Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells.

Michael Bitzer, Sorin Armeanu, Florian Prinz, Guy Ungerechts, Wolfgang Wybranietz, Martin Spiegel, Christian Bernlöhr, Francesco Cecconi, Michael Gregor, Wolfgang J. Neubert, Klaus Schulze-Osthoff, Ulrich M. Lauer

Research output: Contribution to journalArticle

51 Citations (Scopus)

Abstract

Apoptotic cell death is of central importance in the pathogenesis of viral infections. Activation of a cascade of cysteine proteases, i.e. caspases, plays a key role in the effector phase of virus-induced apoptosis. However, little is known about pathways leading to the activation of initiator caspases in virus-infected host cells. Recently, we have shown that Sendai virus (SeV) infection triggers apoptotic cell death by activation of the effector caspase-3 and initiator caspase-8. We now investigated mechanisms leading to the activation of another initiator caspase, caspase-9. Unexpectedly we found that caspase-9 cleavage is not dependent on the presence of active caspases-3 or -8. Furthermore, the presence of caspase-9 in mouse embryonic fibroblast (MEF) cells was a prerequisite for Sendai virus-induced apoptotic cell death. Caspase-9 activation occurred without the release of cytochrome c from mitochondria and was not dependent on the presence of Apaf-1 or reactive oxygen intermediates. Our results therefore suggest an alternative mechanism for caspase-9 activation in virally infected cells beside the well characterized pathways via death receptors or mitochondrial cytochrome c release.

Original languageEnglish
Pages (from-to)29817-29824
Number of pages8
JournalJournal of Biological Chemistry
Volume277
Issue number33
Publication statusPublished - Aug 16 2002

Fingerprint

Sendai virus
Caspase 9
Caspase 8
Initiator Caspases
Viruses
Chemical activation
Cell Death
Cell death
Virus Diseases
Cytochromes c
Caspase 3
Effector Caspases
Death Domain Receptors
Cysteine Proteases
Caspases
Mitochondria
Fibroblasts
Apoptosis
Oxygen
Cells

ASJC Scopus subject areas

  • Biochemistry

Cite this

Bitzer, M., Armeanu, S., Prinz, F., Ungerechts, G., Wybranietz, W., Spiegel, M., ... Lauer, U. M. (2002). Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells. Journal of Biological Chemistry, 277(33), 29817-29824.

Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells. / Bitzer, Michael; Armeanu, Sorin; Prinz, Florian; Ungerechts, Guy; Wybranietz, Wolfgang; Spiegel, Martin; Bernlöhr, Christian; Cecconi, Francesco; Gregor, Michael; Neubert, Wolfgang J.; Schulze-Osthoff, Klaus; Lauer, Ulrich M.

In: Journal of Biological Chemistry, Vol. 277, No. 33, 16.08.2002, p. 29817-29824.

Research output: Contribution to journalArticle

Bitzer, M, Armeanu, S, Prinz, F, Ungerechts, G, Wybranietz, W, Spiegel, M, Bernlöhr, C, Cecconi, F, Gregor, M, Neubert, WJ, Schulze-Osthoff, K & Lauer, UM 2002, 'Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells.', Journal of Biological Chemistry, vol. 277, no. 33, pp. 29817-29824.
Bitzer M, Armeanu S, Prinz F, Ungerechts G, Wybranietz W, Spiegel M et al. Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells. Journal of Biological Chemistry. 2002 Aug 16;277(33):29817-29824.
Bitzer, Michael ; Armeanu, Sorin ; Prinz, Florian ; Ungerechts, Guy ; Wybranietz, Wolfgang ; Spiegel, Martin ; Bernlöhr, Christian ; Cecconi, Francesco ; Gregor, Michael ; Neubert, Wolfgang J. ; Schulze-Osthoff, Klaus ; Lauer, Ulrich M. / Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells. In: Journal of Biological Chemistry. 2002 ; Vol. 277, No. 33. pp. 29817-29824.
@article{b5c322ab13f749328b07726b4c825010,
title = "Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells.",
abstract = "Apoptotic cell death is of central importance in the pathogenesis of viral infections. Activation of a cascade of cysteine proteases, i.e. caspases, plays a key role in the effector phase of virus-induced apoptosis. However, little is known about pathways leading to the activation of initiator caspases in virus-infected host cells. Recently, we have shown that Sendai virus (SeV) infection triggers apoptotic cell death by activation of the effector caspase-3 and initiator caspase-8. We now investigated mechanisms leading to the activation of another initiator caspase, caspase-9. Unexpectedly we found that caspase-9 cleavage is not dependent on the presence of active caspases-3 or -8. Furthermore, the presence of caspase-9 in mouse embryonic fibroblast (MEF) cells was a prerequisite for Sendai virus-induced apoptotic cell death. Caspase-9 activation occurred without the release of cytochrome c from mitochondria and was not dependent on the presence of Apaf-1 or reactive oxygen intermediates. Our results therefore suggest an alternative mechanism for caspase-9 activation in virally infected cells beside the well characterized pathways via death receptors or mitochondrial cytochrome c release.",
author = "Michael Bitzer and Sorin Armeanu and Florian Prinz and Guy Ungerechts and Wolfgang Wybranietz and Martin Spiegel and Christian Bernl{\"o}hr and Francesco Cecconi and Michael Gregor and Neubert, {Wolfgang J.} and Klaus Schulze-Osthoff and Lauer, {Ulrich M.}",
year = "2002",
month = "8",
day = "16",
language = "English",
volume = "277",
pages = "29817--29824",
journal = "Journal of Biological Chemistry",
issn = "0021-9258",
publisher = "American Society for Biochemistry and Molecular Biology Inc.",
number = "33",

}

TY - JOUR

T1 - Caspase-8 and Apaf-1-independent caspase-9 activation in Sendai virus-infected cells.

AU - Bitzer, Michael

AU - Armeanu, Sorin

AU - Prinz, Florian

AU - Ungerechts, Guy

AU - Wybranietz, Wolfgang

AU - Spiegel, Martin

AU - Bernlöhr, Christian

AU - Cecconi, Francesco

AU - Gregor, Michael

AU - Neubert, Wolfgang J.

AU - Schulze-Osthoff, Klaus

AU - Lauer, Ulrich M.

PY - 2002/8/16

Y1 - 2002/8/16

N2 - Apoptotic cell death is of central importance in the pathogenesis of viral infections. Activation of a cascade of cysteine proteases, i.e. caspases, plays a key role in the effector phase of virus-induced apoptosis. However, little is known about pathways leading to the activation of initiator caspases in virus-infected host cells. Recently, we have shown that Sendai virus (SeV) infection triggers apoptotic cell death by activation of the effector caspase-3 and initiator caspase-8. We now investigated mechanisms leading to the activation of another initiator caspase, caspase-9. Unexpectedly we found that caspase-9 cleavage is not dependent on the presence of active caspases-3 or -8. Furthermore, the presence of caspase-9 in mouse embryonic fibroblast (MEF) cells was a prerequisite for Sendai virus-induced apoptotic cell death. Caspase-9 activation occurred without the release of cytochrome c from mitochondria and was not dependent on the presence of Apaf-1 or reactive oxygen intermediates. Our results therefore suggest an alternative mechanism for caspase-9 activation in virally infected cells beside the well characterized pathways via death receptors or mitochondrial cytochrome c release.

AB - Apoptotic cell death is of central importance in the pathogenesis of viral infections. Activation of a cascade of cysteine proteases, i.e. caspases, plays a key role in the effector phase of virus-induced apoptosis. However, little is known about pathways leading to the activation of initiator caspases in virus-infected host cells. Recently, we have shown that Sendai virus (SeV) infection triggers apoptotic cell death by activation of the effector caspase-3 and initiator caspase-8. We now investigated mechanisms leading to the activation of another initiator caspase, caspase-9. Unexpectedly we found that caspase-9 cleavage is not dependent on the presence of active caspases-3 or -8. Furthermore, the presence of caspase-9 in mouse embryonic fibroblast (MEF) cells was a prerequisite for Sendai virus-induced apoptotic cell death. Caspase-9 activation occurred without the release of cytochrome c from mitochondria and was not dependent on the presence of Apaf-1 or reactive oxygen intermediates. Our results therefore suggest an alternative mechanism for caspase-9 activation in virally infected cells beside the well characterized pathways via death receptors or mitochondrial cytochrome c release.

UR - http://www.scopus.com/inward/record.url?scp=19044371418&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=19044371418&partnerID=8YFLogxK

M3 - Article

VL - 277

SP - 29817

EP - 29824

JO - Journal of Biological Chemistry

JF - Journal of Biological Chemistry

SN - 0021-9258

IS - 33

ER -