Inhibition of Mono-ADP-Ribosyltransferase Activity during the Execution Phase of Apoptosis Prevents Apoptotic Body Formation

Lodhi, Irfan J.; Clift, Russell E.; Omann, Geneva M.; Sweeney, John F.; McMahon, Kathryn K.; Hinshaw, Daniel B.

doi:10.1006/abbi.2000.2215

Cited by 15 publications

(12 citation statements)

References 36 publications

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“…The argininemono-ADP-ribosylation causes a decrease in intracellular cyclic-ADP-ribose and a subsequent decrease in Ca 2ϩ influx, resulting in apoptosis of the activated T cells (21,153). Another recent study provided evidence that arginine-mono-ADP-ribosylation of actin during the execution phase of apoptosis could induce apoptotic body formation (236). Cytoskeletal features of apoptosis, leading to apoptotic body formation and release, were inhibited by meta-iodobenzylguanidine, an inhibitor of arginine-mono-ADP-ribosyltransferases.…”

Section: Adp-ribosylation Reactions In Cell Death Processesmentioning

confidence: 99%

“…Cytoskeletal features of apoptosis, leading to apoptotic body formation and release, were inhibited by meta-iodobenzylguanidine, an inhibitor of arginine-mono-ADP-ribosyltransferases. Suppression of mono-ADP-ribosylation as late as 2 h after UV irradiation blocked the depolymerization of actin and release of apoptotic bodies (236). Further investigation is needed to determine if cell death processes could also be regulated or induced by nuclear mono-ADP-ribosylation reactions mediated by Pl-MARTs or SIRTs.…”

Section: Adp-ribosylation Reactions In Cell Death Processesmentioning

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: Adp-ribosylation Reactions In Cell Death Processesmentioning

confidence: 99%

Section: Adp-ribosylation Reactions In Cell Death Processesmentioning

confidence: 99%

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

“…Up-regulation of ADP-ribosyltransferase and the down-regulation of ADP-ribosylarginine hydrolase in apoptotic CGCs is in support of the recent involvement of ADP-ribosylation in apoptosis [50]. ADPribosyltransferase, in fact, catalyzes the transfer of ADPribose to an arginine residue in proteins, whereas ADPribosylarginine hydrolase catalyzes the reverse reaction by removing ADP-ribose and regenerating free arginine.…”

Section: Metabolismmentioning

confidence: 76%

A Genomic Approach to Investigate Neuronal Apoptosis

Cavallaro

Calissano

2006

CAR

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Apoptosis has been postulated to play a possible causal role in the onset of Alzheimer's disease due to shortage of trophic supply, deafferentation and excessive production of free radicals. Many experiments in the past have demonstrated the requirement of de novo gene expression during neuronal apoptosis. In view of the possible involvement of apoptotic processes in Alzheimer's disease and to begin a comprehensive survey of the gene-based molecular mechanisms that underlie these events we have used genome scale screening by DNA microarray technology in cerebellar granule neurons following serum and potassium deprivation. From the 8740 genes interrogated by the microarrays, 423 genes were found regulated both at the transcriptional and post-transcriptional level and segregated into distinct clusters. Functional clustering based on gene ontologies showed coordinated expression of genes with common biological functions and metabolic pathways. Among the genes implicated in apoptotic cerebellar granule neurons, 70 were in common with those differentially expressed in cortical neurons exposed to amyloid beta-protein, indicating the existence of common mechanisms responsible of neuronal cell death. This new approach offer a genomic view of the changes that accompany neuronal apoptosis and yield new insights into the molecular basis underlying it.

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“…And cell death in the apoptotic model required the presence of a cell surface mono (ADPribosyl) transferase (ART) (Adriouch et al 2001). Moreover, inhibition of mono-ADP-ribosyltransferase activity specifically suppressed actin filament disassembly and apoptotic body formation (Lodhi et al 2001). With these findings, we conclude that ART3 may be associated with neurons apoptosis caused by TBI.…”

Section: Discussionmentioning

confidence: 90%

The expression pattern of ADP-ribosyltransferase 3 in rat traumatic brain injury

et al. 2011

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Mammalian ecto ADP-ribosyltransferases (ARTs) can regulate the biological functions of various types of cells by catalyzing the transfer of single ADP-ribose moiety from NAD+ to a specific amino acid in a target protein. ART3 is a member of the known ART family which is involved in cell division, DNA-repair and the regulation of the inflammatory response. To elucidate the expression, cellular localization and possible functions of ART3 in central nervous system (CNS) lesion and repair, we performed an acute traumatic brain injury model in adult rats. Western blot analysis showed that the expression of ART3 in ipsilateral brain cortex increased, then reached a peak at day 3 after traumatic brain injury (TBI), and gradually declined during the following days. But in the contralateral brain cortex, no obvious alterations were observed. Immunohistochemistry revealed the highly significant accumulation of ART3 at the ipsilateral brain in comparison to contralateral cerebral cortex. Double immunofluorescence labeling suggested that ART3 was localized mainly in the plasmalemma of neurons, but not in astrocytes or microglias within 3 mm from the lesion site at day 3 post-injury. In addition, we detected the expression profiles of caspase-3 and growth associated protein 43 (GAP-43) whose changes were correlated with the expression profiles of ART3 in this TBI model. Besides, co-localization of ART3/active caspase-3 and ART3/GAP43 were detected in NeuN-positive cells, respectively. Moreover, Pheochromocytoma (PC12) cells were treated with H₂O₂ to establish an apoptosis model. The results showed that the expression of ART3 was increased in the concentration and time dependence way. To further examine the involvement of ART3 in apoptosis of PC12, 3-Methoxybenzamide was used in flow cytometry analysis of apoptotic cells stained with Annexin V and PI. The experimental group in which 3-Methoxybenzamide used had a relative low level of apoptotic index compared with the untreated group. Together with previous reports, we hypothesize that ART3 may play important roles in CNS pathophysiology after TBI and further research is needed to have a good understanding of its function and mechanism.

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Inhibition of Mono-ADP-Ribosyltransferase Activity during the Execution Phase of Apoptosis Prevents Apoptotic Body Formation

Cited by 15 publications

References 36 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?

A Genomic Approach to Investigate Neuronal Apoptosis

The expression pattern of ADP-ribosyltransferase 3 in rat traumatic brain injury

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