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- W2582321854 abstract "Previous studies from our lab revealed that ischemia causes dephosphorylation and translocation of connexin43 (Cx43) from gap junctions to intracellular sites with a time course that mirrors electrical uncoupling. We also showed that ischemic preconditioning (PC) prevents dephosphorylation of Cx43, preserves Cx43 in gap junctions and delays uncoupling during ischemia. To test the hypothesis that protein kinase C-ε (PKCε) is activated by PC, phosphorylates Cx43 and prevents its internalization during ischemia, we subjected isolated Langendorff-perfused hearts from wildtype (WT) and PKCε-/- mice to 30 min no-flow ischemia with or without PC. Cx43 phosphorylation at C-terminal residues ser368, ser262, ser255, ser279/282, and tyr265 was analyzed by immunoblotting using antibodies specific for each phosphorylated isoform. Total Cx43 immunoreactive signal in gap junctions was measured by confocal microscopy using a monoclonal antibody. PKC activation was determined by immunoblotting of cytosolic and membrane fractions from ventricular lysates using anti-PKCε and anti-PKCδ antibodies. Cx43 signal decreased by 64% in non-PC PKCε-/- hearts during ischemia. PC failed to preserve Cx43 signal in PKCε-/- hearts (56% reduction). Cx43 phosphorylation at probed residues was comparable in WT and PKCε-/- control hearts. While ischemia promoted robust Cx43 phosphorylation at the PKC site ser368 in both PC and non-PC WT hearts (717% and 354% of control, respectively), the response was even greater in PKCε-/- hearts (448% and 212% of WT, respectively). In WT hearts, ischemia caused marked translocation of PKCε from cytosol to membrane fractions, but only limited PKCδ translocation. In PKCε-/-, no PKCε was detected by Western but ischemia induced marked translocation of PKCδ from cytosol to membrane fractions. These results indicate that PC preserves Cx43 signal in gap junctions via PKCε activation. However, Cx43 phosphorylation at the PKC site ser368 is insufficient to prevent intracellular translocation of Cx43, and must be catalyzed by at least one other isoform, probably PKCδ." @default.
- W2582321854 created "2017-02-03" @default.
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- W2582321854 date "2006-05-01" @default.
- W2582321854 modified "2023-09-23" @default.
- W2582321854 title "P3-11" @default.
- W2582321854 doi "https://doi.org/10.1016/j.hrthm.2006.02.543" @default.
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