Mitochondrially localized active caspase-9 and caspase-3 result mostly from translocation from the cytosol and partly from caspase-mediated activation in the organelle. Lack of evidence for Apaf-1-mediated procaspase-9 activation in the mitochondria (Q40667287)

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scientific article published on 28 February 2003

Language	Label	Description	Also known as
English	Mitochondrially localized active caspase-9 and caspase-3 result mostly from translocation from the cytosol and partly from caspase-mediated activation in the organelle. Lack of evidence for Apaf-1-mediated procaspase-9 activation in the mitochondria	scientific article published on 28 February 2003

Statements

scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Mitochondrially localized active caspase-9 and caspase-3 result mostly from translocation from the cytosol and partly from caspase-mediated activation in the organelle. Lack of evidence for Apaf-1-mediated procaspase-9 activation in the mitochondria (English)

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

1

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

author name string

Dean G Tang

2

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

language of work or name

0 references

publication date

28 February 2003

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

278

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

19

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

17408-17420

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

Caspases: intracellular signaling by proteolysis

1 reference

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Death receptors: signaling and modulation

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Caspase-2 induces apoptosis by releasing proapoptotic proteins from mitochondria

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Caspase-2 can trigger cytochrome C release and apoptosis from the nucleus.

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Caspase-2 acts upstream of mitochondria to promote cytochrome c release during etoposide-induced apoptosis

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Requirement for caspase-2 in stress-induced apoptosis before mitochondrial permeabilization

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A novel Apaf-1-independent putative caspase-2 activation complex

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Apoptosis initiated by Bcl-2-regulated caspase activation independently of the cytochrome c/Apaf-1/caspase-9 apoptosome

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Coupling endoplasmic reticulum stress to the cell death program. An Apaf-1-independent intrinsic pathway

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An endoplasmic reticulum stress-specific caspase cascade in apoptosis. Cytochrome c-independent activation of caspase-9 by caspase-12

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Caspases: their intracellular localization and translocation during apoptosis.

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Caspase-2 is localized at the Golgi complex and cleaves golgin-160 during apoptosis

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Caspase-12 mediates endoplasmic-reticulum-specific apoptosis and cytotoxicity by amyloid-beta

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Mitochondrial release of caspase-2 and -9 during the apoptotic process

1 reference

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The caspase-3 precursor has a cytosolic and mitochondrial distribution: implications for apoptotic signaling

1 reference

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Detection of pro-caspase-3 in cytosol and mitochondria of various tissues

1 reference

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Pro-caspase-8 is predominantly localized in mitochondria and released into cytoplasm upon apoptotic stimulation

1 reference

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Release of caspase-9 from mitochondria during neuronal apoptosis and cerebral ischemia

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Activation of caspase-1 in the nucleus requires nuclear translocation of pro-caspase-1 mediated by its prodomain

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Caspase-12 processing and fragment translocation into nuclei of tunicamycin-treated cells

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Different subcellular distribution of caspase-3 and caspase-7 following Fas-induced apoptosis in mouse liver

1 reference

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Prodomain-dependent nuclear localization of the caspase-2 (Nedd2) precursor. A novel function for a caspase prodomain

1 reference

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21 January 2018

Pre-processed caspase-9 contained in mitochondria participates in apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

Early mitochondrial activation and cytochrome c up-regulation during apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

Apoptosis in the absence of cytochrome c accumulation in the cytosol.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

Analysis of the membrane potential of rat- and mouse-liver mitochondria by flow cytometry and possible applications.

1 reference

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21 January 2018

Bax is present as a high molecular weight oligomer/complex in the mitochondrial membrane of apoptotic cells

1 reference

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Ordering the cytochrome c-initiated caspase cascade: hierarchical activation of caspases-2, -3, -6, -7, -8, and -10 in a caspase-9-dependent manner

1 reference

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21 January 2018

Caspase-3 cleaves Apaf-1 into an approximately 30 kDa fragment that associates with an inappropriately oligomerized and biologically inactive approximately 1.4 MDa apoptosome complex

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

Autoactivation of procaspase-9 by Apaf-1-mediated oligomerization

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

1 reference

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Recruitment, activation and retention of caspases-9 and -3 by Apaf-1 apoptosome and associated XIAP complexes

1 reference

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21 January 2018

Biochemical pathways of caspase activation during apoptosis

1 reference

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De novo ceramide regulates the alternative splicing of caspase 9 and Bcl-x in A549 lung adenocarcinoma cells. Dependence on protein phosphatase-1.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

Characterization of a novel isoform of caspase-9 that inhibits apoptosis

1 reference

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21 January 2018

Relief of extrinsic pathway inhibition by the Bid-dependent mitochondrial release of Smac in Fas-mediated hepatocyte apoptosis

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

21 January 2018

TRAIL-induced apoptosis requires Bax-dependent mitochondrial release of Smac/DIABLO.

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M300750200

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Pro-apoptotic apoptosis protease-activating factor 1 (Apaf-1) has a cytoplasmic localization distinct from Bcl-2 or Bcl-x(L).

1 reference

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Chemotherapy: targeting the mitochondrial cell death pathway

1 reference

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The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet.

1 reference

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Release of intact, monomeric cytochrome c from apoptotic and necrotic cells

1 reference

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Activation of membrane-associated procaspase-3 is regulated by Bcl-2.

1 reference

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Caspases are not localized in mitochondria during life or death

1 reference

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Nuclear Apaf-1 and cytochrome c redistribution following stress-induced apoptosis

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Caspases disrupt the nuclear-cytoplasmic barrier

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A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis

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Bid, Bax, and lipids cooperate to form supramolecular openings in the outer mitochondrial membrane

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Identification of a caspase-9 substrate and detection of its cleavage in programmed cell death during mouse development

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Caspase-mediated loss of mitochondrial function and generation of reactive oxygen species during apoptosis

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Activation of Multiple Interleukin-1β Converting Enzyme Homologues in Cytosol and Nuclei of HL-60 Cells during Etoposide-induced Apoptosis

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21 January 2018

Identifiers

10.1074/JBC.M300750200

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

22 September 2017

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