A nuclease that mediates cell death induced by DNA damage and poly(ADP-ribose) polymerase-1
Author(s) -
Yingfei Wang,
Ran An,
George K. E. Umanah,
Hyejin Park,
Kalyani Nambiar,
Stephen Eacker,
BongWoo Kim,
Lei Bao,
Maged M. Harraz,
Calvin Chang,
Rong Chen,
Jennifer E. Wang,
TaeIn Kam,
Jun Seop Jeong,
Zhi Xie,
Stewart Neifert,
Jiang Qian,
Shaida A. Andrabi,
Seth Blackshaw,
Heng Zhu,
Hongjun Song,
Guoli Ming,
Valina L. Dawson,
Ted M. Dawson
Publication year - 2016
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.aad6872
Subject(s) - poly adp ribose polymerase , nuclease , endonuclease , dna damage , programmed cell death , dna fragmentation , macrophage migration inhibitory factor , polymerase , microbiology and biotechnology , dna repair , dna , apoptosis , biology , fragmentation (computing) , apoptosis inducing factor , chemistry , caspase , genetics , cytokine , ecology
DNA damage-activated nuclease identified Cells that experience stresses and accumulate excessive damage to DNA undergo cell death mediated by a nuclear enzyme known as PARP-1. During this process, apoptosis-inducing factor (AIF) translocates to the nucleus and activates one or more nucleases to cleave DNA. Wanget al. found that macrophage migration inhibitory factor (MIF) is an AIF-associated endonuclease that contributes to PARP-1-induced DNA fragmentation (see the Perspective by Jonas). In mouse neurons in culture, loss of MIF protected neurons from cell death caused by excessive stimulation. Targeting MIF could thus provide a therapeutic strategy against diseases in which PARP-1 activation is excessive.Science , this issue p.82 ; see also p.36
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