{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,8]],"date-time":"2026-10-08T02:13:04Z","timestamp":1791425584089,"version":"4.3.3"},"reference-count":33,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"7","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["Circulation Research"],"published-print":{"date-parts":[[2011,9,16]]},"abstract":"<jats:sec>\n                    <jats:title>\n                      <jats:underline>Rationale:<\/jats:underline>\n                    <\/jats:title>\n                    <jats:p>Cardiac resynchronization therapy (CRT) is an effective clinical treatment for heart failure patients with conduction delay, impaired contraction, and energetics. Our recent studies have revealed that mitochondrial posttranslational modifications (PTM) may contribute to its benefits, motivating the present study of the oxidative regulation of mitochondrial ATP synthase.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>\n                      <jats:underline>Objectives:<\/jats:underline>\n                    <\/jats:title>\n                    <jats:p>We tested whether CRT alteration of ATP synthase function is linked to cysteine (Cys) oxidative PTM (Ox-PTM) of specific ATP synthase subunits.<\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>\n                      <jats:underline>Methods and Results:<\/jats:underline>\n                    <\/jats:title>\n                    <jats:p>\n                      Canine left ventricular myocardium was collected under conditions to preserve Ox-PTM from control, dyssynchronous heart failure (DHF), or hearts that had undergone CRT. In-gel ATPase activity showed that CRT increased ATPase activity by \u22482-fold (\n                      <jats:italic>P<\/jats:italic>\n                      &lt;0.05) over DHF, approaching control levels, and this effect was recapitulated with a reducing agent. ATP synthase function and 3 Ox-PTM: disulfide bond, S-glutathionylation and S-nitrosation were assessed. ATP synthase from DHF hearts contained 2 novel disulfide bonds, between ATP synthase \u03b1 subunits themselves and between \u03b1 and \u03b3 subunits, both of which were decreased in CRT hearts (4.38\u00b10.13- and 4.23\u00b10.36-fold, respectively,\n                      <jats:italic>P<\/jats:italic>\n                      &lt;0.01). S-glutathionylation of ATP synthase \u03b1 subunit occurred in DHF hearts and was decreased by CRT (1.56\u00b10.16-fold,\n                      <jats:italic>P<\/jats:italic>\n                      &lt;0.04). In contrast, S-nitrosation of ATP synthase \u03b1 subunit in DHF hearts was lower than in CRT hearts (1.53\u00b10.19-fold,\n                      <jats:italic>P<\/jats:italic>\n                      &lt;0.05). All modifications occurred at ATP synthase \u03b1 subunit Cys294 and Cys to Ser mutation indicated that this residue is critical for ATP synthase function.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>\n                      <jats:underline>Conclusions:<\/jats:underline>\n                    <\/jats:title>\n                    <jats:p>A selective Cys in ATP synthase \u03b1 subunit is targeted by multiple Ox-PTM suggesting that this Cys residue may act as a redox sensor modulating ATP synthase function.<\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/circresaha.111.246124","type":"journal-article","created":{"date-parts":[[2011,8,5]],"date-time":"2011-08-05T00:53:25Z","timestamp":1312505605000},"page":"750-757","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":153,"title":["Redox Regulation of Mitochondrial ATP Synthase"],"prefix":"10.1161","volume":"109","author":[{"given":"Sheng-Bing","family":"Wang","sequence":"first","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"D. Brian","family":"Foster","sequence":"additional","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jasma","family":"Rucker","sequence":"additional","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Brian","family":"O'Rourke","sequence":"additional","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David A.","family":"Kass","sequence":"additional","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jennifer E.","family":"Van Eyk","sequence":"additional","affiliation":[{"name":"From the Department of Medicine (S.-B.W., B.F., J.R., B.O'R., D.A.K., J.E.V.E.), Division of Cardiology, and Department of Biological Chemistry (J.E.V.E.), Johns Hopkins University, Baltimore MD."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"e_1_3_4_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.hrthm.2009.08.017"},{"key":"e_1_3_4_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ddmec.2010.07.003"},{"key":"e_1_3_4_4_2","doi-asserted-by":"publisher","DOI":"10.1161\/CIRCGENETICS.109.871236"},{"key":"e_1_3_4_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2010.02.020"},{"key":"e_1_3_4_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2004.09.011"},{"key":"e_1_3_4_7_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI200524408"},{"key":"e_1_3_4_8_2","doi-asserted-by":"publisher","DOI":"10.1002\/pmic.200700962"},{"key":"e_1_3_4_9_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M602118200"},{"key":"e_1_3_4_10_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10863-009-9217-7"},{"key":"e_1_3_4_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.freeradbiomed.2007.07.014"},{"key":"e_1_3_4_12_2","doi-asserted-by":"publisher","DOI":"10.1089\/ars.2007.1845"},{"key":"e_1_3_4_13_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M110.200584"},{"key":"e_1_3_4_14_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M805310200"},{"key":"e_1_3_4_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0076-6879(10)74009-X"},{"key":"e_1_3_4_16_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M700076-MCP200"},{"key":"e_1_3_4_17_2","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(91)90094-A"},{"key":"e_1_3_4_18_2","doi-asserted-by":"publisher","DOI":"10.1074\/mcp.M110.004721"},{"key":"e_1_3_4_19_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1471-4159.2009.06055.x"},{"key":"e_1_3_4_20_2","first-page":"Unit10.25","article-title":"Preparation of proteins and peptides for mass spectrometry analysis in a bottom-up proteomics workflow","volume":"10","author":"Gundry RL","year":"2009","unstructured":"Gundry RL, White MY, Murray CI, Kane LA, Fu Q, Stanley BA, Van Eyk JE. 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