{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,21]],"date-time":"2026-09-21T11:53:35Z","timestamp":1789991615995,"version":"4.0.1"},"reference-count":38,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"10","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["ATVB"],"published-print":{"date-parts":[[2018,10]]},"abstract":"<jats:sec>\n                    <jats:title>Objective\u2014<\/jats:title>\n                    <jats:p>\n                      This study examined whether caveolae position Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2 (T-type Ca2+ channel encoded by the \u03b1-3.2 subunit) sufficiently close to RyR (ryanodine receptors) for extracellular Ca\n                      <jats:sup>2+<\/jats:sup>\n                      influx to trigger Ca\n                      <jats:sup>2+<\/jats:sup>\n                      sparks and large-conductance Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -activated K\n                      <jats:sup>+<\/jats:sup>\n                      channel feedback.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Approach and Results\u2014<\/jats:title>\n                    <jats:p>\n                      Using smooth muscle cells from mouse mesenteric arteries, the proximity ligation assay confirmed that Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2 reside within 40 nm of caveolin 1, a key caveolae protein. Methyl-\u03b2-cyclodextrin, a cholesterol depleting agent that disrupts caveolae, suppressed Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2 activity along with large-conductance Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -activated K\n                      <jats:sup>+<\/jats:sup>\n                      \u2013mediated spontaneous transient outward currents in cells from C57BL\/6 but not Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice. Genetic deletion of caveolin 1, a perturbation that prevents caveolae formation, also impaired spontaneous transient outward current production but did so without impairing Ca\n                      <jats:sup>2+<\/jats:sup>\n                      channel activity, including Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2. These observations indicate a mistargeting of Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2 in caveolin 1\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      mice, a view supported by a loss of Ni\n                      <jats:sup>2+<\/jats:sup>\n                      -sensitive Ca\n                      <jats:sup>2+<\/jats:sup>\n                      spark generation and colocalization signal (Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2-RyR) from the proximity ligation assay. Vasomotor and membrane potential measurements confirmed that cellular disruption of the Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2-RyR axis functionally impaired the ability of large-conductance Ca\n                      <jats:sup>2+<\/jats:sup>\n                      -activated K\n                      <jats:sup>+<\/jats:sup>\n                      to set tone in pressurized caveolin 1\n                      <jats:sup>\u2212\/\u2212<\/jats:sup>\n                      arteries.\n                    <\/jats:p>\n                  <\/jats:sec>\n                  <jats:sec>\n                    <jats:title>Conclusions\u2014<\/jats:title>\n                    <jats:p>\n                      Caveolae play a critical role in protein targeting and preserving the close structural relationship between Ca\n                      <jats:sub>V<\/jats:sub>\n                      3.2 and RyR needed to drive negative feedback control in resistance arteries.\n                    <\/jats:p>\n                  <\/jats:sec>","DOI":"10.1161\/atvbaha.118.311394","type":"journal-article","created":{"date-parts":[[2018,9,27]],"date-time":"2018-09-27T09:52:45Z","timestamp":1538041965000},"page":"2371-2381","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":27,"title":["Caveolae Link Ca\n                    <sub>V<\/sub>\n                    3.2 Channels to BK\n                    <sub>Ca<\/sub>\n                    -Mediated Feedback in Vascular Smooth Muscle"],"prefix":"10.1161","volume":"38","author":[{"given":"Ahmed M.","family":"Hashad","sequence":"first","affiliation":[{"name":"From the Department of Physiology and Pharmacology, Hotchkiss Brain and Libin Cardiovascular Institutes, University of Calgary, Alberta, Canada (A.M.H., O.F.H., D.G.W.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Osama F.","family":"Harraz","sequence":"additional","affiliation":[{"name":"From the Department of Physiology and Pharmacology, Hotchkiss Brain and Libin Cardiovascular Institutes, University of Calgary, Alberta, Canada (A.M.H., O.F.H., D.G.W.)"},{"name":"Department of Pharmacology, University of Vermont, Burlington (O.F.H.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Suzanne E.","family":"Brett","sequence":"additional","affiliation":[{"name":"Department of Physiology and Pharmacology, University of Western Ontario, London, Canada (S.E.B., D.G.W.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Monica","family":"Romero","sequence":"additional","affiliation":[{"name":"Advanced Imaging and Microscopy Core, Loma Linda University School of Medicine, CA (M.R., S.M.W.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mario","family":"Kassmann","sequence":"additional","affiliation":[{"name":"Experimental and Clinical Research Centre, Charit\u00e9 University Medicine, Berlin, Germany (M.K., M.G.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jose L.","family":"Puglisi","sequence":"additional","affiliation":[{"name":"College of Medicine, California North State University, Sacramento (J.L.P.)."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sean M.","family":"Wilson","sequence":"additional","affiliation":[{"name":"Advanced Imaging and Microscopy Core, Loma Linda University School of Medicine, CA (M.R., S.M.W.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Maik","family":"Gollasch","sequence":"additional","affiliation":[{"name":"Experimental and Clinical Research Centre, Charit\u00e9 University Medicine, Berlin, Germany (M.K., M.G.)"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Donald G.","family":"Welsh","sequence":"additional","affiliation":[{"name":"From the Department of Physiology and Pharmacology, Hotchkiss Brain and Libin Cardiovascular Institutes, University of Calgary, Alberta, Canada (A.M.H., 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