detected from hours to days following injury and may contribute to neurological dysfunction. Given these findings, understanding the biochemical signaling events controlling apoptosis is a first step towards developing therapeutic agents that target this cell death process. This review will focus on molecular cell death pathways that are responsible for generating the apoptotic phenotype. It will also summarize what is currently known about the apoptotic signals that are activated in the injured CNS, and what potential strategies might be pursued to reduce this cell death process as a means to promote functional recovery.

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Section: The Caspase-3 Apoptotic Cascadementioning

confidence: 99%

Section: Therapeutic Interventions: Delivery Of Anti-apoptotic Genes mentioning

confidence: 99%

Apoptotic Cell Death Following Traumatic Injury to the Central Nervous System

Springer¹

2002

BMB Reports

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“…The expression of P35 is able to prevent developmentally programmed cell death in Drosophila melanogaster embryo as well as apoptosis in the eye of D. melanogaster upon X-irradiation (Hay et al, 1994). Expression of P35 in Caenorhabditis elegans prevents programmed cell death in developing larvae (Sugimoto et al, 1994) and microinjection of p35-expression vectors into rat sympathetic neurones can block apoptosis induced by the withdrawal of nerve growth factor (Martinou et al, 1995;Rabizadeh et al, 1993). Overexpression of P35 is also able to inhibit TNF-and Fasmediated apoptosis (Beidler et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Differential inhibitory effects of CrmA, P35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli

Dorstyn

Kumar

1997

Cell Death Differ

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We have investigated the effects of expression of the viral proteins CrmA, P35 and IAP, and the three mammalian IAP homologues (MIHA, MIHB and MIHC), on the regulation of apoptosis induced by either the overexpression of caspases (ICE, CPP32 and Nedd2), by serum-deprivation, or by girradiation in NIH3T3 fibroblasts. As previously shown, CrmA strongly inhibited ICE-induced apoptosis but was ineffective against Nedd2-or CPP32-mediated apoptosis. P35, IAP and MIHA protected cells from apoptosis induced by the three caspases to varying extents but MIHB and MIHC were largely ineffective. NIH3T3 cells expressing P35 and MIHA, but not IAP, CrmA, MIHB and MIHC, showed enhanced cell survival under serum-deprived conditions. In addition, P35, CrmA and MIHA could provide substantial protection against death induced by g-irradiation. These results suggest the presence of multiple apoptotic pathways with differential sensitivity to various naturally occurring apoptosis inhibitors.

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“…However, roles of other members of this family in cell death remain to be elucidated. Since apoptosis induced by a variety of stimuli is inhibited by baculovirus p35 (Clem et al, 1991;Rabizadeh et al, 1993;Hay et al, 1994;Sugimoto et al, 1994;Beidler et al, 1995), which inhibits the activities of caspases (Xue and Horvitz, 1995;Bump et al, 1995), and by a cowpox virus-derived caspase-1 inhibitor, CrmA (Pickup et al, 1986;Ray et al, 1992;Gagliardini et al, 1994;Tewari and Dixit, 1995;Los et al, 1995;Enari et al, 1995;Tewari et al, 1995b;Li et al, 1996), it would be interesting to identify CrmA-inhibitable members of the caspase family.…”

Section: Introductionmentioning

confidence: 99%

Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases

1997

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Proteases of the caspase family are implicated in mammalian apoptosis and constitute a protease cascade. We characterized caspase-4 (TX/ICH-2/ICE rel II) and caspase-5 (ICE rel III/TY), which are most closely related to caspase-1 (ICE) among the caspase family. Although overexpression of caspase-4 and caspase-5 induced apoptosis, confirming previous observations, this apoptosis was not inhibited by a caspase-1-specific tetrapeptide inhibitor (Ac-YVAD-CHO), suggesting that caspase-4 and caspase-5 have different substrate specificities from caspase-1 and also that caspase-4-and caspase-5-induced apoptosis is not mediated by caspase-1. CrmA, a cowpox virus-derived caspase-1 inhibitor that prevents apoptosis induced by various stimuli, was cleaved by caspase-4 and caspase-5, and inhibited their proteolytic activity as assessed by cleavage of pro-caspase-3 (pro-CPP32/Yama/apopain). Thus, caspase-4 and caspase-5 are CrmA-inhibitable proteases like caspase-1 and might be involved in apoptosis.

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Expression of the Baculovirus p35 Gene Inhibits Mammalian Neural Cell Death

Cited by 191 publications

References 18 publications

Apoptotic Cell Death Following Traumatic Injury to the Central Nervous System

Apoptotic Cell Death Following Traumatic Injury to the Central Nervous System

Differential inhibitory effects of CrmA, P35, IAP and three mammalian IAP homologues on apoptosis in NIH3T3 cells following various death stimuli

Caspase-4 and caspase-5, members of the ICE/CED-3 family of cysteine proteases, are CrmA-inhibitable proteases

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