Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9

@article{Kuida1998ReducedAA,
  title={Reduced Apoptosis and Cytochrome c–Mediated Caspase Activation in Mice Lacking Caspase 9},
  author={Keisuke Kuida and Tarik F. Haydar and Chia-Yi Kuan and Yong Gu and Choji Taya and Hajime Karasuyama and Michael S.-S. Su and Pasko Rakic and Richard A. Flavell},
  journal={Cell},
  year={1998},
  volume={94},
  pages={325-337}
}

Figures from this paper

Deficiency in caspase-9 or caspase-3 induces compensatory caspase activation
TLDR
It is demonstrated here that elimination of certain caspases was compensated in vivo by the activation of othercaspases, providing direct experimental evidence for compensatory pathways of caspase activation.
Bcl-2–regulated apoptosis and cytochrome c release can occur independently of both caspase-2 and caspase-9
TLDR
It is suggested that caspases other than caspase 2 and 9 can promote cytochrome c release and initiate Bcl-2–regulated apoptosis, and lymphocytes and fibroblasts lacking both remained sensitive to diverse apoptotic stimuli.
Dual Role of Caspase-11 in Mediating Activation of Caspase-1 and Caspase-3 under Pathological Conditions
TLDR
It is demonstrated that caspase-11–deficient mice have a reduced number of apoptotic cells and a defect in casp enzyme-3 activation after middle cerebral artery occlusion (MCAO), a mouse model of stroke, and that Recombinant procaspases can autoprocess itself in vitro.
Caspases and Their Regulation in Apoptosis during Brain Development
TLDR
The results suggest complex regulation mechanisms and distinct functions of caspase activation in mammalian brain development, and the Jun N-terminal kinase (JNK) signaling pathway appears to be an important mechanism that regulates the brain region-specific activation of casedases.
Identification of a Caspase-9 Substrate and Detection of Its Cleavage in Programmed Cell Death during Mouse Development*
TLDR
Immunohistochemical analysis showed that caspase-9 cleaves vimentin in apoptotic cells in the embryonic nervous system and the interdigital regions, consistent with observations that gene knockouts of caspases and its activator, Apaf-1, result in developmental defects in these tissues.
Roles of caspases in apoptosis, development, and cytokine maturation revealed by homozygous gene deficiencies.
TLDR
Deletion of genes that encode murine caspases suggests that caspased are involved not only in apoptosis but also in cytokine maturation and cell growth and differentiation.
Emerging roles of caspase-3 in apoptosis
TLDR
Caspase-3 is essential for certain processes associated with the dismantling of the cell and the formation of apoptotic bodies, but it may also function before or at the stage when commitment to loss of cell viability is made.
Caspase Enzyme Activity Is Not Essential for Apoptosis During Thymocyte Development1
TLDR
Results indicate that caspase-independent signal transduction pathways can mediate thymocyte death during normal T cell development.
Caspase-12 compensates for lack of caspase-2 and caspase-3 in female germ cells
TLDR
Interestingly, DKO oocytes were more resistant to apoptosis induced by methotrexate (MTX) than WT oocytes, and these results revealed that in female germ cells, insults that directly interfere with their metabolic status require caspase-2 and caspasing-3 as obligatory executioners of the ensuing cell death cascade.
...
1
2
3
4
5
...

References

SHOWING 1-10 OF 69 REFERENCES
Defects in regulation of apoptosis in caspase-2-deficient mice.
TLDR
Caspase-2 acts both as a positive and negative cell death effector, depending upon cell lineage and stage of development, and underwent apoptosis more effectively than wild-type neurons when deprived of NGF.
Essential contribution of caspase 3/CPP32 to apoptosis and its associated nuclear changes.
TLDR
Examination of the role of CPP32 in apoptosis using mice, embryonic stem cells, and mouse embryonic fibroblasts deficient for the caspase indicates that CPP 32 is an essential component in apoptotic events that is remarkably system- and stimulus-dependent.
The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
TLDR
In a cell-free apoptosis system, mitochondria spontaneously released cytochrome c, which activated DEVD-specific caspases, leading to fodrin cleavage and apoptotic nuclear morphology, and Bcl-2 acts to inhibit cy tochrome c translocation, thereby blocking caspase activation and the apoptotic process.
Decreased apoptosis in the brain and premature lethality in CPP32-deficient mice
TLDR
CPP32 is shown to play a critical role during morphogenetic cell death in the mammalian brain during embryonic day 12, resulting in a variety of hyperplasias and disorganized cell deployment.
A caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
TLDR
A caspase-activated deoxyribonuclease (CAD) and its inhibitor (ICAD) have now been identified in the cytoplasmic fraction of mouse lymphoma cells and seems to function as a chaperone for CAD during its synthesis, remaining complexed with CAD to inhibit its DNase activity.
Mitochondrial cytochrome c release in apoptosis occurs upstream of DEVD‐specific caspase activation and independently of mitochondrial transmembrane depolarization
TLDR
It is reported that cytochrome c release from mitochondria is an early event in the apoptotic process induced by UVB irradiation or staurosporine treatment in CEM or HeLa cells, preceding or at the time of DEVD‐specific caspase activation and substrate cleavage.
Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
TLDR
One possible role of Bcl-2 in prevention of apoptosis is to block cytochrome c release from mitochondria, which is normally located in the mitochondrial intermembrane space.
...
1
2
3
4
5
...