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Compound 22 promotes HepG2 cell <t>LDLR</t> expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals <t>of</t> <t>β</t> -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.
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Compound 22 promotes HepG2 cell <t>LDLR</t> expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals <t>of</t> <t>β</t> -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.
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Compound 22 promotes HepG2 cell <t>LDLR</t> expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals <t>of</t> <t>β</t> -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.
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Compound 22 promotes HepG2 cell <t>LDLR</t> expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals <t>of</t> <t>β</t> -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.
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Compound 22 promotes HepG2 cell <t>LDLR</t> expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals <t>of</t> <t>β</t> -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.
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Compound 22 promotes HepG2 cell LDLR expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals of β -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.

Journal: Acta Pharmaceutica Sinica. B

Article Title: Design, synthesis, and biological evaluation of novel tetrahydroprotoberberine derivatives (THPBs) as proprotein convertase subtilisin/kexin type 9 (PCSK9) modulators for the treatment of hyperlipidemia

doi: 10.1016/j.apsb.2019.06.006

Figure Lengend Snippet: Compound 22 promotes HepG2 cell LDLR expression in a dose-dependent manner. Total protein of HepG2 cells treated with increasing concentrations of compound 22 (0.1, 0.5, 1, 2.5, and 5 μmol/L) for 24 h was isolated by RIPA buffer. Western blot was utilized to measure LDLR expression in HepG2 cells. The protein abundance of LDLR was quantified using imageJ software with normalization by signals of β -actin. Results are shown as mean ± SEM of three independent experiments. ∗ P < 0.05; ∗∗ P < 0.01; as compared to the DMSO group.

Article Snippet: Non-specific binding sites were blocked in 5% Blotting Grade Blocker Non-Fat Dry Milk (Bio-Rad, cat. 170-6404, Hercules, USA) for 2 h. The membranes were incubated with antibodies specific for PCSK9 (Abcam, cat. ab181142, Cambridge, UK; 1:2000), LDLR (Proteintech, cat. 10785-1-AP, Wuhan, China; 1:2500) and β -actin (CST, cat. #3700, Danvers, MA, USA; 1:1000), respectively, at 4 °C overnight.

Techniques: Expressing, Isolation, Western Blot, Software