共查询到20条相似文献,搜索用时 15 毫秒
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Nakajima H Nagaso H Kakui N Ishikawa M Hiranuma T Hoshiko S 《The Journal of biological chemistry》2004,279(41):42774-42786
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Giorgi Zaalishvili Dina Margiani 《Biochemical and biophysical research communications》2010,393(1):123-125
Poly(ADP-ribose) polymerase-1 (PARP-1), a nuclear enzyme that catalyzes the NAD+-dependent addition of ADP-ribose polymers on a variety of nuclear proteins, has been shown to be associated with the nuclear matrix. As yet, the properties and conditions of this association are unclear. Here, we show the existence of two PARP-1 pools associated with the nuclear matrix of rat liver and the ability of PARP-1 automodification to facilitate its binding to the nuclear matrix. 相似文献
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Poly(ADP-ribose) polymerase-1 cleavage during apoptosis: an update 总被引:11,自引:1,他引:10
Soldani C Scovassi AI 《Apoptosis : an international journal on programmed cell death》2002,7(4):321-328
Poly(ADP-ribosylation) is a post-translational modification of proteins playing a crucial role in many processes, including DNA repair and cell death. The best known poly(ADP-ribosylating) enzime, PARP-1, is a DNA nick sensor and uses NAD+ to form polymers of ADP-ribose which are further bound to nuclear protein acceptors. To strictly regulate poly(ADP-ribose) turnover, its degradation is assured by the enzyme poly(ADP-ribose) glycohydrolase (PARG). During apoptosis, PARP-1 plays two opposite roles: its stimulation leads to poly(ADP-ribose) synthesis, whereas caspases cause PARP-1 cleavage and inactivation. PARP-1 proteolysis produces an 89 kDa C-terminal fragment, with a reduced catalytic activity, and a 24 kDa N-terminal peptide, which retains the DNA binding domains. The fate and the possible role of these fragments during apoptosis will be discussed. 相似文献
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Transcriptional control by PARP-1: chromatin modulation, enhancer-binding, coregulation, and insulation 总被引:2,自引:0,他引:2
Kraus WL 《Current opinion in cell biology》2008,20(3):294-302
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Cristiana Soldani Maria Claudia Lazz Maria Grazia Bottone Gianluca Tognon Marco Biggiogera Carlo E. Pellicciari A. Ivana Scovassi 《Experimental cell research》2001,269(2):193
Poly(ADP-ribose) polymerase-1 (PARP-1) plays the active role of “nick sensor” during DNA repair and apoptosis, when it synthesizes ADP-ribose from NAD+ in the presence of DNA strand breaks. Moreover, PARP-1 becomes a target of apoptotic caspases, which originate two proteolytic fragments of 89 and 24 kDa. The precise relationship between PARP-1 activation and degradation during apoptosis is still a matter of debate. In human Hep-2 cells driven to apoptosis by actinomycin D, we have monitored PARP-1 activity by the mAb 10H, which is specific for the ADP-ribose polymers, and we have observed that poly(ADP-ribose) synthesis is a very early response to the apoptotic stimulus. The analysis of the presence and fate of the p89 proteolytic fragment revealed that PARP-1 proteolysis by caspases is concomitant with poly(ADP-ribose) synthesis and that p89 migrates from the nucleus into the cytoplasm in late apoptotic cells with advanced nuclear fragmentation. 相似文献
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