Cytochrome c in the apoptotic and antioxidant cascades

  title={Cytochrome c in the apoptotic and antioxidant cascades},
  author={Vladimir P. Skulachev},
  journal={FEBS Letters},

Redox regulation of apoptosis before and after cytochrome C release

This review summarizes what is known about the biological role of ROS and its targets in apoptosis with an emphasis on its intricate connections to mitochondria and the basic components of cell death.

Anticancer drugs induce increased mitochondrial cytochrome c expression that precedes cell death.

The teniposide-induced increase of cytochrome c was inhibited by cycloheximide, indicating new protein synthesis, and the increase in mitochondrial protein expression may play a role in the early cellular defense against anticancer drugs.

Molecular mechanisms of apoptosis. Structure of cytochrome c-cardiolipin complex

It is shown that under the action of cooperative forces, the protein in the globule expands greatly in volume, its conformation is modified, and the protein becomes a peroxidase in extended membranes, such as giant monolayer liposomes, and very likely in biological membranes, the formation of nanospheres of cytochrome c-cardiolipin complex causes fusion of membrane sections and dramatic chaotization of the whole membrane structure.



Cytochrome c activation of CPP32‐like proteolysis plays a critical role in a Xenopus cell‐free apoptosis system

In a cell‐free system based on Xenopus egg extracts, Bcl‐2 blocks apoptotic activity by preventing cytochrome c release from mitochondria, which induces apoptosis by activating CPP32‐like caspases, via unknown cytosolic factors.

The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis

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.

Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked

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.

Bcl-2 and the Outer Mitochondrial Membrane in the Inactivation of Cytochrome c during Fas-mediated Apoptosis*

In Jurkat cells, cytochrome c inactivation during Fas-driven apoptosis requires the permeabilization of the outer mitochondrial membrane; and the post-mitochondrial fraction from CEM cells that overexpress Bcl-2 both prevents and reverses cy tochrome cinactivation.

Bcl-2 inhibits the mitochondrial release of an apoptogenic protease

It is shown that mitochondria contain a pre-formed approximately 50-kD protein which is released upon delta psi m disruption and which, in a cell-free in vitro system, causes isolated nuclei to undergo apoptotic changes such as chromatin condensation and internucleosomal DNA fragmentation, and the effect of Bcl-2 on the formation, release, and action of AIF.

Role for Bcl-xL as an inhibitor of cytosolic cytochrome C accumulation in DNA damage-induced apoptosis.

  • S. KharbandaP. Pandey D. Kufe
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 1997
A role for Bcl-xL in protecting cells from apoptosis by inhibiting the availability of cytochrome C in the cytosol is support by coimmunoprecipitation studies.

Loss of Function of Cytochrome c in Jurkat Cells Undergoing Fas-mediated Apoptosis*

The results suggest that a rapid loss in mitochondrial function due at least in part to the inhibition or inactivation of cytochrome c is a potentially fatal component of the apoptosis program of Jurkat cells.

The Central Executioner of Apoptosis: Multiple Connections between Protease Activation and Mitochondria in Fas/APO-1/CD95- and Ceramide-induced Apoptosis

A protease activation pathway with the mitochondrial phase of apoptosis regulation is connected, providing a plausible explanation of why Bcl-2 fails to interfere with Fas-triggered apoptosis in most cell types, yet prevents ceramide- and prooxidant-induced apoptosis.cmk.