{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,11,6]],"date-time":"2026-11-06T21:30:19Z","timestamp":1794000619288,"version":"4.8.0"},"reference-count":35,"publisher":"Ovid Technologies (Wolters Kluwer Health)","issue":"7","content-domain":{"domain":["www.ahajournals.org"],"crossmark-restriction":true},"short-container-title":["Stroke"],"published-print":{"date-parts":[[2003,7]]},"abstract":"<jats:p>\n                    <jats:bold>\n                      <jats:italic>Background and Purpose\u2014<\/jats:italic>\n                    <\/jats:bold>\n                    Mitochondrial ATP-sensitive potassium (mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    ) channels are present in the brain, and several reports have shown that mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel openers protect the brain against ischemic injury. However, the precise mechanisms of this protection are not well established. We hypothesized that mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel openers prevent apoptosis by preserving mitochondrial membrane potential.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>\n                      <jats:italic>Methods\u2014<\/jats:italic>\n                    <\/jats:bold>\n                    We investigated the effect of mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel openers on apoptosis induced by oxidative stress using cultured cerebellar granule neurons.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>\n                      <jats:italic>Results\u2014<\/jats:italic>\n                    <\/jats:bold>\n                    The mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel opener diazoxide (100 \u03bcmol\/L) significantly suppressed the number of cells with terminal deoxynucleotidyl transferase\u2013mediated dUTP nick end-labeling (TUNEL)\u2013positive nuclei and the increase in caspase-3 activity induced by 20 \u03bcmol\/L H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    . Diazoxide and another opener, pinacidil, prevented the loss of mitochondrial inner membrane potential (\u0394\u03a8\n                    <jats:sub>m<\/jats:sub>\n                    ) induced by H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    . These effects were abolished by 5-hydroxydecanoate (500 \u03bcmol\/L), a mitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel blocker. Cyclosporin A and bongkrekic acid, inhibitors of the mitochondrial permeability transition pore, also prevented \u0394\u03a8\n                    <jats:sub>m<\/jats:sub>\n                    loss, confirming the involvement of the mitochondrial permeability transition in the apoptotic cascade in neurons. Furthermore, diazoxide prevented the increase in extracellular glutamate concentration induced by H\n                    <jats:sub>2<\/jats:sub>\n                    O\n                    <jats:sub>2<\/jats:sub>\n                    , but this effect was not attributable to activation of surface K\n                    <jats:sub>ATP<\/jats:sub>\n                    channels.\n                  <\/jats:p>\n                  <jats:p>\n                    <jats:bold>\n                      <jats:italic>Conclusions\u2014<\/jats:italic>\n                    <\/jats:bold>\n                    MitoK\n                    <jats:sub>ATP<\/jats:sub>\n                    channel openers inhibited apoptosis by preserving mitochondrial inner membrane potential. These beneficial effects may suggest a possible new target for neuroprotection.\n                  <\/jats:p>","DOI":"10.1161\/01.str.0000077017.60947.ae","type":"journal-article","created":{"date-parts":[[2003,6,10]],"date-time":"2003-06-10T03:32:04Z","timestamp":1055215924000},"page":"1796-1802","update-policy":"https:\/\/doi.org\/10.1161\/crossmarkpolicy","source":"Crossref","is-referenced-by-count":112,"title":["Mitochondrial ATP-Sensitive Potassium Channel Activation Protects Cerebellar Granule Neurons From Apoptosis Induced by Oxidative Stress"],"prefix":"10.1161","volume":"34","author":[{"given":"Yasushi","family":"Teshima","sequence":"first","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Masaharu","family":"Akao","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ronald A.","family":"Li","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tae H.","family":"Chong","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"William A.","family":"Baumgartner","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michael V.","family":"Johnston","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eduardo","family":"Marba\u0301n","sequence":"additional","affiliation":[{"name":"From the Institute of Molecular Cardiobiology (Y.T., M.A., R.A.L., E.M.), Kennedy Krieger Institute (T.H.C., M.V.J.), and Department of Surgery (W.A.B.), The Johns Hopkins University, Baltimore, Md."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"276","reference":[{"key":"e_1_3_2_1_2","doi-asserted-by":"publisher","DOI":"10.1161\/res.81.6.1072"},{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1161\/circ.97.24.2463"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1161\/res.88.12.1267"},{"key":"e_1_3_2_4_2","first-page":"1045","volume":"146","year":"1995","unstructured":"Li Y, Sharov VG, Jiang N, Zaloga C, Sabbah HN, Chopp M. 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