{"doi":"10.1007/bf00926177","title":"Angiotensin II induces phosphatidic acid formation in neonatal rat cardiac fibroblasts: Evaluation of the roles of phospholipases C and D","abstract":null,"journal":"Molecular and Cellular Biochemistry","year":1994,"id":649303,"datarank":0.4566783656585135,"base_score":3.044522437723423,"endowment":3.044522437723423,"self_citation_contribution":0.4566783656585135,"citation_network_contribution":0.0,"self_endowment_contribution":0.4566783656585135,"citer_contribution":0.0,"corpus_percentile":null,"corpus_rank":null,"citation_count":20,"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":1692561,"name":"Mohiuddin M. Taher","orcid":null,"position":1,"is_corresponding":false},{"id":1692563,"name":"Kenneth M. Baker","orcid":null,"position":2,"is_corresponding":false},{"id":109573,"name":"Harold A. Singer","orcid":"0000-0001-8554-3239","position":3,"is_corresponding":false},{"id":117291,"name":"George W. Booz","orcid":null,"position":0,"is_corresponding":false}],"reference_count":0,"raw_metadata":{"has_enrichment":true,"resolved":true,"title":"Angiotensin II induces phosphatidic acid formation in neonatal rat cardiac fibroblasts: Evaluation of the roles of phospholipases C and D","abstract":"Phosphatidic acid has been proposed to contribute to the mitogenic actions of various growth factors. In 32P-labeled neonatal rat cardiac fibroblasts, 100 nM [Sar1]angiotensin II was shown to rapidly induce formation of 32P-phosphatidic acid. Levels peaked at 5 min (1.5-fold above control), but were partially sustained over 2 h. Phospholipase D contributed in part to phosphatidic acid formation, as 32P- or 3H-phosphatidylethanol was produced when cells labeled with [32P]H3PO4 or 1-O-[1,2- 3H]hexadecyl-2-lyso-sn-glycero-3-phosphocholine were stimulated in the presence of 1% ethanol. [Sar1]angiotensin II-induced phospholipase D activity was transient and mainly mediated through protein kinase C (PKC), since PKC downregulation reduced phosphatidylethanol formation by 68%. Residual activity may have been due to increased intracellular Ca2+, as ionomycin also activated phospholipase D in PKC-depleted cells. Phospholipase D did not fully account for [Sar1]angiotensin II-induced phosphatidic acid: 1) compared to PMA, a potent activator of phospholipase D, [Sar1]angiotensin II produced more phosphatidic acid relative to phosphatidylethanol, and 2) PKC downregulation did not affect [Sar1]angiotensin II-induced phosphatidic acid formation. The diacylglycerol kinase inhibitor R59949 depressed [Sar1]angiotensin II-induced phosphatidic acid formation by only 21%, indicating that activation of a phospholipase C and diacylglycerol kinase also can not account for the bulk of phosphatidic acid. Thus, additional pathways not involving phospholipases C and D, such as de novo synthesis, may contribute to [Sar1]angiotensin II-induced phosphatidic acid in these cells. Finally, as previously shown for [Sar1]angiotensin II, phosphatidic acid stimulated mitogen activated protein (MAP) kinase activity.(ABSTRACT TRUNCATED AT 250 WORDS)","is_dataset_classified":null,"base_score":3.044522437723423,"endowment":3.044522437723423,"datacite_reuse_total":0,"file_count":0,"downloads":0,"views":0,"has_version_chain":false,"is_dataset":false,"is_oa":false,"pmid":"7891671","pmcid":null,"openalex_id":"https://openalex.org/W2068569759","authors":[],"funders":[{"funder_name":"NHLBI NIH HHS","grant_id":"HL40992","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"HL44379","title":null},{"funder_name":"NHLBI NIH HHS","grant_id":"HL44883","title":null}],"total_grants":3,"fwci":1.4581,"citation_percentile":0.8198029,"influential_citations":0,"citation_trend":[{"year":2021,"count":2}],"oa_status":"closed","license":"http://www.springer.com/tdm","oa_locations":[{"url":"http://link.springer.com/content/pdf/10.1007/BF00926177.pdf","host_type":"publisher"},{"url":"http://link.springer.com/article/10.1007/BF00926177/fulltext.html","host_type":"publisher"},{"url":"http://link.springer.com/content/pdf/10.1007/BF00926177","host_type":"publisher"},{"url":"https://doi.org/10.1007/bf00926177","host_type":"journal"},{"url":"https://pubmed.ncbi.nlm.nih.gov/7891671","host_type":"repository"}],"fields_of_study":["Protein Kinase Regulation and GTPase Signaling","Cell death mechanisms and regulation","Receptor Mechanisms and Signaling"],"mesh_terms":["Angiotensin II","Animals","Cells, Cultured","Fibroblasts","Heart","Myocardium","Phosphatidic Acids","Phosphatidylcholines","Phosphatidylinositols","Type C Phospholipases","Phospholipase D","Signal Transduction","Rats, Sprague-Dawley","Phosphotransferases (Alcohol Group Acceptor)","Diacylglycerol Kinase","Rats"],"keywords":["Phosphatidic acid","Phosphatidylethanol","Phospholipase D","Angiotensin II","Diacylglycerol kinase","PLD2","Phospholipase","Protein kinase C","Phospholipase C","Chemistry","Biochemistry","Biology","Endocrinology","Signal transduction","Phospholipid","Enzyme","Receptor"],"sdg_mappings":[],"linked_datasets":[],"clinical_trials":[],"software_tools":[],"database_accessions":[],"source":"live","citation_network_status":"fetched"},"created_at":"2026-08-10T03:30:03.285935Z","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":[]}