The role of the Grb2–p38 MAPK signaling pathway in cardiac hypertrophy and fibrosis
J. Clin. Invest. Shaosong Zhang, et al. 111:833
doi:10.1172/JCI16290 [Go to this article.]

Figure 1
Biochemical characterization of Grb2 and MAPK in murine cardiac tissue 7 days after TAC or sham operation. (a) Load-induced formation of a Grb2-FAK complex. Anti-FAK immunoprecipitates (IP) derived from ventricular lysates were separated by SDS-PAGE and analyzed by immunoblotting with an anti-Grb2 antibody (lower panel). Anti-FAK immunoprecipitates were also analyzed in parallel by immunoblotting with an anti-FAK antibody (upper panel). (b) Reduced Grb2 protein content in Grb2+/– cardiac tissue. Upper panel, ventricular lysates were analyzed by immunoblotting with an anti-Grb2 antibody. Lower panel, quantification of Grb2 protein levels by densitometric analysis of immunoreactive bands. (c) Analysis of p38 MAPK activation in Grb2+/– cardiac tissue. Ventricular lysates were analyzed by immunoblotting with an anti-phospho–p38 MAPK antibody (upper panel). Lysates were also analyzed in parallel by immunoblotting with an anti–p38 MAPK (lower panel) antibody to control for protein content. (d) Analysis of JNK activation in Grb2+/– cardiac tissue. Lysates were analyzed by immunoblotting with an anti–phospho-JNK antibody (upper panel). Lysates were also analyzed in parallel by immunoblotting with an anti-JNK (lower panel) antibody to control for protein content. (e) Analysis of ERK activity in Grb2+/– cardiac tissue. Anti-ERK immunoprecipitates derived from ventricular lysates were analyzed by in vitro kinase assay by use of Elk-1 protein as a substrate. Anti-phospho–Elk-1 antibody immunoblotting was performed to assess ERK activity (upper panel). Lysates were also analyzed in parallel by immunoblotting with an anti-ERK (lower panel) antibody to control for protein content. Sham, sham operation.