The "pro-apoptotic genies" get out of mitochondria: oxidative lipidomics and redox activity of cytochrome c/cardiolipin complexes (Q23923111)

HELD

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25 September 2023

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19 July 2017

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29 March 2020

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29 March 2020

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29 March 2020

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13

A.A. Shvedova

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Valerian E. Kagan

1

V.E. Kagan

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Yulia Y. Tyurina

2

Y.Y. Tyurina

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Hülya Bayır

3

H. Bayir

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Steven T. DeKosky

12

S. DeKosky

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author name string

C.T. Chu

4

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A.A. Kapralov

5

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I.I. Vlasova

6

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N.A. Belikova

7

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V.A. Tyurin

8

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A. Amoscato

9

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M. Epperly

10

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J. Greenberger

11

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J. Jiang

Chemico-biological Interactions

14

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language of work or name

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27 October 2006

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published in

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volume

163

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issue

1-2

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page(s)

15-28

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performing organization

University of Pittsburgh

University of Pittsburgh at Pittsburgh

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NIOSHTIC-2

on focus list of Wikimedia project

2 February 2024

Wikimedia–NIOSH collaboration

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25 September 2023

Mitochondria, oxygen free radicals, and apoptosis

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Loss of molecular interaction between cytochrome c and cardiolipin due to lipid peroxidation

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The mechanism of cardiolipin biosynthesis in liver mitochondria

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Nitrosative stress results in irreversible inhibition of purified mitochondrial complexes I and III without modification of cofactors.

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Reactive oxygen species generated from the mitochondrial electron transport chain induce cytochrome c dissociation from beef-heart submitochondrial particles via cardiolipin peroxidation. Possible role in the apoptosis

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

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The cardiolipin-binding domain of Bid affects mitochondrial respiration and enhances cytochrome c release

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Cytochrome c acts as a cardiolipin oxygenase required for release of proapoptotic factors

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