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Table 1.

Primer Sequence Used for qRT-PCR.

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Table 2.

SBP, BW and vascular morphology changes in Ang II-infused rats.

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Fig 1.

In vivo induction of KLF5 in response to Ang II and altered expression in response to rosiglitazone.

(A) KLF5 and cyclin D1 expression as measured by real-time RT-PCR in the thoracic aorta of Ang II-infused rats (150 ng/kg/min) with or without rosiglitazone. Values are expressed as fold induction compared with control group. (B) Immunohistochemical analysis of KLF5 and cyclin D1 expression in each group. Images are representative of 6 animals studied in each group. Scale bar = 50 μm. Quantification results are presented as gray scale levels and mean ± S.E.M. data of 24 measurements in 6 slides. (C) PPAR-γ mRNA expression was analyzed by real-time RT-PCR. (D) PPAR-γ activation was analyzed by DNA-binding assay. *P<0.05 vs. control; #P<0.05 vs. Ang II alone. Ros: rosiglitazone.

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Fig 2.

Effects of PPAR-γ activation on cell proliferation and cell cycle in Ang II-stimulated vascular smooth muscle cells (VSMCs).

Growth-arrested VSMCs were switched to fresh medium containing 0.5% of serum when pretreated with or without PPAR-γ antagonist GW9662 (3 μM), BADGE (1 μM) for 30 min or PPAR-γ specific siRNA for 48 hrs prior to the addition of rosiglitazone (1, 5 and 10 μM) or PPAR-γ nature ligand 15-d-PGJ2 (1, 5 and 10 μM). Ang II (0.1 μM) was then added for 24 hrs. (A). CCK8 assays (values represent the mean ± S.E.M. (n = 12) were carried out to assess cell proliferation. Ros = rosiglitazone; 15d = 15-d-PGJ; Ang II = Angiotensin. *P<0.05 vs. control; #P<0.05 vs. Ang II; †P<0.05 vs. Ang II + Ros.

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Fig 3.

PPAR-γ agonists inhibit KLF5 and cyclin D1 expression in Ang II-stimulated VSMCs.

Cells were pretreated with increasing concentrations of rosiglitazone (1, 5 and 10 μM) or 15-d-PGJ2 (1, 5 and 10 μM) for 1 hr and then stimulated with Ang II (0.1 μM) for 24 hr. (A) Real-time RT-PCR analysis of KLF5 mRNA expression in VSMCs. Results are expressed as fold increase over control group, and data are mean ± S.E.M. of 3 independent experiments. GAPDH served as an internal control. (B) Immunocytochemical staining of KLF5 staining in VSMCs. Scale bar: 100 mm. (C) Western blot analysis of KLF5 protein expression in VSMCs. Results are representative of 3 independent experiments. β-actin served as an internal control. Data are mean ± S.E.M. of 3 experiments. (D) Real-time RT-PCR analysis of cyclin D1 mRNA expression in VSMCs. Results are expressed as fold increase over control group, and data are mean ± S.E.M. of 3 independent experiments. GAPDH served as an internal control. (*P <0.05 vs. control; #P <0.05 vs. Ang II). Ros = rosiglitazone; 15d = 15-d-PGJ; Ang II = Angiotensin.

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Fig 3 Expand

Fig 4.

Relationship between effect of rosiglitazone on Ang II-induced cell proliferation and KLF5 expression in VSMCs.

VSMCs were pretreated with KLF5 siRNA for 1 hr prior to the addition of rosiglitazone (5 μM) for 1 hr, and subsequently stimulated with Ang II (0.1 μM) for 24 hrs. CCK8 assays (values represent the mean ± S.E.M. n = 12) were carried out to assess cell proliferation. *P<0.05 vs. control; #P<0.05 vs. Ang II; †P<0.05 vs. Ang II + Ros.

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Fig 5.

Suppression of KLF5 expression is mediated by PPAR-γ activation.

Cells were pretreated with or without PPAR-γ antagonist GW9662 (3 mM) or BADGE (1 μM) for 30 min or PPAR-γ specific siRNA for 48 hrs prior before the addition of PPAR-γ activator rosiglitazone (Ros) (5μM), 15-d-PGJ2 (15D) (5μM) or pioglitazone (Pio) (50 μM) for 1 hr, and subsequently stimulated with Ang II (0.1 μM) for 24 hrs. (A) Representative immunoblots for PPAR-γ and β-actin from 3 separate experiments. PPAR-γ protein expression is shown as fold increase over control group. Results are mean ± S.E.M. β-actin was used as an internal control. (B) PPAR-γ activation was analyzed by DNA-binding assay. NSB: non-specific binding, C1: competitor binding, PC: positive control binding. Results are mean ± S.E.M. of 3 independent experiments, expressed as OD 450. (C) Western blot analysis of KLF5 protein expression in VSMCs. Representative western blot (upper panel), and data are mean ± S.E.M. (bottom panel) of 3 independent experiments. Results are expressed as fold increase over control group. β-actin served as an internal control. (D) Real-time RT-PCR analysis of KLF5 mRNA expression in response to different treatment in VSMCs. Results are fold increase over control, and data are mean ± S.E.M. of 3 independent experiments. GAPDH served as an internal control. (*P<0.05 vs. control; # P<0.05 vs. Ang II; †P<0.05 vs. Ang II + Ros).

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Fig 6.

Blockade of AT1 with losartan was not involved in the inhibitory effect of rosiglitzone on Ang II-induced KLF5 expression in VSMCs.

Western blot analysis (upper panel), and data are mean ± S.E.M. (bottom panel) of 3 independent experiments. Results are expressed as fold increase over control group. β-actin served as an internal control (*P<0.05 vs. control; #P<0.05 vs. Ang II).

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Fig 7.

PKC signaling pathway in the effect of PPAR-γ agonist on Ang II-induced KLF5 expression.

(A) and (B). VSMCs were pretreated with rosiglitazone (5 μM) for 1hr, and incubated with Ang II (0.1 μM) for 30 min; phosphorylated PKCε and PKCζ were then detected by western blot. Representative western blot of p-PKCε and p-PKCζ, and data of mean ± S.E.M. of 3 experiments (bottom panel) were shown. (C). VSMCs were pretreated with PKCζ siRNA for 48 hrs prior to the addition of rosiglitazone (5 μM) for 1 h, and subsequently stimulated with Ang II (0.1 μM) for 24 h. A representative western blot of KLF5, and data of mean ± S.E.M. of 3 experiments (bottom panel) were shown. All results are expressed as fold increase over control group. β-actin served as an internal control. (*P<0.05 vs. control; #P<0.05 vs. Ang II).

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Fig 8.

ERK signaling pathway in the effects of PPAR-γ agonist on Ang II-mediated KLF5 expression.

(A) VSMCs were subjected to ERK1/2 inhibitor PD098059 (1 μM) for 30min, followed by treatment of rosiglitazone (5 μM) for further 1 h, and finally stimulated with Ang II (0.1 mM) for 24 h. A representative western blot of KLF5 (upper panel), and data of mean ± S.E.M. of 3 experiments (bottom panel) were shown. (B) VSMCs were pretreated with rosiglitazone (5 μM) for 1h, and incubated with Ang II (0.1 μM) for 30 min, phosphorylated ERK1/2 were then detected by western blot. A representative western blot of ERK1/2 and p-ERK1/2, and data of mean ± S.E.M. of 3 experiments (bottom panel) were shown. Results are expressed as fold increase over control group. β-actin served as an internal control. (*P<0.05 vs. control; #P<0.05 vs. Ang II.)

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Fig 9.

Effect of PPAR-γ agonist on Egr activity.

Egr activation was analyzed by DNA-binding assay. Results are mean ± S.E.M. of 3 independent experiments, expressed as relative light units (RLUs). (*P<0.05 vs. control; #P<0.05 vs. Ang II).

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Fig 10.

Agonist-induced activation of PPAR-γ suppresses Ang II-induced KLF5 expression, likely by interfering with the Ang II/PKCζ/ERK1/2/Egr pathway.

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