PP1α reverses CaMKIIα Thr286 phosphorylation and mediates the dephosphorylation of NR2B Ser1303 upon OGD.

<p>(<b>a</b>) Representative Western blots and corresponding quantitative analysis of CaMKIIα Thr286 phosphorylation. CaMKIIα phosphorylation significantly increases 1 min after OGD (control 1 min post-OGD, n = 8) with no significant change at 16 min (control 16 min post-OGD, n = 6) in control slices. PP1α slices do not display any change in CaMKIIα phosphorylation either 1 min (PP1α 1 min post-OGD, n = 6) or 16 min post-OGD (PP1α 16 min post-OGD, n = 7) compared to control. Phospho-protein levels were normalized to non-phosphorylated protein levels and β-actin was used as a loading control. Quantitative data for each condition were normalized to levels of non-OGD condition (control non-OGD, n = 14) from the same blot and exposure. *p<0.05. (<b>b</b>) Representative Western blots and corresponding quantitative analysis of NR2B Ser1303 phosphorylation. Increased level of phospho-NR2B in control slices 1 min after OGD (control 1 min post-OGD, n = 9), but not 16 min after OGD (control 16 min post-OGD, n = 8). PP1α expression or KN-93 treatment blocks this increase (PP1α 1 min post-OGD, n = 6; KN-93 1 min post-OGD, n = 6), but has no effect 16 min post-OGD (PP1α 16 min post-OGD, n = 8; KN-93 16 min post-OGD, n = 5). Phospho-protein levels were normalized to non-phosphorylated protein levels, and β-actin was used as a loading control. Quantitative data for each condition were normalized to levels of non-OGD condition (control non-OGD, n = 14) from the same blot and exposure. *p<0.05.