Modulation of Chromatin Structure by Poly(ADP-Ribosyl)ation

Huletsky, Ann; Murcia, Gilbert de; Muller, Sylviane; Lamarre, Daniel; Hengartner, M; Poirier, Guy G.

doi:10.1007/978-1-4615-8507-7_30

Cited by 12 publications

(15 citation statements)

References 18 publications

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“…15) and an inactive mutant of CrmA (11) were purified from E. coli-expressed material. Bovine PARP was purified as described (17). The anti-PARP monoclonal antibody clone C-2-10 (18) recognizes an epitope near the N-terminal end of PARP, located between amino acids 216 and 375.…”

Section: Methodsmentioning

confidence: 99%

Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B.

Quan

Tewari

O’Rourke

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

169

101

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Section: Methodsmentioning

confidence: 99%

Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B.

Quan

Tewari

O’Rourke

et al. 1996

Proc. Natl. Acad. Sci. U.S.A.

169

101

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“…Enzyme Purification-PARP was purified to homogeneity from bovine thymus essentially as described by Zahradka and Ebisuzaki (22) and modified by Huletsky et al (23). The specific activity of the purified enzyme was 1341 units/mg protein.…”

Section: Materials-[mentioning

confidence: 99%

Cleavage of Automodified Poly(ADP-ribose) Polymerase during Apoptosis

Germain¹,

Affar²,

D’Amours³

et al. 1999

Journal of Biological Chemistry

412

269

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The abundant nuclear enzyme poly(ADP-ribose) polymerase (PARP) synthesizes poly(ADP-ribose) in response to DNA strand breaks. During almost all forms of apoptosis, PARP is cleaved by caspases, suggesting the crucial role of its inactivation. A few studies have also reported a stimulation of PARP during apoptosis. However, the role of PARP stimulation and cleavage during this cell death process remains poorly understood. Here, we measured the stimulation of endogenous poly(ADPribose) synthesis during VP-16-induced apoptosis in HL60 cells and found that PARP was cleaved by caspases at the time of its poly(ADP-ribosyl)ation. In vitro experiments showed that PARP cleavage by caspase-7, but not by caspase-3, was stimulated by its automodification by long and branched poly(ADP-ribose). Consistently, caspase-7 exhibited an affinity for poly(ADP-ribose), whereas caspase-3 did not. In addition, caspase-7 was activated and accumulated in the nucleus of HL60 cells in response to the VP-16 treatment. Furthermore, caspase-7 activation was concommitant with PARP cleavage in the caspase-3-deficient cell line MCF-7 in response to staurosporine treatment. These results strongly suggest that, in vivo, it is caspase-7 that is responsible for PARP cleavage and that poly(ADP-ribosyl)ation of PARP accelerates its proteolysis. Cleavage of the active form of caspase substrates could be a general feature of the apoptotic process, ensuring the rapid inactivation of stress signaling proteins.

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“…These domains allow PARP-1 to bind directly to specific DNA sequences or structures in the regulatory regions of genes (42)(43)(44). PARP-1 has also been shown to modulate chromatin structure and composition by competing with histone for binding to nucleosomes or by PARylation (45,46). In addition, PARP-1 acts as a promoterspecific co-regulator (a co-activator or a co-repressor) for many different transcriptional regulators (39,(47)(48)(49).…”

Section: Discussionmentioning

confidence: 99%

RANKL Up-regulates Brain-type Creatine Kinase via Poly(ADP-ribose) Polymerase-1 during Osteoclastogenesis

Chen

Sun

Mao

et al. 2010

Journal of Biological Chemistry

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Receptor activator of nuclear factor B ligand (RANKL) is the key regulator for osteoclast formation and function. During osteoclastogenesis, RANKL-stimulated signals differentially modulate expression of a large number of proteins. Using proteomics approaches, we identified that brain-type cytoplasmic creatine kinase (Ckb) was greatly induced in mature osteoclasts. Ckb has been shown to contribute to osteoclast function. However, the mechanisms of Ckb regulation and the contribution of other isoforms of creatine kinase during RANKL-induced osteoclastogenesis are unknown. We found that Ckb was the predominant isoform of creatine kinase during osteoclastogenesis. Real-time PCR confirmed that RANKL induced ckb mRNA expression by over 40-fold in primary mouse bone marrow macrophages and Raw 264.7 cells. The RANKL-responsive region was identified within the ؊0.4-to ؊0.2-kb 5-flanking region of the ckb gene. Affinity binding purification followed by mass spectrometry analysis revealed that poly(ADP-ribose) polymerase-1 (PARP-1) bound to the ؊0.4/؊0.2-kb fragment that negatively regulated expression of ckb in response to RANKL stimulation. Electrophoretic mobility shift assays with PARP-1-specific antibody located the binding site of PARP-1 to the TTCCCA consensus sequence. The expression of PARP-1 was reduced during RANKL-induced osteoclastogenesis, concurrently with increased expression of Ckb. Consistently, knockdown of PARP-1 by lentivirus-delivered shRNA enhanced ckb mRNA expression. The activity of PARP-1 was determined to be required for its inhibitory effect on the ckb expression. In summary, we have demonstrated that PARP-1 is a negative regulator of the ckb expression. Down-regulation of PARP-1 is responsible for the up-regulation of ckb during RANKL-induced osteoclastogenesis.

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Modulation of Chromatin Structure by Poly(ADP-Ribosyl)ation

Cited by 12 publications

References 18 publications

Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B.

Proteolytic activation of the cell death protease Yama/CPP32 by granzyme B.

Cleavage of Automodified Poly(ADP-ribose) Polymerase during Apoptosis

RANKL Up-regulates Brain-type Creatine Kinase via Poly(ADP-ribose) Polymerase-1 during Osteoclastogenesis

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