Table 2.
Phosphorylation of Cx43 in LV and SSM samples of Cx43MAPKmut, Cx43PKCmut, and Cx43CK1mut mice
| Strain | Sample | P-S262 (a.u.) | P-S325/328/330 (a.u.) |
P-S365 (a.u.) | P-S368 (a.u.) | P-S373 (a.u.) |
|---|---|---|---|---|---|---|
|
WT Cx43MAPKmut |
LV | n.d |
1.64 ± 0.60, n = 8 1.18 ± 0.23, n = 8 p = ns |
0.48 ± 0.15 n = 8 0.35 ± 0.09, n = 8 p = ns |
1.17 ± 0.26, n = 8 0.70 ± 0.0, n = 7, p = ns |
0.57 ± 0.17, n = 8 0.35 ± 0.07, n = 7, p = ns |
|
WT Cx43PKCmut |
LV |
0.74 ± 0.07, n = 6 0.90 ± 0.22, n = 6 p = ns |
1.26 ± 0.18, n = 8 0.12 ± 0.03, n = 8 p < 0.05 |
0.76 ± 0.34, n = 8 0.02 ± 0.002, n = 8 p < 0.05 |
n.d |
0.60 ± 0.13, n = 6 0.07 ± 0.02, n = 6 p < 0.05 |
|
WT Cx43CK1mut |
LV |
0.27 ± 0.05, n = 6 0.48 ± 0.18, n = 6 p = ns |
n.d |
0.88 ± 0.13, n = 6 0.24 ± 0.04, n = 6 p < 0.05 |
0.92 ± 0.05, n = 6 0.40 ± 0.06, n = 6 p < 0.05 |
0.87 ± 0.20, n = 6 0.31 ± 0.04, n = 6 p < 0.05 |
|
WT Cx43MAPKmut |
SSM | n.d |
0.53 ± 0.06, n = 7 0.45 ± 0.06, n = 10 p = ns |
0.19 ± 0.04, n = 7 0.19 ± 0.04, n = 9 p = ns |
0.66 ± 0.11, n = 8 0.63 ± 0.06, n = 11 p = ns |
0.18 ± 0.02, n = 8 0.07 ± 0.02, n = 9 p < 0.05 |
|
WT Cx43PKCmut |
SSM |
0.11 ± 0.0, n = 8 0.04 ± 0.005, n = 8 p < 0.05 |
0.50 ± 0.03, n = 6 0.03 ± 0.005, n = 6 p < 0.05 |
0.35 ± 0.04, n = 8 0.08 ± 0.01, n = 8 p < 0.05 |
n.d |
0.11 ± 0.02, n = 8 0.02 ± 0.004, n = 5 p < 0.05 |
|
WT Cx43CK1mut |
SSM |
0.08 ± 0.01, n = 6 0.22 ± 0.08 n = 6 p = ns |
n.d |
0.46 ± 0.11, n = 6 0.31 ± 0.04, n = 6 p = ns |
0.56 ± 0.11, n = 6 0.33 ± 0.05, n = 5 p = ns |
0.13 ± 0.02, n = 6 0.10 ± 0.03, n = 6 p = ns |
Western blot analysis was performed for Cx43 phosphorylated at S262, S325/328/330, S365, S368, and S373 on left-ventricular (LV) and subsarcolemmal mitochondria (SSM) protein samples isolated from wild-type mice (WT) or Cx43MAPKmut, Cx43PKCmut, and Cx43CK1mut mice. Signal intensities are shown in arbitrary units (a.u.). Phosphorylated Cx43 was normalized to GAPDH in LV samples and to MnSOD in SSM samples, n.d.: not determined, ns: not significant