Cell cycle-related expression of poly(ADP-ribosyl)transferase in proliferating rat thymocytes

Wein, Karl-Heinz; Netzker, Roland; Brand, Karl

doi:10.1016/0167-4889(93)90179-s

Cited by 13 publications

(9 citation statements)

References 34 publications

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“…ERK1/2 kinase has also been reported to phosphorylate and activate PARP-1 (Kauppinen et al, 2006). There is a strong evidence in the literature showing that PARP expression and activity are affected by differentiation and cell proliferation with generally higher PARP activity and expression in proliferating cells (Wein et al, 1993). Negroni and Bertazzoni (1993) showed that growing HeLa cells and mitogen-stimulated human lymphocytes have very similar levels of PARP-1 mRNA, whereas in quiescent lymphocytes the value was 20-fold lower.…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP-ribose) polymerase-1 polymorphisms, expression and activity in selected human tumour cell lines

et al. 2009

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BACKGROUND: Poly(ADP-ribose) polymerase-1 (PARP-1) is a DNA-binding enzyme activated by DNA breaks and involved in DNA repair and other cellular processes. Poly(ADP-ribose) polymerase activity can be higher in cancer than in adjacent normal tissue, but cancer predisposition is reported to be greater in individuals with a single-nucleotide polymorphism (SNP) V762A (T2444C) in the catalytic domain that reduces PARP-1 activity. METHODS: To resolve these divergent observations, we determined PARP-1 polymorphisms, PARP-1 protein expression and activity in a panel of 19 solid and haematological, adult and paediatric human cancer cell lines. RESULTS: There was a wide variation in PARP activity in the cell line panel (coefficient of variation, CV ¼ 103%), with the lowest and the highest activity being 2460 pmol PAR/10 6 (HS-5 cells) and 85 750 pmol PAR/10 6 (NGP cells). Lower variation (CV ¼ 32%) was observed in PARP-1 protein expression with the lowest expression being 2.0 ng mg À1 (HS-5 cells) and the highest being 7.1 ng mg À1 (ML-1 cells). The mean activity in the cancer cells was 45-fold higher than the mean activity in normal human lymphocytes and the PARP-1 protein levels were 23-fold higher. CONCLUSIONS: Surprisingly, there was no significant correlation between PARP activity and PARP-1 protein level or the investigated polymorphisms, T2444C and CA.

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Section: Discussionmentioning

confidence: 99%

Poly(ADP-ribose) polymerase-1 polymorphisms, expression and activity in selected human tumour cell lines

et al. 2009

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“…PARP-1 acts at the S phase, both by participating in a multiprotein DNA replication complex (SimbulanRosenthal et al, 1996) and by acting as a positive regulator of E2F1-mediated transcription and, hence, of S-phase gene expression (Simbulan-Rosenthal et al, 1999. Moreover, previous evidence correlated increased PARP expression and activity with liver regeneration (Cesarone et al, 1990), PBMC activation (Menegazzi et al, 1992) and thymocyte proliferation (Wein et al, 1993), but the role of PARPs in cell cycle re-entry was not further investigated.…”

Section: Discussionmentioning

confidence: 99%

Poly(ADP-ribosyl)ation is implicated in the G0–G1 transition of resting cells

et al. 2008

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Poly(ADP-ribosyl)ation, catalysed by a family of poly (ADP-ribose) polymerases (PARPs), plays an important role in a large variety of physiological processes, including cell proliferation, but its role in cell cycle progression is not yet completely defined. As reported here, the examination of early times following serum stimulation of quiescent fibroblasts suggests that poly(ADP-ribosyl) ation is necessary for the transition from the G0 phase to the G1 phase. We show that PARP activity is involved in this step through the regulation of immediate-early response genes, such as c-Fos and c-Myc. This is supported by the finding that exogenous Myc expression substantially restores cell cycle reactivation in the absence of polymer synthesis. Furthermore, using RNA interference, we show that PARP-1 is the PARP family member playing the most prominent role in the upregulation of c-Fos and c-Myc during G0-G1 transition. We report that even in lectin-stimulated peripheral blood mononucleated cells, the inhibition of PARP activity interferes with the upregulation of immediate-early genes and delays the induction of proliferation, suggesting a general role for PARP-1 in linking growth factor signaling with cell cycle entry.

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“…Although PARP-1, the main poly(ADP-ribosyl)ating enzyme (2), is expressed in a variety of cells and organs, its transcriptional regulation during cell cycle progression, cell proliferation, and differentiation is likely to impact on the timing and extent of PARP-1 activity and function. Indeed, it has been shown that PARP-1 mRNA levels increase just before maximal enzymatic activity during thymocyte proliferation (22), astrocyte proliferation and differentiation (25), and lymphocyte activation (28). Furthermore, elevated levels of PARP-1 mRNA apparently account for the enhanced poly(ADP-ribosyl)ation observed in Ewing's sarcoma cells (24).…”

Section: Discussionmentioning

confidence: 99%

“…PARP-1 mRNA level is regulated at the cell cycle level, reaching its peak at either the G 1 (17)(18)(19)(20) or the S phases (21,22). It has also been shown that a decrease in PARP-1 mRNA levels is associated with cellular differentiation (23)(24)(25)(26) and senescence (27), whereas an increase is observed upon activation of lymphocytes (17,28) or peripheral blood mononuclear cells (18).…”

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confidence: 99%

Nuclear Factor 1 Interferes with Sp1 Binding through a Composite Element on the Rat Poly(ADP-ribose) Polymerase Promoter to Modulate Its Activity in Vitro

Laniel

Poirier

Guérin

2001

Journal of Biological Chemistry

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Poly(ADP-ribose) polymerase-1 (PARP-1) catalyzes the rapid and extensive poly(ADP-ribosyl)ation of nuclear proteins in response to DNA strand breaks, and its expression, although ubiquitous, is modulated from tissue to tissue and during cellular differentiation. PARP-1 gene promoters from human, rat, and mouse have been cloned, and they share a structure common to housekeeping genes, as they lack a functional TATA box and contain multiple GC boxes, which bind the transcriptional activator Sp1. We have previously shown that, although Sp1 is important for rat PARP1 (rPARP) promoter activity, its finely tuned modulation is likely dependent on other transcription factors that bind the rPARP proximal promoter in vitro. In this study, we identified one such factor as NF1-L, a rat liver isoform of the nuclear factor 1 family of transcription factors. The NF1-L site on the rPARP promoter overlaps one of the Sp1 binding sites previously identified, and we demonstrated that binding of both factors to this composite element is mutually exclusive. Furthermore, we provide evidence that NF1-L has no effect by itself on rPARP promoter activity, but rather down-regulates the Sp1 activity by interfering with its ability to bind the rPARP promoter in order to modulate transcription of the rPARP gene.Poly(ADP-ribose) polymerase-1 (PARP-1) 1 is a nuclear enzyme which catalyzes the addition of ADP-ribose units from nicotinamide adenine dinucleotide (NAD ϩ ) onto itself and other nuclear proteins such as histones and topoisomerases (reviewed in Refs. 1 and 2). It is made up of three functional domains, namely the amino-terminal DNA-binding domain, the central automodification domain, and the carboxyl-terminal catalytic domain (3). Although PARP-1 is often associated with DNA repair, because of its rapid and extensive activation following DNA damage (4, 5), it has also been implicated in other major nuclear functions such as transcription (6, 7), DNA replication (8, 9) and recombination (10). PARP-1 is also important for cell differentiation (11-13) and is involved in cell death, likely acting as a molecular switch between apoptosis and necrosis (14).PARP-1 is expressed in all organs, albeit at varying degrees, with highest mRNA expression found in brain, thymus, heart, and testis (15, 16). PARP-1 mRNA level is regulated at the cell cycle level, reaching its peak at either the G 1 (17-20) or the S phases (21, 22). It has also been shown that a decrease in PARP-1 mRNA levels is associated with cellular differentiation (23-26) and senescence (27), whereas an increase is observed upon activation of lymphocytes (17, 28) or peripheral blood mononuclear cells (18). All these studies show that, although PARP-1 is ubiquitously expressed, its modulation, likely through complex transcriptional regulation, is critical to major cellular functions.In order to better understand the transcriptional mechanisms regulating PARP-1 expression, the PARP-1 gene promoter has been identified and cloned from three mammalian species, human (29, 30), rat (31), ...

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Cell cycle-related expression of poly(ADP-ribosyl)transferase in proliferating rat thymocytes

Cited by 13 publications

References 34 publications

Poly(ADP-ribose) polymerase-1 polymorphisms, expression and activity in selected human tumour cell lines

Poly(ADP-ribose) polymerase-1 polymorphisms, expression and activity in selected human tumour cell lines

Poly(ADP-ribosyl)ation is implicated in the G0–G1 transition of resting cells

Nuclear Factor 1 Interferes with Sp1 Binding through a Composite Element on the Rat Poly(ADP-ribose) Polymerase Promoter to Modulate Its Activity in Vitro

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