Figure 4
(A) EGFR expression (EGFR) in mVSMCs derived from WT and TRPM7 kinase-deficient mice (TRPM7+/Δkinase, M7+/Δ). Protein expression normalized to β-actin. (B) c-Src phosphorylation (p-c-Src), normalized by total c-Src expression (t-Src) in mVSMCs derived from WT and TRPM7+/Δkinase mice. (C) ERK1/2 phosphorylation in primary cultured mVSMCs derived from WT and TRPM7+/Δkinase (M7+/Δ) mice, at basal levels (veh) and after 5-min treatment with EGF (50 ng/ml). ERK1/2 activity was assessed by phosphorylation level (p-ERK1/2) and normalized by total ERK1/2 expression (t-ERK1/2). Results are mean ± SEM of three to six experiments. (D,E) Representative images and quantification of aortic wall thickness in WT and TRPM7+/Δkinase mice; 20×: Scale bar =150 µm. 40×: Scale bar =75 µm. Results represent the mean ± SEM of three to seven independent experiments. *P<0.05 compared with WT mice.
Reduced expression of EGFR is associated with vascular remodeling in TRPM7-deficient mice

(A) EGFR expression (EGFR) in mVSMCs derived from WT and TRPM7 kinase-deficient mice (TRPM7+/Δkinase, M7+/Δ). Protein expression normalized to β-actin. (B) c-Src phosphorylation (p-c-Src), normalized by total c-Src expression (t-Src) in mVSMCs derived from WT and TRPM7+/Δkinase mice. (C) ERK1/2 phosphorylation in primary cultured mVSMCs derived from WT and TRPM7+/Δkinase (M7+/Δ) mice, at basal levels (veh) and after 5-min treatment with EGF (50 ng/ml). ERK1/2 activity was assessed by phosphorylation level (p-ERK1/2) and normalized by total ERK1/2 expression (t-ERK1/2). Results are mean ± SEM of three to six experiments. (D,E) Representative images and quantification of aortic wall thickness in WT and TRPM7+/Δkinase mice; 20×: Scale bar =150 µm. 40×: Scale bar =75 µm. Results represent the mean ± SEM of three to seven independent experiments. *P<0.05 compared with WT mice.

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