Figure 1.

FGFR inhibition upregulates FAO while suppressing glycolysis in HDLECs.A–E, HDLECs were treated with vehicle or the FGFR inhibitor ASP5878 for 2 days and then analyzed for glycolytic flux with 5-³H-glucose, glucose oxidation flux with 6-¹⁴C-glucose, glutamine oxidation flux with ¹⁴C(U)-glutamine, and FAO flux with 9,10-³H-palmitic acid and 1-¹⁴C-oleic acid (representative of two independent experiments). n = 6 biological replicates for (A), n = 4 biological replicates for (B), n = 4 biological replicates for (C), n = 6 biological replicates for (D), and n = 3 to 4 biological replicates for (E). F and G, Western blot analysis (F) and densitometric quantification (n = 3 independent experiments) (G) of FGFR1 proteins in HDLECs transfected with nontargeting (control) or FGFR1 siRNA. α-Tubulin served as a loading control. H–J, HDLECs transfected with nontargeting (control) or FGFR1 siRNA were analyzed for glycolytic flux with 5-³H-glucose and for FAO flux with 9,10-³H-palmitic acid and 1-¹⁴C-oleic acid (representative of two independent experiments). n = 6 biological replicates for (H), n = 6 biological replicates for (I), and n = 4 biological replicates for (J). Data represent mean ± SD; p values were calculated by unpaired t test. FAO, fatty acid β-oxidation; FGFR, fibroblast growth factor receptor; HDLEC, human dermal lymphatic endothelial cell.