Fig. 2

FGFR-agonist promotes FGFR signaling of NPCs. (A) ELISA-based quantification of FGFR1 phosphorylation in NPCs. FGFR1 (Tyr653/654) phosphorylation levels were measured in serum-starved NPCs after 10-minute exposure to either bFGF (20 ng/mL) or FGFR-agonist (40 nM). Data are represented as mean ± SD (n = 3); **p < 0.01(unpaired two-tailed Student’s t-test). (B) ERK1/2 phosphorylation profile via Western Blot. Serum-starved NPCs were treated with either bFGF (20 ng/mL) or FGFR-agonist (40 nM) for 10 min. Phosphorylation of ERK1/2 (Thr202/Tyr204) was then examined by Western blot, with GAPDH serving as an internal control. (C) Quantification of relative ERK1/2 phosphorylation to total ERK. The phosphorylation levels of ERK1/2 were quantified and normalized to the control group without any treatment. Data are expressed as means ± SD (n = 3); **p < 0.01(unpaired two-tailed Student’s t-test). (D) Time-dependent Activation of ERK1/2. Serum-starved NPCs were exposed to either bFGF (20 ng/mL) or FGFR-agonist (40 nM) over varying time intervals (5, 10, 15, 30, 60 min). The phosphorylation of ERK1/2 (Thr202/Tyr204) was assessed via Western blot. (E) Quantification of the time-dependent data from panel D, illustrating the kinetics of ERK1/2 phosphorylation in NPCs when stimulated by either bFGF or FGFR-agonist. Data are presented as mean ± SD (n = 3); no significance (n.s.) was found, as determined by one-way ANOVA