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Schematic illustration of RDNVs reverse osteoporosis by potentiating osteogenic differentiation of hBMSCs via targeting estrogen receptor α (ER α ) signaling. RDNVs, a natural product isolated from fresh Rhizoma Drynariae root juice by differential ultracentrifugation, exhibited potent bone tissue-targeting activity and anti-osteoporosis efficacy in an ovariectomized mouse model. RDNVs, effectively internalized by hBMSCs, enhanced proliferation and ER α expression levels of hBMSC, and promoted osteogenic differentiation and bone formation. Mechanistically, via the ER α signaling pathway, RDNVs facilitated mRNA and protein expression of bone morphogenetic protein 2 and runt-related transcription factor 2 in hBMSCs, which are involved in regulating osteogenic differentiation. Further analysis revealed that naringin, existing in RDNVs, was the active component targeting ER α in the osteogenic effect.
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Schematic illustration of RDNVs reverse osteoporosis by potentiating osteogenic differentiation of hBMSCs via targeting estrogen receptor α (ER α ) signaling. RDNVs, a natural product isolated from fresh Rhizoma Drynariae root juice by differential ultracentrifugation, exhibited potent bone tissue-targeting activity and anti-osteoporosis efficacy in an ovariectomized mouse model. RDNVs, effectively internalized by hBMSCs, enhanced proliferation and ER α expression levels of hBMSC, and promoted osteogenic differentiation and bone formation. Mechanistically, via the ER α signaling pathway, RDNVs facilitated mRNA and protein expression of bone morphogenetic protein 2 and runt-related transcription factor 2 in hBMSCs, which are involved in regulating osteogenic differentiation. Further analysis revealed that naringin, existing in RDNVs, was the active component targeting ER α in the osteogenic effect.
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( A ) Western blot analysis on the effects of TNC on decidualization markers <t>(BMP2,</t> WNT4, E2F8 and CYCLIN D3) after stromal cells were treatment with TNC for 72 hr. ( B ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with TNC for 72 hr. ( C ) Western blot analysisof the effects of S100A4 on decidualization markers after stromal cells were treated with S100A4 for 72 hr. ( D ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with S100A4 for 72 hr. ( E ) Western blot analysis on the effects after stromal cells were treated with SPARC for 72 hr. ( F ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated SPARC for 72 hr. ( G ) Western blot analysis on ACTIVIN A protein levels in mouse uteri on D4, D4.5, PD4, and PD4.5, respectively. ( H ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 72 hr. ( I ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with ACTIVIN A for 72 hr. ( J ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 48 hr under in vitro decidualization. EP, 17β-estradiol+progesterone. All data were is presented as means ± SD. *, p<0.05; **, p<0.01; ***, p<0.001. CYC D3: CYCLIN D3; ACT-A: ACTIVIN A. Figure 2—source data 1. Raw data of all western blots from . Figure 2—source data 2. Complete and uncropped membranes of all western blots from .
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Bone morphogenic protein 2 <t>(BMP2)</t> immunostaining results. (A) Immunohistochemical observation of jaw defects at different healing stages (BMP2 immunostaining × 100). (B) BMP2 expression (n = 6, mean ± standard deviation) was consistent in the 4 mm, 5 mm, 6 mm, 8 mm, and 10 mm groups at different cycles. There was no significant difference among groups (p > 0.05). n. s., not significant.
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Bone morphogenic protein 2 <t>(BMP2)</t> immunostaining results. (A) Immunohistochemical observation of jaw defects at different healing stages (BMP2 immunostaining × 100). (B) BMP2 expression (n = 6, mean ± standard deviation) was consistent in the 4 mm, 5 mm, 6 mm, 8 mm, and 10 mm groups at different cycles. There was no significant difference among groups (p > 0.05). n. s., not significant.
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Image Search Results


Schematic illustration of RDNVs reverse osteoporosis by potentiating osteogenic differentiation of hBMSCs via targeting estrogen receptor α (ER α ) signaling. RDNVs, a natural product isolated from fresh Rhizoma Drynariae root juice by differential ultracentrifugation, exhibited potent bone tissue-targeting activity and anti-osteoporosis efficacy in an ovariectomized mouse model. RDNVs, effectively internalized by hBMSCs, enhanced proliferation and ER α expression levels of hBMSC, and promoted osteogenic differentiation and bone formation. Mechanistically, via the ER α signaling pathway, RDNVs facilitated mRNA and protein expression of bone morphogenetic protein 2 and runt-related transcription factor 2 in hBMSCs, which are involved in regulating osteogenic differentiation. Further analysis revealed that naringin, existing in RDNVs, was the active component targeting ER α in the osteogenic effect.

Journal: Acta Pharmaceutica Sinica. B

Article Title: Rhizoma Drynariae-derived nanovesicles reverse osteoporosis by potentiating osteogenic differentiation of human bone marrow mesenchymal stem cells via targeting ER α signaling

doi: 10.1016/j.apsb.2024.02.005

Figure Lengend Snippet: Schematic illustration of RDNVs reverse osteoporosis by potentiating osteogenic differentiation of hBMSCs via targeting estrogen receptor α (ER α ) signaling. RDNVs, a natural product isolated from fresh Rhizoma Drynariae root juice by differential ultracentrifugation, exhibited potent bone tissue-targeting activity and anti-osteoporosis efficacy in an ovariectomized mouse model. RDNVs, effectively internalized by hBMSCs, enhanced proliferation and ER α expression levels of hBMSC, and promoted osteogenic differentiation and bone formation. Mechanistically, via the ER α signaling pathway, RDNVs facilitated mRNA and protein expression of bone morphogenetic protein 2 and runt-related transcription factor 2 in hBMSCs, which are involved in regulating osteogenic differentiation. Further analysis revealed that naringin, existing in RDNVs, was the active component targeting ER α in the osteogenic effect.

Article Snippet: Rabbit polyclonal antibodies against BMP2 ([EPR24209-61] (ab284387)) and RUNX2 ([EPR22858-106] (ab236639)) were purchased from Abcam (Cambridge, MA, USA).

Techniques: Isolation, Activity Assay, Expressing

( A ) Western blot analysis on the effects of TNC on decidualization markers (BMP2, WNT4, E2F8 and CYCLIN D3) after stromal cells were treatment with TNC for 72 hr. ( B ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with TNC for 72 hr. ( C ) Western blot analysisof the effects of S100A4 on decidualization markers after stromal cells were treated with S100A4 for 72 hr. ( D ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with S100A4 for 72 hr. ( E ) Western blot analysis on the effects after stromal cells were treated with SPARC for 72 hr. ( F ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated SPARC for 72 hr. ( G ) Western blot analysis on ACTIVIN A protein levels in mouse uteri on D4, D4.5, PD4, and PD4.5, respectively. ( H ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 72 hr. ( I ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with ACTIVIN A for 72 hr. ( J ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 48 hr under in vitro decidualization. EP, 17β-estradiol+progesterone. All data were is presented as means ± SD. *, p<0.05; **, p<0.01; ***, p<0.001. CYC D3: CYCLIN D3; ACT-A: ACTIVIN A. Figure 2—source data 1. Raw data of all western blots from . Figure 2—source data 2. Complete and uncropped membranes of all western blots from .

Journal: eLife

Article Title: Embryo-derive TNF promotes decidualization via fibroblast activation

doi: 10.7554/eLife.82970

Figure Lengend Snippet: ( A ) Western blot analysis on the effects of TNC on decidualization markers (BMP2, WNT4, E2F8 and CYCLIN D3) after stromal cells were treatment with TNC for 72 hr. ( B ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with TNC for 72 hr. ( C ) Western blot analysisof the effects of S100A4 on decidualization markers after stromal cells were treated with S100A4 for 72 hr. ( D ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with S100A4 for 72 hr. ( E ) Western blot analysis on the effects after stromal cells were treated with SPARC for 72 hr. ( F ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated SPARC for 72 hr. ( G ) Western blot analysis on ACTIVIN A protein levels in mouse uteri on D4, D4.5, PD4, and PD4.5, respectively. ( H ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 72 hr. ( I ) QPCR analysis of Prl8a2 mRNA level after mouse stromal cells were treated with ACTIVIN A for 72 hr. ( J ) Western blot analysis on the effects of ACTIVIN A on decidualization markers after stromal cells were treated with ACTIVIN A for 48 hr under in vitro decidualization. EP, 17β-estradiol+progesterone. All data were is presented as means ± SD. *, p<0.05; **, p<0.01; ***, p<0.001. CYC D3: CYCLIN D3; ACT-A: ACTIVIN A. Figure 2—source data 1. Raw data of all western blots from . Figure 2—source data 2. Complete and uncropped membranes of all western blots from .

Article Snippet: Antibody , Anti- BMP2 (rabbit polyclonal) , Abclonal , Cat. #: A0231 RRID: AB_2313822 , 1:1000.

Techniques: Western Blot, In Vitro

Journal: eLife

Article Title: Embryo-derive TNF promotes decidualization via fibroblast activation

doi: 10.7554/eLife.82970

Figure Lengend Snippet:

Article Snippet: Antibody , Anti- BMP2 (rabbit polyclonal) , Abclonal , Cat. #: A0231 RRID: AB_2313822 , 1:1000.

Techniques: Recombinant, Enzyme-linked Immunosorbent Assay, Staining, Software

Bone morphogenic protein 2 (BMP2) immunostaining results. (A) Immunohistochemical observation of jaw defects at different healing stages (BMP2 immunostaining × 100). (B) BMP2 expression (n = 6, mean ± standard deviation) was consistent in the 4 mm, 5 mm, 6 mm, 8 mm, and 10 mm groups at different cycles. There was no significant difference among groups (p > 0.05). n. s., not significant.

Journal: Heliyon

Article Title: Determination of critical-sized defect of mandible in a rabbit model: Micro-computed tomography, and histological evaluation

doi: 10.1016/j.heliyon.2023.e18047

Figure Lengend Snippet: Bone morphogenic protein 2 (BMP2) immunostaining results. (A) Immunohistochemical observation of jaw defects at different healing stages (BMP2 immunostaining × 100). (B) BMP2 expression (n = 6, mean ± standard deviation) was consistent in the 4 mm, 5 mm, 6 mm, 8 mm, and 10 mm groups at different cycles. There was no significant difference among groups (p > 0.05). n. s., not significant.

Article Snippet: Nonspecific binding sites were blocked using normal goat serum (Sigma-Aldrich, USA) for 30 min, after which the tissue sections were incubated with rabbit anti-bone morphogenetic protein 2 (BMP2) polyclonal antibody (1:100, bs-1012 R, Bioss, Beijing), anti-collagen type I (Col I) polyclonal antibody (1:100, bs-10423 R, Bioss, Beijing), anti-CD31 polyclonal antibody (1:100, bs-0195 R, Bioss, Beijing), overnight at 4 °C.

Techniques: Immunostaining, Immunohistochemical staining, Expressing, Standard Deviation