{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Dikalova A"],"funding":["NCATS NIH HHS","NIAID NIH HHS","NHLBI NIH HHS","NIGMS NIH HHS"],"pagination":["1451-1464"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11116043"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["134(11)"],"pubmed_abstract":["<h4>Background</h4>Nearly half of adults have hypertension, a major risk factor for cardiovascular disease. Mitochondrial hyperacetylation is linked to hypertension, but the role of acetylation of specific proteins is not clear. We hypothesized that acetylation of mitochondrial CypD (cyclophilin D) at K166 contributes to endothelial dysfunction and hypertension.<h4>Methods</h4>To test this hypothesis, we studied CypD acetylation in patients with essential hypertension, defined a pathogenic role of CypD acetylation in deacetylation mimetic CypD-K166R mutant mice and endothelial-specific GCN5L1 (general control of amino acid synthesis 5 like 1)-deficient mice using an Ang II (angiotensin II) model of hypertension.<h4>Results</h4>Arterioles from hypertensive patients had 280% higher CypD acet"],"journal":["Circulation research"],"pubmed_title":["Mitochondrial CypD Acetylation Promotes Endothelial Dysfunction and Hypertension."],"pmcid":["PMC11116043"],"funding_grant_id":["T32 AI060519","K23 GM129662","R01 HL164909","UL1 TR000445","R01 HL157583","R01 GM112871","R01 HL144943","R35 GM145375"],"pubmed_authors":["Billings FT","Ao M","Sack MN","Dikalov S","Dikalova A","Mayorov V","Amarnath V","Fehrenbach D","Lopez MG","Lantier L","Panov A"],"additional_accession":[]},"is_claimable":false,"name":"Mitochondrial CypD Acetylation Promotes Endothelial Dysfunction and Hypertension.","description":"<h4>Background</h4>Nearly half of adults have hypertension, a major risk factor for cardiovascular disease. Mitochondrial hyperacetylation is linked to hypertension, but the role of acetylation of specific proteins is not clear. We hypothesized that acetylation of mitochondrial CypD (cyclophilin D) at K166 contributes to endothelial dysfunction and hypertension.<h4>Methods</h4>To test this hypothesis, we studied CypD acetylation in patients with essential hypertension, defined a pathogenic role of CypD acetylation in deacetylation mimetic CypD-K166R mutant mice and endothelial-specific GCN5L1 (general control of amino acid synthesis 5 like 1)-deficient mice using an Ang II (angiotensin II) model of hypertension.<h4>Results</h4>Arterioles from hypertensive patients had 280% higher CypD acet","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 May","modification":"2026-06-03T07:52:59.714Z","creation":"2026-05-29T03:06:32.051Z"},"accession":"S-EPMC11116043","cross_references":{"pubmed":["38639088"],"doi":["10.1161/CIRCRESAHA.123.323596","10.1161/circresaha.123.323596"]}}