Two Tests of the Direction of Elongation of Poly(ADP-ribose): Residues are Added at the Polymerase-Proximal Terminus

Ikejima, Miyoko; Marsischky, Gerald; Gill, D M

doi:10.1007/978-1-4615-8507-7_12

Cited by 7 publications

(16 citation statements)

References 7 publications

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“…Therefore, the alternative model of PAR synthesis as proposed by Ikejima et al. (57) seems to be quite reasonable in this case and should be discussed.…”

Section: The ‘Structural Basis' Of Poly(adp-ribosyl)ationmentioning

confidence: 85%

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Alemasova

Lavrik

2019

Nucleic Acids Research

332

243

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Poly(ADP-ribosyl)ation (PARylation) is posttranslational modification of proteins by linear or branched chains of ADP-ribose units, originating from NAD+. The central enzyme for PAR production in cells and the main target of poly(ADP-ribosyl)ation during DNA damage is poly(ADP-ribose) polymerase 1 (PARP1). PARP1 ability to function as a catalytic and acceptor protein simultaneously made a considerable contribution to accumulation of contradictory data. This topic is directly related to other questions, such as the stoichiometry of PARP1 molecules in auto-modification reaction, direction of the chain growth during PAR elongation and functional coupling of PARP1 with PARylation targets. Besides DNA damage necessary for the folding of catalytically active PARP1, other mechanisms appear to be required for the relevant intensity and specificity of PARylation reaction. Indeed, in recent years, PARP research has been enriched by the discovery of novel PARP1 interaction partners modulating its enzymatic activity. Understanding the details of PARP1 catalytic mechanism and its regulation is especially important in light of PARP-targeted therapy and may significantly aid to PARP inhibitors drug design. In this review we summarize old and up-to-date literature to clarify several points concerning PARylation mechanism and discuss different ways for regulation of PAR synthesis by accessory proteins reported thus far.

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“…Therefore, the alternative model of PAR synthesis as proposed by Ikejima et al. (57) seems to be quite reasonable in this case and should be discussed.…”

Section: The ‘Structural Basis' Of Poly(adp-ribosyl)ationmentioning

confidence: 85%

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Alemasova

Lavrik

2019

Nucleic Acids Research

332

243

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show abstract

“…In the presence of anti‐Fas antibody and a caspase inhibitor, PARP is activated and depletes the cells of ATP and NAD. PARP hydrolyzes NAD into an ADP‐ribose moiety and nicotinamide (Hayaishi and Ueda, 1977; Ikejima et al, 1987). The nicotinamide released from NAD by poly(ADP‐ribosylation) is reconverted to NAD in a reaction that consumes ATP.…”

Section: Discussionmentioning

confidence: 99%

Re‐evaluation of the distinction between type I and type II cells: The necessary role of the mitochondria in both the extrinsic and intrinsic signaling pathways upon fas receptor activation

Tafani

Karpinich²,

Serroni

et al. 2006

Journal Cellular Physiology

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Cyclosporin A (CyA) and bongkrekic acid (BK) prevented Fas-induced apoptosis in two type I cell lines (H9 and SKW6.4) and two type II cell lines (Jurkat and CEM). CyA and BK inhibited the release of cytochrome c in all four cell lines. In type I cells and in CEM cells, CyA and BK did not prevent the translocation of Bax to the mitochondria. In these same cells, full-length Bid decreased in the mitochondria and cytosol. The cleavage product of Bid, tBid, appeared in the cytosol and to a lesser extent in the mitochondria. In Jurkat cells, Bid also decreased in the cytosol, but increased in the mitochondria. Similar to the other cells, tBid appeared in the mitochondria and cytosol. In the type I H9 and SKW6.4 cells and type II Jurkat cells, the caspase-8 inhibitor Z-Ile-Glu(OMe)-Thr-Asp(OMe)-CH2F (IETD) prevented the cell killing. In the type I cells, IETD prevented the translocation of Bax, the degradation of Bid and the accumulation of tBid. By contrast, IETD only marginally protected the type II CEM cells. In these cells in the presence of IETD, Bax translocated to the mitochondria, in the absence of any degradation of Bid or accumulation of tBid. In the type I H9 cells, IETD produced a depletion of ATP, an effect that did not occur in the type II CEM cells. It is concluded that in type I cells the extrinsic signaling pathway is mitochondrial dependent to the same extent as is the intrinsic pathway in type II cells.

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“…PARP hydrolyzed NAD into an ADP-ribose moiety and nicotinamide (40,41). Repetition of this activity produced extended chains of ADP-ribose.…”

Section: Expression Of Pro-apoptotic Proteins In Jurkat Cells-thementioning

confidence: 99%

Cytochrome c Release upon Fas Receptor Activation Depends on Translocation of Full-length Bid and the Induction of the Mitochondrial Permeability Transition

Tafani¹,

Karpinich²,

Hurster³

et al. 2002

Journal of Biological Chemistry

117

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Two Tests of the Direction of Elongation of Poly(ADP-ribose): Residues are Added at the Polymerase-Proximal Terminus

Cited by 7 publications

References 7 publications

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins

Re‐evaluation of the distinction between type I and type II cells: The necessary role of the mitochondria in both the extrinsic and intrinsic signaling pathways upon fas receptor activation

Cytochrome c Release upon Fas Receptor Activation Depends on Translocation of Full-length Bid and the Induction of the Mitochondrial Permeability Transition

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