Poly(ADPR)polymerase expression and activity during proliferation and differentiation of rat astrocyte and neuronal cultures

Chabert, Magali; Niedergang, Claude; Hog, F.; Partisani, Mariagrazia; Mandel, P.

doi:10.1016/0167-4889(92)90257-c

Cited by 12 publications

(9 citation statements)

References 26 publications

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“…The correlation between differentiation and high levels of poly-ADP-ribosylation activities may be dependent on the cell type. In primary cultures of rat astrocytes, a biphasic increase in nuclear poly-ADP-ribosylation activities was observed (62). The first rise in poly-ADPribosylation occurred at the beginning of cell proliferation, and the second coincided with the start of cell differentiation (after treatment with fibroblast growth factor ␤ or nerve growth factor).…”

Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 93%

“…Alternatively, the results may indicate the participation of distinct MARTs and PARPs that modify different substrates with opposing roles or that produce distinct types of poly-ADPribose structures with opposite activities. When poly-ADPribose levels were directly measured ex vivo, a correlation between high levels of poly-ADP-ribosylation activity and proliferation was observed (56,61,62,251,336). For instance, nuclear poly-ADP-ribosylation activity was shown to increase when quiescent 3T3 cells or B and T lymphocytes were stimulated to proliferate (56,251,336).…”

Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 99%

“…However, in primary cultures of neurons, an initial high level of poly-ADP-ribosylation activities was followed by a decrease. Differentiation was progressively achieved concomitant with only a limited increase of poly-ADP-ribosylation activity during this phase (62). Poly-ADP-ribosylation was recently shown to be upregulated in spermatids during spermiogenesis (270).…”

Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 99%

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Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

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SUMMARY Since poly-ADP ribose was discovered over 40 years ago, there has been significant progress in research into the biology of mono- and poly-ADP-ribosylation reactions. During the last decade, it became clear that ADP-ribosylation reactions play important roles in a wide range of physiological and pathophysiological processes, including inter- and intracellular signaling, transcriptional regulation, DNA repair pathways and maintenance of genomic stability, telomere dynamics, cell differentiation and proliferation, and necrosis and apoptosis. ADP-ribosylation reactions are phylogenetically ancient and can be classified into four major groups: mono-ADP-ribosylation, poly-ADP-ribosylation, ADP-ribose cyclization, and formation of O-acetyl-ADP-ribose. In the human genome, more than 30 different genes coding for enzymes associated with distinct ADP-ribosylation activities have been identified. This review highlights the recent advances in the rapidly growing field of nuclear mono-ADP-ribosylation and poly-ADP-ribosylation reactions and the distinct ADP-ribosylating enzyme families involved in these processes, including the proposed family of novel poly-ADP-ribose polymerase-like mono-ADP-ribose transferases and the potential mono-ADP-ribosylation activities of the sirtuin family of NAD+-dependent histone deacetylases. A special focus is placed on the known roles of distinct mono- and poly-ADP-ribosylation reactions in physiological processes, such as mitosis, cellular differentiation and proliferation, telomere dynamics, and aging, as well as “programmed necrosis” (i.e., high-mobility-group protein B1 release) and apoptosis (i.e., apoptosis-inducing factor shuttling). The proposed molecular mechanisms involved in these processes, such as signaling, chromatin modification (i.e., “histone code”), and remodeling of chromatin structure (i.e., DNA damage response, transcriptional regulation, and insulator function), are described. A potential cross talk between nuclear ADP-ribosylation processes and other NAD+-dependent pathways is discussed.

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Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 93%

Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 99%

Section: Nuclear Adp-ribosylation In Cellular Differentiation and Promentioning

confidence: 99%

See 1 more Smart Citation

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Hassa

Haenni

Elser

et al. 2006

Microbiol Mol Biol Rev

635

644

View full text Add to dashboard Cite

show abstract

“…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). All these studies show that, although PARP-1 is ubiquitously expressed, its modulation, likely through complex transcriptional regulation, is critical to major cellular functions.…”

mentioning

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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FGF2‐mediated upregulation of urokinase‐type plasminogen activator expression requires a MAP‐kinase dependent activation of poly(ADP‐ribose) polymerase

Caldini¹,

Barletta²,

Rosso³

et al. 2004

Journal Cellular Physiology

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Poly(ADP-ribosyl)ation is a post-translational modification of protein occurring in the nucleus by poly(ADP-ribose) polymerase enzyme activity. The main role of poly(ADP-ribose) polymerase system as "nick sensor" and DNA breaks repair is based on its activation via DNA strand breaks. Furthermore, poly(ADP-ribose) polymerase modifies the binding to DNA of several transcriptional factors by poly(ADP-ribosyl)ation, thereby regulating also transcriptional gene expression. We have analyzed whether poly(ADP-ribose) polymerase activity is involved in basic fibroblast growth factor (FGF2)-mediated upregulation of urokinase-type plasminogen activator (uPA) mRNA. We demonstrated that specific inhibition of poly(ADP-ribose) polymerase activity via 3-aminobenzamide (3ABA) or NAD+ deprivation prevents FGF2-mediated uPA mRNA over-expression and cell-associated plasminogen activator (PA) production in GM7373 endothelial cell line. We verified that FGF2 stimulates poly(ADP-ribose) polymerase activity by a DNA strand breaks-independent manner which involves a mitogen-activated protein kinases (MAPK)-dependent pathway, as confirmed by using PD98059 inhibitor and anisomycin stimulation. Poly(ADP-ribose) polymerase involved in this mechanism is mainly the 60 kDa molecular mass isoform, that presents an increase in serine phosphorylation in the presence of FGF2.

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Poly(ADPR)polymerase expression and activity during proliferation and differentiation of rat astrocyte and neuronal cultures

Cited by 12 publications

References 26 publications

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

Nuclear ADP-Ribosylation Reactions in Mammalian Cells: Where Are We Today and Where Are We Going?

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

FGF2‐mediated upregulation of urokinase‐type plasminogen activator expression requires a MAP‐kinase dependent activation of poly(ADP‐ribose) polymerase

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