Signal transduction in <i>Lrrc10^−/−</i> hearts.

<p>(A) Western blotting analysis for activation of Akt, p38, ERK, and STAT signaling pathways and PKC expression reveals no changes in phosphorylation of p38, ERK, or STAT or protein abundance of PKCα or PKCε. (B) Western blotting indicates hyperphosphorylation of Akt at Ser 473 in <i>Lrrc10</i><b><i>⁻</i></b>^{<i>/</i><b><i>−</i></b>} hearts. (C) Quantitation of Western blotting confirms increased phosphorylation of Akt in <i>Lrrc10</i><b><i>⁻</i></b>^{<i>/</i><b><i>−</i></b>} hearts (n = 7). Phosphorylated Akt was normalized to total Akt expression and GAPDH was used as a loading control. (D) Representative Western blotting of particulate and nonparticulate fractions of adult heart extracts in control (WT) and <i>Lrrc10</i><b><i>⁻</i></b>^{<i>/</i><b><i>−</i></b>} mice. (E) Quantification of PKCε expression in the particulate fraction relative to the nonparticulate fraction. Myosin heavy chain (MyHC) and α-actinin were used as a particulate/myofilament loading control.