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. 2013 Nov 4;4:43. doi: 10.1186/2040-2392-4-43

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Copyright © 2013 Nuytens et al.; licensee BioMed Central Ltd.

This is an open access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Abnormal Protein kinase A(PKA) phosphorylation pattern in Nbea^+/-mice. Visualization of proteins phosphorylated by PKA revealed several changes in phosphorylation levels of proteins in resting platelets (A) and brain lysates (B) of Nbea^+/- mice. Phosphorylation levels were first calculated within a litter, followed by t-test for single means, with the mean of wild-type samples being 100%, to detect significant differences between Nbea^+/+ and Nbea^+/- mice. (A) In resting platelets the three proteins with the highest molecular weight had a significantly higher phosphorylation status. The following three bands had an unaltered phosphorylation level whereas the last two bands had a significantly reduced phosphorylation profile (n = 4 samples/genotype). (B) Two different exposure times are shown for the PKA phosphorylation pattern of brain tissue, which were used for quantification. Image analysis revealed a significant decrease in phosphorylation level of four different proteins in brain tissue of Nbea^+/- mice (n = 5 samples/genotype).