Endonuclease G: a mitochondrial protein released in apoptosis and involved in caspase-independent DNA degradation.
Cell Death Differ
; 8(12): 1136-42, 2001 Dec.
Article
em En
| MEDLINE
| ID: mdl-11753562
ABSTRACT
A hallmark of apoptosis is the fragmentation of nuclear DNA. Although this activity involves the caspase-3-dependent DNAse CAD (caspase-activated DNAse), evidence exists that DNA fragmentation can occur independently of caspase activity. Here we report on the ability of truncated Bid (tBid) to induce the release of a DNAse activity from mitochondria. This DNAse activity was identified by mass spectrometry as endonuclease G, an abundant 30 kDa protein released from mitochondria under apoptotic conditions. No tBid-induced endonuclease G release could be observed in mitochondria from Bcl-2-transgenic mice. The in vivo occurrence of endonuclease G release from mitochondria during apoptosis was confirmed in the liver from mice injected with agonistic anti-Fas antibody and is completely prevented in Bcl-2 transgenic mice. These data indicate that endonuclease G may be involved in CAD-independent DNA fragmentation during cell death pathways in which truncated Bid is generated.
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Base de dados:
MEDLINE
Assunto principal:
Apoptose
/
Caspases
/
Proteínas Mitocondriais
/
Endodesoxirribonucleases
/
Fragmentação do DNA
Limite:
Animals
Idioma:
En
Ano de publicação:
2001
Tipo de documento:
Article