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. 2010 Apr;159(8):1693-1703.
doi: 10.1111/j.1476-5381.2010.00664.x.

"V体育ios版" Naringin improves bone properties in ovariectomized mice and exerts oestrogen-like activities in rat osteoblast-like (UMR-106) cells

Wai-Yin Pang  1 , Xin-Lun Wang, Sau-Keng Mok, Wan-Ping Lai, Hung-Kay Chow, Ping-Chung Leung, Xin-Sheng Yao, Man-Sau Wong
Affiliations

Naringin improves bone properties in ovariectomized mice and exerts oestrogen-like activities in rat osteoblast-like (UMR-106) cells

Wai-Yin Pang (V体育官网入口) et al. Br J Pharmacol. 2010 Apr.

Abstract

Background and purpose: Naringin, a flavanone glycoside in citrus fruits, has been recently reported to stimulate bone formation in vitro and in vivo. The present study was designed to determine if naringin could exert oestrogen-like protective actions in bone VSports手机版. .

Experimental approach: Young C57/BL6J mice were ovariectomized (OVX) and treated orally with naringin (0. 2 or 0. 4 mg*g(-1)*day(-1)), 17beta-oestradiol (2 microg*g(-1)*day(-1)) or its vehicle for 6 weeks. Bone mineral densities (BMD) and polar stresss-train index (SSI) were measured by peripheral quantitative computed tomography. Rat osteoblast-like UMR-106 cells were co-incubated with the oestrogen receptor (ER) antagonist ICI 182780 to determine if the effects of naringin on osteoblastic functions were ER dependent. Functional transactivation of ERalpha and ERbeta as well as ERalpha phosphorylation by naringin were also studied V体育安卓版. .

Key results: Naringin at 0. 4 mg*g(-1)*day(-1) increased BMD at trabecular-rich bone in OVX mice. Naringin (at both doses) significantly increased SSI at distal femur and lumbar spine and increased biomechanical strength (ultimate load and energy for breaking) at tibia diaphysis in OVX mice V体育ios版. The stimulatory effects of naringin on osteoblastic functions could be abolished by co-incubation with ICI 182780 in UMR-106 cells. Naringin failed to stimulate ERalpha- or ERbeta-mediated oestrogen response element-dependent luciferase activity but could significantly induce ERalpha phosphorylation at serine 118, in UMR-106 cells. .

Conclusions and implications: Naringin was effective in protecting against OVX-induced bone loss in mice and its actions might be mediated through ligand-independent activation of ER in osteoblastic cells VSports最新版本. .

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VSports最新版本 - Figures

Figure 1
Figure 1
Effects of naringin on cell proliferation and alkaline phosphatase (ALP) activity in UMR-106 cells. (A) UMR-106 cells were treated with vehicle (C), 17β-oestradiol (E2; 10−8 M) or 10−10–10−5 M of naringin for 24 or 48 h. Cell proliferation rate was assessed by the 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulphophenyl)-2H-tetrazolium assay. Results were obtained from three independent experiments and were expressed as mean ± SEM. *P < 0.05; **P < 0.01 versus control (C). ^P < 0.05; ^^^P < 0.001 versus control. (B) UMR-106 cells were treated with vehicle (C), E2; (10−8 M) or 10−10–10−5 M of naringin for 24 h. The lysates were used for analysis of ALP activity. Results were obtained from three independent experiments in triplicate and were expressed as mean ± SEM. **P < 0.01; ***P < 0.001 versus control (C).
Figure 2
Figure 2
Effects of ICI 182780 on the stimulatory effects of naringin on cell proliferation and differentiation in UMR-106 cells. UMR-106 cells were treated with vehicle (C), 17β-oestradiol (E2; 10−8 M) or naringin (10 nM or 100 nM) of naringin in the presence or absence of ICI 182780. (A) Cell proliferation rate was assessed by the 3-(4,5-dimethylthiazol-2-yl)-5-(3-carboxymethoxyphenyl)-2-(4-sulphophenyl)-2H-tetrazolium (MTS) assay. Results were obtained from three independent experiments and were expressed as mean ± SEM. **P < 0.01 versus control (C). (B) Cell lysates were used for alkaline phosphatase (ALP) activity measurement. Results were obtained from three independent experiments in triplicate and were expressed as mean ± SEM. *P < 0.05; **P < 0.01; ***P < 0.001 versus control; #P < 0.05, ##P < 0.01; ###P < 0.001 versus ICI-treated cells.
Figure 3
Figure 3
Effects of naringin on osteoprotegerin (OPG) and nuclear factor-κB ligand (RANKL) mRNA expressions in UMR-106 cells. UMR-106 cells were treated with vehicle (C), 17β-oestradiol (E2; 10−8 M) or naringin (10 nM) of naringin in the presence or absence of ICI 182780 for 48 h. Total RNA was isolated and real-time-RT-PCR was performed to determine the mRNA expressions of (A) OPG, (B) RANKL and (C) OPG/RANKL, which were normalized to that of glyceraldehyde-3-phosphate dehydrogenase (GAPDH). Results were obtained from two independent experiments in triplicate and expressed as mean ± SEM. ^P < 0.05 versus control (C); *P < 0.05; **P < 0.01 versus ICI-treated cells.
Figure 4
Figure 4
Effects of naringin on ERα- or ERβ-mediated oestrogen response element (ERE)-dependent luciferase activity in UMR-106 cells. Cells were co-transfected with 0.4 µg ERα or ERβ plasmid, 0.4 µg ERE-containing luciferase reporter plasmid and 0.1 µg pRL-TK luciferase internal reporter plasmid using the Lipofectamine 2000 reagent according to the manufacturer's instructions. Transfected cells were treated with vehicle (C), 17β-oestradiol (E2; 10−8 M) or naringin [Nar(10 nM) and Nar (100 nM)] for 24 h. Activities of luciferase encoded by experimental and internal control plasmid were measured sequentially with the DLR assay reagents. The ERE firefly luciferase activities were normalized for pRL-TK Renilla luciferase values. 100% represents the ERE luciferase activity of the control. Results were obtained from three independent experiments and expressed as mean ± SEM. *P < 0.05; **P < 0.01; ***P < 0.001 versus control (C).
Figure 5
Figure 5
Effects of naringin on phosphorylation of ERα at serine 118, in UMR-106 cells. Cells were treated with vehicle (C), 17β-oestradiol (E2; 10−8 M) or naringin [Nar(10 nM) and Nar (100 nM)] for 24 h. Proteins extracted from cell lysates were transblotted onto a membrane and probed with anti-phospho-ERα (at Serine 118) (pERα) and anti-ERα (ERα) primary antibodies followed by the corresponding secondary antibodies. Relative intensity of chemiluminescence was measured and phospho-ERα to ERα ratio was calculated. Protein blots of pERα, ERα and β-actin (A) and graphical presentations of pERα protein expression (B), ERα protein expression (C), ratio of pERα/ERα (D) are shown. Results were obtained from three independent experiments and expressed as mean ± SEM. *P < 0.05; **P < 0.01; ***P < 0.001 versus control (C).
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