Ouabain‐induced changes in MAP kinase phosphorylation in primary culture of rat cerebellar cells

In this study we investigated the effect of ouabain on the level of phosphorylation of three MAPK (ERK1/2, JNK and p38) and on cell survival in the primary culture of rat cerebellar cells. Using Western blotting we described the time course and concentration dependence of phosphorylation for ERK1/2, JNK and p38 in response to ouabain. We discovered that ouabain at a concentration of 1 μM does not cause cell death in cultured neurons while it changes the phosphorylation level of the three MAPK: ERK1/2 is phosphorylated transiently, p38 shows sustained phosphorylation, and JNK is dephosphorylated after a long‐term incubation. We showed that ERK1/2 phosphorylation increase does not depend on ouabain‐induced calcium increase and p38 activation. Changes in p38 phosphorylation, which is independent from ERK1/2 activation, are calcium dependent. Changes in JNK phosphorylation are calcium dependent and also depend on ERK1/2 and p38 activation. Ten‐micromolar ouabain leads to cell death, and we conclude that different effects of 1‐μM and 10‐μM ouabain depend on different ERK1/2 and p38 phosphorylation profiles. Copyright © 2016 John Wiley & Sons, Ltd.
Source: Cell Biochemistry and Function - Category: Biochemistry Authors: Tags: Research Article Source Type: research