2001
DOI: 10.1074/jbc.m010498200
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Abstract: Apoptosis-inducing factor (AIF) is a mitochondrial flavoprotein, which translocates to the nucleus during apoptosis and causes chromatin condensation and large scale DNA fragmentation. Here we report the biochemical characterization of AIF's redox activity. Natural AIF purified from mitochondria and recombinant AIF purified from bacteria (AIF⌬1-120) exhibit NADH oxidase activity, whereas superoxide anion (O 2 ؊ ) is formed. AIF⌬1-120 is a monomer of 57 kDa containing 1 mol of noncovalently bound FAD/mol of pro… Show more

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Cited by 348 publications
(287 citation statements)
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“…11 AIF has been proposed to act as a scavenger of ROS, particularly peroxides. 12,13 However, more recent work has shown that AIF is required for efficient oxidative phosphorylation, most probably through its role in ensuring proper assembly and functionality of mitochondrial respiratory complex I. 14 Furthermore, because of this capacity, AIF can exert a cytoprotective role in the mitochondria, enabling cells to cope more effectively with oxidative stress.…”
Section: Introductionmentioning
confidence: 99%
See 1 more Smart Citation
“…11 AIF has been proposed to act as a scavenger of ROS, particularly peroxides. 12,13 However, more recent work has shown that AIF is required for efficient oxidative phosphorylation, most probably through its role in ensuring proper assembly and functionality of mitochondrial respiratory complex I. 14 Furthermore, because of this capacity, AIF can exert a cytoprotective role in the mitochondria, enabling cells to cope more effectively with oxidative stress.…”
Section: Introductionmentioning
confidence: 99%
“…23 Perhaps not surprisingly, the conserved FAD-binding domain of AIF, required for its NADH oxidase activity and for its cytoprotective effects, 15 is dispensable for its proapoptotic function. 13,24 Thus, AIF has a dual mission in the cell: normally, it resides in the mitochondrial membrane, helps maintain optimal mitochondrial respiratory function and protects cells against the undesirable and eventually deadly consequences of oxidative damage. On the other hand, under conditions of excessive stress leading to mitochondrial dysfunction and culminating in apoptosis, AIF translocates from the mitochondria to the cell nucleus, resulting in large-scale DNA fragmentation.…”
Section: Introductionmentioning
confidence: 99%
“…Once in mitochondria, the full-length AIF is processed and the prodomain removed, giving rise to a mature form of B57 kDa (Otera et al, 2005). Under physiological conditions, AIF is a mitochondrial FAD-dependent oxidoreductase that plays a role in oxidative phosphorylation (Miramar et al, 2001). However, after a cellular insult, AIF is cleaved by calpains and/or cathepsins (Polster et al, 2005;Yuste et al, 2005) and translocates from mitochondria to cytosol and to nucleus where it causes, in a caspase-independent fashion, chromatin condensation and large-scale (B50 kb) DNA fragmentation (Susin et al, 1999).…”
Section: Introductionmentioning
confidence: 99%
“…This effect depends on its redox activity (Urbano et al, 2005). Indeed, AIF is a flavoprotein that can oxidize NADH and NADPH in vitro (Miramar et al, 2001) and may participate in the detoxification of reactive oxygen species (Klein et al, 2002) and in the maintenance of glutathione levels (Cande et al, 2004b), although the mechanisms of this antioxidant activity remain to be determined. Upon activation of a serine protease that liberates AIF from its membrane attachment (Polster et al, 2005;Yuste et al, 2005), combined with outer mitochondrial membrane permeabilization, for instance through Bax/Bak-mediated pores (Green and Kroemer, 2004), AIF is released from mitochondria and participates in the catastrophic catabolic process that allows the digestion of the cellular content from within.…”
Section: Introductionmentioning
confidence: 99%