Differential regulation of CXC ligand 1 transcription in melanoma cell lines by poly(ADP-ribose) polymerase-1

Amiri, Katayoun I.; Ha, Hyo Chol; Smulson, Mark E.; Richmond, Ann

doi:10.1038/sj.onc.1209751

Cited by 44 publications

(39 citation statements)

References 36 publications

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“…Our results suggest that catalytic activity of Parp-1 is important at the Bcl-6 locus, and therefore, a coactivator role (Hassa et al, 2001) is not likely. Others have demonstrated a dual effect at some promoters whereby Parp-1 inhibition represses expression and Parp-1 knockdown has the opposite effect (Amiri et al, 2006;Soldatenkov et al, 2002). The proposed mechanism for this is that Parp-1 binding represses transcription but activation of Parp-1 followed by auto poly-(ADP-ribosylation) and dissociation from DNA leads to induction of transcription.…”

Section: Discussionmentioning

confidence: 99%

“…It can contact DNA directly either by specific sequence recognition (Zhang et al, 2002;Huang et al, 2004;Amiri et al, 2006) or possibly by binding to secondary hairpin structures (Lonskaya et al, 2005;Potaman et al, 2005). In some transcription factor complexes, Parp-1 has a coactivator role and associates with other proteins in a manner that Reduction in PARP activity produces an increase in Bcl-6 transcription.…”

Section: Discussionmentioning

confidence: 99%

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Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription

et al. 2007

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Bcl-6 is a transcription factor that is normally expressed in germinal centre B cells. It is essential for the formation of germinal centres and the production of high-affinity antibodies. Transcriptional downregulation of Bcl-6 occurs on terminal differentiation to plasma cells. Bcl-6 is highly expressed in B-cell non-Hodgkin's lymphoma and, in a subset of cases of diffuse large cell lymphoma, the mechanism of Bcl-6 overexpression involves interruption of normal transcriptional controls. Transcriptional control of Bcl-6 is, therefore, important for normal antibody responses and lymphomagenesis, but little is known of the cis-acting control elements. This report focuses on a region of mouse/human sequence homology in the first intron of Bcl-6, which is a candidate site for such a control element. We demonstrate that poly-(ADP-ribose) polymerase-1 (Parp-1) binds in vitro and in vivo to specific sequences in this region. We further show that PARP inhibitors, and Parp-1 knockdown by siRNA induce Bcl-6 mRNA expression in Bcl-6 expressing cell lines. We speculate that Parp-1 activation plays a role in switching off Bcl-6 transcription and subsequent B-cell exit from the germinal centre.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription

et al. 2007

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“…NF-B was found to be one of the major regulators for GRO1 expression (37,38). The proximal GRO1 promoter was found to contain an NF-B binding site along with a TATA box and an immediate upstream region.…”

Section: Discussionmentioning

confidence: 99%

Identification of GRO1 as a Critical Determinant for Mutant p53 Gain of Function

Yan

Chen

2009

Journal of Biological Chemistry

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Mutant p53 gain of function contributes to cancer progression, increased invasion and metastasis potentials, and resistance to anticancer therapy. The ability of mutant p53 to acquire its gain of function is shown to correlate with increased expression of progrowth genes, such as c-MYC, MDR1, and NF-B2. However, most of the published studies to identify mutant p53 target genes were performed in a cell system that artificially overexpresses mutant p53. Thus, it remains unclear whether such mutant p53 targets can be regulated by endogenous physiological levels of mutant p53. Here, we utilized SW480 and MIA-PaCa-2 cells, in which endogenous mutant p53 can be inducibly knocked down, to identify mutant p53 target genes that potentially mediate mutant p53 gain of function. We found that knockdown of mutant p53 inhibits GRO1 expression, whereas ectopic expression of mutant R175H in p53-null HCT116 cells increases GRO1 expression. In addition, we found that endogenous mutant p53 is capable of binding to and activating the GRO1 promoter. Interestingly, ectopic expression of GRO1 can rescue the proliferative defect in SW480 and MIAPaCa-2 cells induced by knockdown of mutant p53. Conversely, knockdown of endogenous GRO1 inhibits cell proliferation and thus abrogates mutant p53 gain of function in SW480 cells. Taken together, our findings define a novel mechanism by which mutant p53 acquires its gain of function via transactivating the GRO1 gene in cancer cells. Thus, targeting GRO1 for cancer therapy would be applicable to a large portion of human tumors with mutant p53, but the exploration of GRO1 as a potential target should take the mutation status of p53 into consideration.

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“…Poly-(ADP-ribose) polymerase-1, in its inactive state, attaches to specific sequences in the C-X-C-motif chemokine ligand 1 promoter and prevents NF-B (p65/p50) binding and transcription activation. 87 In stress conditions, PARP-1 activation and PAR modification resulted in a loss of its binding to the CXC ligand 1 promoter, thus allowing NF-B binding and enhanced CXC ligand 1 expression. 87 Others 88 showed that PARP-1 binding to the iNOS promoter enhances NO production, and s-nitrosylation of PARP-1 by NO negatively regulated the PARP-1 transactivation of the iNOS gene, likely by altering its binding and/or action at the iNOS promoter.…”

Section: Role Of Parp-1 In Inflammatory Gene Expressionmentioning

confidence: 99%

Signaling Mechanism of Poly(ADP-Ribose) Polymerase-1 (PARP-1) in Inflammatory Diseases

Garg

2011

The American Journal of Pathology

162

140

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Poly(ADP-ribosyl)ation, attaching the ADP-ribose polymer chain to the receptor protein, is a unique posttranslational modification. Poly(ADP-ribose) polymerase-1 (PARP-1) is a well-characterized member of the PARP family. In this review, we provide a general update on molecular structure and structure-based activity of this enzyme. However, we mainly focus on the roles of PARP-1 in inflammatory diseases. Specifically, we discuss the signaling pathway context that PARP-1 is involved in to regulate the pathogenesis of inflammation. PARP-1 facilitates diverse inflammatory responses by promoting inflammation-relevant gene expression, such as cytokines, oxidation-reductionrelated enzymes, and adhesion molecules. Excessive activation of PARP-1 induces mitochondria-associated cell death in injured tissues and constitutes another mechanism for exacerbating inflammation. There are many posttranslational protein modifications (eg, phosphorylation, acetylation, methylation, and ubiquitylation) that are involved in a wide scope of cellular processes, including chromatin remodeling, transcriptional regulation, and signal transmission response to extracellular stimulation. Poly(ADP-ribosyl)ation (PARylation) is one of such essential protein modifications, whereby polymers of ADP-ribose (PARs) are formed from donor NAD ϩ molecules and covalently attached via an ester linkage to glutamic acid and less commonly to aspartic acid or lysine of target proteins.1-3 The target proteins generally contain a PAR-binding consensus motif that frequently overlaps with a functional domain, such as a protein-or DNA-binding domain (DBD), and thus accounts for PAR modification, altering the functional properties of the targets. 4 The process of PARylation is catalyzed by the poly-(ADP-ribose) polymerase (PARP) family of enzymes that consists of 18 members. 5 The PARPs, historically known as poly(ADP-ribose) synthases and poly(ADP-ribose) transferases, 6,7 show different structure, cellular location, and functions. 8,9 Only two members of this family (ie, PARP-1 and PARP-2) are DNA damage related; and PARP-1, the best-understood member, is an abundant nuclear enzyme and accounts for at least 85% of the cellular PARP activity. 10Since the discovery of PAR synthesis and PARP-1 decades ago, 11,12 new discoveries have been consistently published related to their structure, property, and functions. PARP-1 is a multifunctional enzyme and has a key role in the spatial and temporal organization of DNA repair, thus maintaining genome integrity and facilitating cell survival. PARP-1 catalyzes the synthesis and attachment of highly negatively charged PARs to target proteins, including histones, topoisomerases, DNA helicases, and single-strand break repair and base excision repair factors; and facilitates relaxation of the chromatin superstructure, protein-protein interaction, and DNAbinding ability of the members of the DNA repair machinery. A recently published article 13 reviews the role of PARP-1 in DNA repair. In addition, the importance of poly-(ADP-...

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Differential regulation of CXC ligand 1 transcription in melanoma cell lines by poly(ADP-ribose) polymerase-1

Cited by 44 publications

References 36 publications

Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription

Poly-(ADP-ribose) polymerase-1 (Parp-1) binds in a sequence-specific manner at the Bcl-6 locus and contributes to the regulation of Bcl-6 transcription

Identification of GRO1 as a Critical Determinant for Mutant p53 Gain of Function

Signaling Mechanism of Poly(ADP-Ribose) Polymerase-1 (PARP-1) in Inflammatory Diseases

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