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Updated: Oct 3, 2026

Quantitative Detection of DNA-Protein Crosslinks and Their Post-Translational Modifications
Published on: April 21, 2023
TCDD-inducible poly(ADP-ribose) polymerase: a novel response to 2,3,7,8-tetrachlorodibenzo-p-dioxin
Q Ma1, K T Baldwin, A J Renzelli
1Receptor Biology Laboratory, Toxicology and Molecular Biology Branch, Health Effects Laboratory Division, National Institute for Occupational Safety and Health, Centers for Disease Control and Prevention, Morgantown, West Virginia 26505, USA. qam1@cdc.gov
Abstract:
2,3,7,8-Tetrachlorodibenzo-p-dioxin (TCDD) causes pleotropic effects in mammalian species through modulating gene expression. Here we analyzed TCDD-induced mRNA expression by using mRNA differential display and report the cloning of a novel TCDD-inducible poly(ADP-ribose) polymerase (TiPARP). TiPARP cDNA contains an open reading frame of 657 amino acid residues; the carboxyl half shares sequence similarity to the catalytic domain of PARP, a family of enzymes that catalyze poly ADP-ribosylation of proteins. Expression of the cDNA by in vitro transcription/translation reveals a protein of approximately 75 kDa. The expressed TiPARP exhibits PARP activity toward histone. TiPARP is highly homologous to RM1 which is induced during long-term potentiation, a memory formation process, and to TIL which is induced in T cells infiltrating progressing tumors. TiPARP mRNA is expressed in a broad range of mouse tissues. Together, these data demonstrate that TiPARP is a novel target of TCDD that may contribute to multiple responses to TCDD by modulating protein function through poly ADP-ribosylation.
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