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. 2014 Aug 5;9(8):e104338. doi: 10.1371/journal.pone.0104338

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© 2014 Chakraborty et al

This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.

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(A) Immunoblots of PKD, pPKD-S744/748 and pPKD-S916 of heart homogenates from 10-day old Ryr2^+/+/AC3-C (WC) and/AC3-I (WI) and Ryr2^ADA/ADA/AC3-C (HC) and/AC3-I (HI) mice. Glyceraldehyde-3 phosphate dehydrogenase was the loading control. (B) Intensity of protein PKD bands in RyR2^+/+ and RyR2^ADA/ADA hearts normalized for RyR2^+/+/AC3-C protein band intensities. (C and D) pPKD/PKD on S744/748 and S916, respectively. Data were obtained analyzing proteins from 4–5 hearts of each genotype and are the mean ± SEM of 13 (B), 13(C) and 12 (D) determinations using two way ANOVA. None of the differences were significant.