First Author | Ma Q | Year | 2001 |
Journal | Biochem Biophys Res Commun | Volume | 289 |
Issue | 2 | Pages | 499-506 |
PubMed ID | 11716501 | Mgi Jnum | J:73109 |
Mgi Id | MGI:2154582 | Doi | 10.1006/bbrc.2001.5987 |
Citation | Ma Q, et al. (2001) TCDD-Inducible Poly(ADP-ribose) Polymerase: A Novel Response to 2,3,7,8-Tetrachlorodibenzo-p-dioxin. Biochem Biophys Res Commun 289(2):499-506 |
abstractText | 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. (c)2001 Elsevier Science. |