{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,22]],"date-time":"2026-10-22T12:12:55Z","timestamp":1792671175969,"version":"4.5.0"},"reference-count":37,"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>Calcium\/calmodulin-dependent protein kinase II (CaMKII) is a key mediator of intracellular signaling in the heart. However, the tools currently available for assessing dynamic changes in CaMKII localization and activation in living myocytes are limited.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>\n              <jats:underline>Objective:<\/jats:underline>\n            <\/jats:title>\n            <jats:p>We use Camui, a novel FRET-based biosensor in which full-length CaMKII is flanked by CFP and YFP, to measure CaMKII activation state in living rabbit myocytes.<\/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>We show that Camui and mutant variants that lack the sites of CaMKII autophosphorylation (T286A) and oxidative regulation (CM280\/1VV) serve as useful biosensors for CaMKII\u03b4 activation state. Camui (wild-type or mutant) was expressed in isolated adult cardiac myocytes, and localization and CaMKII activation state were determined using confocal microscopy. Camui, like CaMKII\u03b4, is concentrated at the z-lines, with low baseline activation state. Camui activation increased directly with pacing frequency, but the maximal effect was blunted with the T286A, consistent with frequency-dependent phosphorylation of CaMKII at T286 mainly at high-frequency and high-amplitude Ca transients. Camui was also activated by 4 neurohormonal agonists. Angiotensin II and endothelin-1 activated Camui, largely through an oxidation-dependent mechanism, whereas isoproterenol- and phenylephrine-mediated mechanisms had a significant autophosphorylation-dependent component.<\/jats:p>\n          <\/jats:sec>\n          <jats:sec>\n            <jats:title>\n              <jats:underline>Conclusions:<\/jats:underline>\n            <\/jats:title>\n            <jats:p>Camui is a novel, nondestructive tool that allows spatiotemporally resolved measurement of CaMKII activation state in physiologically functioning myocytes. This represents a first step in using Camui to elucidate key mechanistic details of CaMKII signaling in live hearts and myocytes.<\/jats:p>\n          <\/jats:sec>","DOI":"10.1161\/circresaha.111.247148","type":"journal-article","created":{"date-parts":[[2011,8,12]],"date-time":"2011-08-12T03:51:40Z","timestamp":1313121100000},"page":"729-738","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":99,"title":["Fluorescence Resonance Energy Transfer\u2013Based Sensor Camui Provides New Insight Into Mechanisms of Calcium\/Calmodulin-Dependent Protein Kinase II Activation in Intact Cardiomyocytes"],"prefix":"10.1161","volume":"109","author":[{"given":"Jeffrey R.","family":"Erickson","sequence":"first","affiliation":[{"name":"From the Department of Pharmacology, University of California Davis, Davis, CA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ruchi","family":"Patel","sequence":"additional","affiliation":[{"name":"From the Department of Pharmacology, University of California Davis, Davis, CA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Amanda","family":"Ferguson","sequence":"additional","affiliation":[{"name":"From the Department of Pharmacology, University of California Davis, Davis, CA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Julie","family":"Bossuyt","sequence":"additional","affiliation":[{"name":"From the Department of Pharmacology, University of California Davis, Davis, CA."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donald M.","family":"Bers","sequence":"additional","affiliation":[{"name":"From the Department of Pharmacology, University of California Davis, Davis, 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