{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,2]],"date-time":"2026-04-02T07:46:42Z","timestamp":1775116002425,"version":"3.50.1"},"reference-count":16,"publisher":"Wiley","issue":"6","license":[{"start":{"date-parts":[[2026,3,17]],"date-time":"2026-03-17T00:00:00Z","timestamp":1773705600000},"content-version":"vor","delay-in-days":16,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"},{"start":{"date-parts":[[2026,3,1]],"date-time":"2026-03-01T00:00:00Z","timestamp":1772323200000},"content-version":"tdm","delay-in-days":0,"URL":"http:\/\/doi.wiley.com\/10.1002\/tdm_license_1.1"}],"content-domain":{"domain":["physoc.onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Physiological Reports"],"published-print":{"date-parts":[[2026,3]]},"abstract":"<jats:title>Abstract<\/jats:title>\n                  <jats:p>\n                    The heart constantly adapts to acute hemodynamic load by increasing contractility and stretch\u2010induced compliance (SIC). The latter involves titin phosphorylation, notably by cGMP\u2010dependent protein kinase (PKG). Given that Ca\n                    <jats:sup>2+<\/jats:sup>\n                    \/calmodulin\u2010dependent protein kinase II (CaMKII) also phosphorylates titin and is activated under acute stress via redox signaling, we hypothesized a role for CaMKII in SIC. We assessed passive tension (PT) decay in the 15\u2009min following sudden stretch in isometrically contracting rabbit right ventricular papillary muscles, with or without PKG or CaMKII inhibition. Additionally, Wistar Han rat hearts were Langendorff\u2010perfused and acutely stretched or left unstretched. Skinned cardiomyocytes extracted from these hearts were analyzed for sarcomere length\u2010PT relationships before and after incubation with PKG, CaMKII, or both. Both kinases reduced PT, with diminished effects in pre\u2010stretched cells, suggesting prior kinase activation. PKG inhibition significantly blunted SIC, while CaMKII inhibition showed a similar but non\u2010significant trend. Our findings support that CaMKII contributes to SIC, likely via shared phosphorylation targets with PKG. These results provide mechanistic insight into SIC and suggest CaMKII as a potential modulator of diastolic function during acute stretch, such as in preload challenges.\n                  <\/jats:p>","DOI":"10.14814\/phy2.70709","type":"journal-article","created":{"date-parts":[[2026,3,18]],"date-time":"2026-03-18T06:49:43Z","timestamp":1773816583000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Ca\n                    <sup>2+<\/sup>\n                    \/calmodulin\u2010dependent protein kinase\n                    <scp>II<\/scp>\n                    and protein kinase G independently contribute to acutely enhance myocardial compliance with stretch"],"prefix":"10.14814","volume":"14","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2035-061X","authenticated-orcid":false,"given":"Andr\u00e9 M.","family":"Leite\u2010Moreira","sequence":"first","affiliation":[{"name":"Cardiovascular R&amp;D Centre \u2010 UnIC@RISE, Department of Surgery and Physiology Faculty of Medicine of the University of Porto  Porto Portugal"},{"name":"Department of Anesthesiology S\u00e3o Jo\u00e3o Local Health Unit  Porto Portugal"}]},{"given":"Jo\u00e3o","family":"Almeida\u2010Coelho","sequence":"additional","affiliation":[{"name":"Cardiovascular R&amp;D Centre \u2010 UnIC@RISE, Department of Surgery and Physiology Faculty of Medicine of the University of Porto  Porto Portugal"}]},{"given":"In\u00eas","family":"Falc\u00e3o\u2010Pires","sequence":"additional","affiliation":[{"name":"Cardiovascular R&amp;D Centre \u2010 UnIC@RISE, Department of Surgery and Physiology Faculty of Medicine of the University of Porto  Porto Portugal"}]},{"given":"Andr\u00e9 P.","family":"Louren\u00e7o","sequence":"additional","affiliation":[{"name":"Cardiovascular R&amp;D Centre \u2010 UnIC@RISE, Department of Surgery and Physiology Faculty of Medicine of the University of Porto  Porto Portugal"},{"name":"Department of Anesthesiology S\u00e3o Jo\u00e3o Local Health Unit  Porto Portugal"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-7808-3596","authenticated-orcid":false,"given":"Adelino F.","family":"Leite\u2010Moreira","sequence":"additional","affiliation":[{"name":"Cardiovascular R&amp;D Centre \u2010 UnIC@RISE, Department of Surgery and Physiology Faculty of Medicine of the University of Porto  Porto Portugal"},{"name":"Department of Cardiothoracic Surgery S\u00e3o Jo\u00e3o Local Health Unit  Porto Portugal"}]}],"member":"311","published-online":{"date-parts":[[2026,3,17]]},"reference":[{"key":"e_1_2_10_2_1","doi-asserted-by":"publisher","DOI":"10.1113\/JP283427"},{"key":"e_1_2_10_3_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.yjmcc.2015.10.014"},{"key":"e_1_2_10_4_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00395-018-0688-8"},{"key":"e_1_2_10_5_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12933-018-0732-x"},{"key":"e_1_2_10_6_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2008.02.048"},{"key":"e_1_2_10_7_1","doi-asserted-by":"publisher","DOI":"10.1002\/ehf2.13973"},{"key":"e_1_2_10_8_1","first-page":"1","article-title":"In vitro assessment of cardiac function using skinned cardiomyocytes","volume":"160","author":"Gon\u00e7alves\u2010Rodrigues P.","year":"2020","journal-title":"Journal of Visualized 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