{"doi":"10.1074/jbc.274.40.28379","title":"Cleavage of Automodified Poly(ADP-ribose) Polymerase during Apoptosis","abstract":null,"journal":"Journal of Biological Chemistry","year":1999,"id":672702,"datarank":0.9170523269748349,"base_score":6.113682179832232,"endowment":6.113682179832232,"self_citation_contribution":0.9170523269748349,"citation_network_contribution":0.0,"self_endowment_contribution":0.9170523269748349,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":451,"citer_count":0,"citers_with_citation_signal":0,"citers_with_endowment":0,"datacite_reuse_total":0,"is_dataset":false,"is_dataset_confidence":null,"is_data_producer":false,"deposit_databanks":null,"is_oa":false,"file_count":0,"downloads":0,"has_version_chain":false,"published_date":null,"fair_score":null,"fair_percentile":null,"algorithm_id":"datarank_citation_only_1hop_v6","ranking_scope":"data_only","authors":[{"id":648484,"name":"El Bachir Affar","orcid":"0000-0002-6374-3683","position":1,"is_corresponding":false},{"id":1757617,"name":"Damien D'Amours","orcid":null,"position":2,"is_corresponding":false},{"id":624286,"name":"Vishva M. Dixit","orcid":"0000-0001-6983-0326","position":3,"is_corresponding":false},{"id":90292,"name":"Guy S. Salvesen","orcid":"0000-0002-7933-6732","position":4,"is_corresponding":false},{"id":263073,"name":"Guy G. Poirier","orcid":"0000-0002-4869-1424","position":5,"is_corresponding":false},{"id":1161450,"name":"Marc Germain","orcid":"0000-0001-7942-3185","position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Cleavage of Automodified Poly(ADP-ribose) Polymerase during Apoptosis","abstract":"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(ADP-ribose) 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.","is_dataset_classified":null,"base_score":0.0,"endowment":0.0,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"10497198","pmcid":null,"openalex_id":null,"authors":[],"funders":[],"total_grants":0,"fwci":null,"citation_percentile":null,"influential_citations":0,"citation_trend":[],"oa_status":"hybrid","license":"cc-by","oa_locations":[{"url":"http://www.jbc.org/article/S0021925819520610/pdf","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925819520610?httpAccept=text/xml","host_type":"publisher"},{"url":"https://api.elsevier.com/content/article/PII:S0021925819520610?httpAccept=text/plain","host_type":"publisher"},{"url":"https://syndication.highwire.org/content/doi/10.1074/jbc.274.40.28379","host_type":"publisher"}],"fields_of_study":[],"mesh_terms":["HL-60 Cells","Humans","Caspases","Poly(ADP-ribose) Polymerases","Apoptosis","Enzyme Activation","Hydrolysis","Caspase 3","Caspase 7"],"keywords":[],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-16T10:27:16.261859Z","pmid":null,"pmcid":null,"fwci":null,"citation_percentile":null,"influential_citations":0,"oa_status":null,"license":null,"views":0,"total_file_size_bytes":0,"version_count":0,"fair_f":null,"fair_a":null,"fair_i":null,"fair_r":null,"fair_zscore":null,"fair_rationale":null,"fair_model":null,"fair_agent_version":null,"fair_fulltext_source":null,"fair_has_llm":null,"fair_computed_at":null,"clinical_trials":[],"software_tools":[],"db_accessions":[],"linked_datasets":[],"topics":[]}