Poly(ADP-ribosyl)ation of Apoptosis Antagonizing Transcription Factor Involved in Hydroquinone-Induced DNA Damage Response

The molecular mechanism of DNA damage induced by hydroquinone (HQ) remains unclear. Poly(ADP-ribose) polymerase-1 (PARP-1) usually works as a DNA damage sensor, and hence, it is possible that PARP-1 is involved in the DNA damage response induced by HQ. In TK6 cells treated with HQ, PARP activity as...

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Published in:Biomedical and environmental sciences 2016-01, Vol.29 (1), p.80-84
Main Authors: LING, Xiao Xuan, LIU, Jia Xian, YUN, Lin, DU, Yu Jun, CHEN, Shao Qian, CHEN, Jia Long, TANG, Huan Wen, LIU, Lin Hua
Format: Article
Language:English
Subjects:
Antioxidants - toxicity
Apoptosis Regulatory Proteins - genetics
Apoptosis Regulatory Proteins - metabolism
Cell Line
DNA Damage - drug effects
Gene Expression Regulation - drug effects
Gene Silencing
Histones - genetics
Histones - metabolism
Humans
Hydroquinones - toxicity
Poly (ADP-Ribose) Polymerase-1
Poly(ADP-ribose) Polymerases - genetics
Poly(ADP-ribose) Polymerases - metabolism
Protein Transport
Repressor Proteins - genetics
Repressor Proteins - metabolism
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Summary:The molecular mechanism of DNA damage induced by hydroquinone (HQ) remains unclear. Poly(ADP-ribose) polymerase-1 (PARP-1) usually works as a DNA damage sensor, and hence, it is possible that PARP-1 is involved in the DNA damage response induced by HQ. In TK6 cells treated with HQ, PARP activity as well as the expression of apoptosis antagonizing transcription factor (AATF), PARP-1, and phosphorylated H2AX (γ-H2AX) were maximum at 0.5 h, 6 h, 3 h, and 3 h, respectively. To explore the detailed mechanisms underlying the prompt DNA repair reaction, the above indicators were investigated in PARP-1-silenced cells. PARP activity and expression of AATF and PARP-1 decreased to 36%, 32%, and 33%, respectively, in the cells; however, γ-H2AX expression increased to 265%. Co-immunoprecipitation (co-IP) assays were employed to determine whether PARP-1 and AATF formed protein complexes. The interaction between these proteins together with the results from IP assays and confocal microscopy indicated that poly(ADP-ribosyl)ation (PARylation) regulated AATF expression. In conclusion, PARP-1 was involved in the DNA damage repair induced by HQ via increasing the accumulation of AATF through PARylation.
ISSN:0895-3988
2214-0190
DOI:10.3967/bes2016.008