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Increased electrophoretic mobility of Cx43 in the ischemic heart involves dephosphorylation at serine residues 325, 328 and/or 330. Increased electrophoretic.

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Presentation on theme: "Increased electrophoretic mobility of Cx43 in the ischemic heart involves dephosphorylation at serine residues 325, 328 and/or 330. Increased electrophoretic."— Presentation transcript:

1 Increased electrophoretic mobility of Cx43 in the ischemic heart involves dephosphorylation at serine residues 325, 328 and/or 330. Increased electrophoretic mobility of Cx43 in the ischemic heart involves dephosphorylation at serine residues 325, 328 and/or 330. Western blot of total protein isolated from three control (lanes 1,3,5, respectively) or three globally ischemic hearts (30' at 37°C; lanes 2,4,6, respectively) simultaneously probed for total Cx43 (Cx43NT-1) and Cx43 phosphorylated at S325, S328 and/or S330 followed by GAPDH and vinculin antibodies. Notice the increased mobility of Cx43 and decreased pS325/328/330-Cx43 content in the ischemic samples. Molecular mass standards are 28, 49, 62 and 98 kDa (bottom to top); P, position of the Cx43 P isoform; P0, position of the Cx43 P0 isoform. Paul D. Lampe et al. J Cell Sci 2006;119: © The Company of Biologists Limited 2006

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