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. 2022 Apr 1;298(5):101887. doi: 10.1016/j.jbc.2022.101887

Figure 4.

Figure 4

PALMD enhances glycolysis in hVICs. hVICs were transfected with 20 nM siScrambled or siPALMD and treated with control medium (Ctr) or calcifying medium (Cal.) for 48 h. A, RT-qPCR showing expression of the key glycolytic genes in hVICs with PALMD depletion after 48 h, n = 5. B, representative Western blotting images for HK1, PFKFB3, and β-actin protein expression in hVICs with PALMD depletion at day 3 and day 7, n = 4 or 5. C, RT-qPCR showing expression of the key glycolytic genes in hVICs infected with Ad-null (MOI = 100) or Ad-PALMD (MOI = 100) for 48 h, n = 6. D, representative Western blotting images for HK1, PFKFB3, and β-actin protein expression in hVICs with PALMD overexpression at day 3 and day 7, n = 3. E, normalized fluorescence of the glucose analog 2-NBDG (fl/μg protein) determined after 48 h in hVICs with silencing of PALMD, n = 7. F and G, the glycolysis rate assay using the Seahorse in hVICs with PALMD overexpression after 48 h, n = 9. Data are presented as mean ± SEM, and statistical significance was analyzed by a two-tailed unpaired Student’s t test or one-way ANOVA followed by Tukey's multiple comparisons test. hVIC, human valve interstitial cell.