Decreased heterogeneity of CS histone variants after hydrolysis of the ADP‐ribose moiety

Imschenetzky, María; Morín, Violeta; Carvajal, Nelson; Montecino, Martín; Puchi, Marcia

doi:10.1002/(sici)1097-4644(19960401)61:1<109::aid-jcb12>3.0.co;2-j

Cited by 6 publications

(4 citation statements)

References 36 publications

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“…However, two seminal studies published by Sajish www.nature.com/scientificreports www.nature.com/scientificreports/ et al have established a SIRT1 independent mechanism of action for RSV through other potential targets, such as mammalian phosphodiesterase-4 (PDE4) and poly-ADP-ribose polymerase-1 (PARP1) 21,22 . Interestingly, PDE4 degrades poly(ADP-ribose) polymer and recycles the ADP-ribose into adenosine monophosphate (AMP) units, resulting in a transient competitive inhibition of cAMP hydrolysis [23][24][25][26] . cAMPs regulate the localization, duration, and amplitude of cyclic nucleotide signaling.…”

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Nicotinamide Augments the Anti-Inflammatory Properties of Resveratrol through PARP1 Activation

Yanez

Jhanji

Murphy

et al. 2019

Sci Rep

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Resveratrol (RSV) and nicotinamide (NAM) have garnered considerable attention due to their anti-inflammatory and anti-aging properties. NAM is a transient inhibitor of class III histone deacetylase SIRTs (silent mating type information regulation 2 homologs) and SIRT1 is an inhibitor of poly-ADP-ribose polymerase-1 (PARP1). The debate on the relationship between RSV and SIRT1 has precluded the use of RSV as a therapeutic drug. Recent work demonstrated that RSV facilitates tyrosyl-tRNA synthetase (TyrRS)-dependent activation of PARP1. Moreover, treatment with NAM is sufficient to facilitate the nuclear localization of TyrRS that activates PARP1. RSV and NAM have emerged as potent agonists of PARP1 through inhibition of SIRT1. In this study, we evaluated the effects of RSV and NAM on pro-inflammatory macrophages. Our results demonstrate that treatment with either RSV or NAM attenuates the expression of pro-inflammatory markers. Strikingly, the combination of RSV with NAM, exerts additive effects on PARP1 activation. Consistently, treatment with PARP1 inhibitor antagonized the anti-inflammatory effect of both RSV and NAM. For the first time, we report the ability of NAM to augment PARP1 activation, induced by RSV, and its associated anti-inflammatory effects mediated through the induction of BCL6 with the concomitant down regulation of COX-2.

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confidence: 99%

Nicotinamide Augments the Anti-Inflammatory Properties of Resveratrol through PARP1 Activation

Yanez

Jhanji

Murphy

et al. 2019

Sci Rep

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“…In sea urchin sperm, the five histones are found in an unmodified form. By contrast , the CS histone variants are extensively poly(ADPribosylated) in unfertilized eggs [Imschenetzky et al, 1996b]. Shortly after fertilization, sperm histone variants SpH1 and SpH2B become phosphorylated.…”

Section: Post-translational Modifications Of Histones At Fertilizationmentioning

confidence: 99%

“…In contrast with sperm histones, the CS histone variants that organize the chromatin in sea urchin unfertilized eggs and zygotes and during the initial cleavage divisions are extensively poly(ADP-ribosylated). It was found that the poly(ADP-ribosylation) of CS histone variants changes in a cell cycle-dependent manner and is required for zygotic DNA replication [Imschenetzky et al, 1993;1996b]. This posttranslational modification is catalyzed by the poly(ADP-ribose) synthetase (PARP), a nuclear enzyme found in a wide variety of eukaryotic cells.…”

Section: Post-translational Modifications Of Histones At Fertilizationmentioning

confidence: 99%

Potential involvement of post‐translational modifications as a mechanism modulating selective proteolysis after fertilization

Imschenetzky

Puchi

Morín

et al. 1999

J of Cellular Biochemistry

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The role of proteolysis during fertilization has been investigated only to a very limited extent as compared with its role on the control of cell cycle progression. In this report, we discuss briefly the proteases involved in fertilization, their relevance in the egg-sperm interaction and in the chromatin remodeling that occurs before the reestablishment of the diploid condition of the zygote. We further emphasize how the post-translational modifications of target proteins modulate these proteolytic events. J. Cell. Biochem. Suppls. 32/33:149-157, 1999 Key words: fertilization/proteolysis; phosphorylation; ubiquitination; poly (ADP-ribosylation) Fertilization is a crucial event in bisexual reproduction whereby two cells fuse together creating a new individual that inherits the genetic potentials of both parents. The initial step involves a specific recognition of both gametes followed by the entry of the sperm into the egg. This event promotes the activation of egg metabolism, which is in a quiescent state before fertilization. The consequence of fertilization is the reestablishment of the diploid condition, which precedes the initiation of the developmental program of the resulting zygote.Proteolysis plays essential roles in the spermegg initial interaction, in egg activation, and in the establishment of the diploid condition of the zygotes. In the initial steps of fertilization, proteolysis is required for triggering the acrosomal reaction and sperm penetration of the egg. In a variety of animal species, meiosis in oocytes is arrested at prophase of the first meiotic cell cycle. Reinitiation of meiosis is evidenced by the dissolution of the nuclear envelope, signaled as germinal vesicle breakdown (GVBD), followed by chromosome condensation and the extrusion of the first polar body. GVBD is triggered by the maturation promoting factor (MPF). MPF contains a 34-kDa cyclin-dependent protein kinase (p34cdc2) and cyclin B. Further transition to anaphase is concurrent with the rapid degradation of cyclin B, thus inactivating the MPF. Cyclin B is poly-ubiquitinated by a cyclin-specific ubiquitination cascade of reactions, thus committing this protein to be degraded by the ubiquitin/proteasome pathway. This pathway is highly conserved in eukaryotes and represents the selective cellular degradation mechanism better understood at present. In other species, meiosis is arrested at the end of metaphase I or II, in such condition its reinitiation is triggered by sperm penetration. Finally there are other species, such as sea urchins and sand dollars, in which the final stage of oocyte maturation occurs before fertilization. Consequently, the haploid state is attained before insemination and these eggs remain arrested in the G1 phase of the cell cycle before fertilization.After fertilization, the sperm nucleus decondenses and transforms into male pronucleus, which moves toward the egg pronucleus and fuses at amphimixis, thus reestablishing the diploid condition of the future embryo. Sperm chromatin is condensed by a...

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“…This step is consistently blocked in vivo as well as in vitro by protein kinase inhibitors [Cothreen and Poccia, 1993;Cameron and Poccia, 1994]. Immunobiochemical evidence indicates that at an intermediate step of male pronucleus formation, sperm chromatin is organized into hybrid nucleoprotein particles formed by sperm-specific histones H1 (SpH1) and H2A-H2B (SpH2A-SpH2B), and by a subset of CS histone variants derived from maternal stores [Imschenetzky et al, 1991;1996a;1996b]. Therefore, in the context of the selective proteolysis of the complete set of sperm histones by the SpH-protease, these hybrid nucleoprotein particles containing a partial subset of sperm histones together with CS histone variants are a puzzling observation.…”

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confidence: 99%

Phosphorylation protects sperm-specific histones H1 and H2B from proteolysis after fertilization

Morín¹,

Acuña²,

Díaz³

et al. 2000

J. Cell. Biochem.

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At intermediate stages of male pronucleus formation, sperm-derived chromatin is composed of hybrid nucleoprotein particles formed by sperm H1 (SpH1), dimers of sperm H2A-H2B (SpH2A-SpH2B), and a subset of maternal cleavage stage (CS) histone variants. At this stage in vivo, the CS histone variants are poly(ADP-ribosylated), while SpH2B and SpH1 are phosphorylated. We have postulated previously that the final steps of sperm chromatin remodeling involve a cysteine-protease (SpH-protease) that degrades sperm histones in a specific manner, leaving the maternal CS histone variants unaffected. More recently we have reported that the protection of CS histones from degradation is determined by the poly(ADP-ribose) moiety of these proteins. Because of the selectivity displayed by the SpH-protease, the coexistence of a subset of SpH together with CS histone variants at intermediate stages of male pronucleus remodeling remains intriguing. Consequently, we have investigated the phosphorylation state of SpH1 and SpH2B in relation to the possible protection of these proteins from proteolytic degradation. Histones H1 and H2B were purified from sperm, phosphorylated in vitro using the recombinant alpha-subunit of casein kinase 2, and then used as substrates in the standard assay of the SpH-protease. The phosphorylated forms of SpH1 and SpH2B were found to remain unaltered, while the nonphosphorylated forms were degraded. On the basis of this result, we postulate a novel role for the phosphorylation of SpH1 and SpH2B that occurs in vivo after fertilization, namely to protect these histones against degradation at intermediate stages of male chromatin remodeling.

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Decreased heterogeneity of CS histone variants after hydrolysis of the ADP‐ribose moiety

Cited by 6 publications

References 36 publications

Nicotinamide Augments the Anti-Inflammatory Properties of Resveratrol through PARP1 Activation

Nicotinamide Augments the Anti-Inflammatory Properties of Resveratrol through PARP1 Activation

Potential involvement of post‐translational modifications as a mechanism modulating selective proteolysis after fertilization

Phosphorylation protects sperm-specific histones H1 and H2B from proteolysis after fertilization

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