Controllable Synthesis, Formation Process, and Luminescence Performances of Diverse Yttrium Compounds with Hollow Structures

Hollow spherical Y2O3 and YBO3 have been prepared by a facile template-directed strategy using phenol-formaldehyde (PF) resin spheres as templates. The PF@Y(OH)CO3 precursor can be fabricated by a simple precipitation route. The Y2O3 hollow spheres are obtained via a direct annealing process, and the hollow spherical YBO3 are fabricated via a hydrothermal route followed by an annealing process at the expense of the same PF@Y(OH)CO3 precursor. The whole synthesis procedure is performed in aqueous solution without any surfactant or catalyst. Moreover, YVO4 quasi-octahedral microcrystals with spherical holes are obtained. The formation mechanisms of the yttrium compounds with different morphologies have been discussed. By incorporating proper rare earth activator ions into the Y2O3, YBO3, and YVO4 hosts, the as-synthesized luminescent materials can exhibit eminent performances with both down-conversion and up-conversion luminescence. Furthermore, the as-fabricated light-emitting diode (LED) devices can emit dazzling characteristic emission light, which reveals that the phosphors have application potential in lighting and displays. This simple synthesis strategy may provide a new idea for the fabrication of inorganic compounds with perfect hollow structures and excellent properties

Dose-volume-histograms for ten patient data set.

<p>Dose volume histograms (DVH) for all 10 patients in our study with a planning evaluation of step-and-shoot IMRT, RapidArc, and TomoTherapy for the brain.</p

Defect-Related Luminescent Mesoporous Silica Nanoparticles Employed for Novel Detectable Nanocarrier

Uniform and well-dispersed walnut kernel-like mesoporous silica nanoparticles (MSNs) with diameters about 100 nm have been synthesized by a templating sol–gel route. After an annealing process, the as-obtained sample (DLMSNs) inherits the well-defined morphology and good dispersion of MSNs, and exhibits bright white-blue luminescence, higher specific surface area and pore volume, and better biocompatibility. The drug loading and release profiles show that DLMSNs have high drug loading capacity, and exhibit an initial burst release followed by a slow sustained release process. Interestingly, the luminescence intensity of the DLMSNs-DOX system increases gradually with the increase of cumulative released DOX, which can be verified by the confocal laser scanning images. The drug carrier DLMSNs can potentially be applied as a luminescent probe for monitoring the drug release process. Moreover, the DLMSNs-DOX system exhibits potent anticancer effect against three kinds of cancer cells (HeLa, MCF-7, and A549 cells)

Up-Conversion Y₂O₃:Yb³⁺,Er³⁺ Hollow Spherical Drug Carrier with Improved Degradability for Cancer Treatment

The rare earth hollow spheres with up-conversion luminescence properties have shown potential applications in drug delivery and bioimaging fields. However, there have been few reports for the degradation properties of rare earth oxide drug carriers. Herein, uniform and well-dispersed Y₂O₃:Yb³⁺,Er³⁺ hollow spheres (YOHSs) have been fabricated by a general Pechini sol–gel process with melamine formaldehyde colloidal spheres as template. The novel YOHSs with up-conversion luminescence has good drug loading amount and drug-release efficiency; moreover, it exhibits pH-responsive release patterns. In particular, the YOHSs sample exhibits low cytotoxicity and excellent degradable properties in acid buffer. After the sample was loaded with anticancer drug doxorubicin (DOX), the antitumor result <i>in vitro</i> indicates that YOHS-DOX might be effective in cancer treatment. The animal imaging test also reveals that the YOHSs drug carrier can be used as an outstanding luminescent probe for bioimaging <i>in vivo</i> application prospects. The results suggest that the degradable drug carrier with up-conversion luminescence may enhance the delivery efficiency of drugs and improve the cancer therapy in clinical applications

Effect of pristimerin on cell growth.

<p>BxPC-3, PANC-1 and AsPC-1 cells were grown in the absence or presence of increasing concentration of pristimerin for 24 h, 48 h and 72 h and then the viability of cells was measured by CCK-8 assay as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>. Data shown are representative of at least three independent experiments. *P<0.05, compared with control. **P<0.01, compared with control.</p

Effect of pristimerin on apoptosis induction in pancreatic cancer cells.

<p>(A) Effect of pristimerin on apoptosis induction assessed by Annexin V/PI method using flow cytometry. BxPC-3, PANC-1 and AsPC-1 cells were cultured in complete medium and treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h. Apoptosis rate was determined by flow cytometry on annexin V-FITC. (B) Representative dot-plots from cytometrically illustrating apoptotic status in BxPC-3 (upper panel), PANC-1 (middle panel) and AsPC-1 (lower panel) cells. (C) Effect of pristimerin on apoptosis induction assessed by fluorescence microscopy. Cells were also viewed under a fluorescence microscopy. Representative photographs were taken from Annexin V/PI-stained pancreatic cancer cells under certain treatment. (D) Effect of pristimerin on apoptosis induction assessed by caspase-3 activity assay. Cell lysates were assayed for caspase-3 activity as described in “<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and methods</a>”. (E) Effect of pristimerin on cleavage of caspase-3. As detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>, pancreatic cancer cells (BxPC-3, PANC-1 and AsPC-1) were treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h and then harvested. Total cell lysates were prepared and subjected to SDS-PAGE followed by Western blot analysis. β-actin was detected as protein loading control. The immunoblots shown here are representative of at least three independent experiments with similar results. *P<0.05, compared with control. **P<0.01, compared with control.</p

Potentiation of the effect of gemcitabine by pristimerin in pancreatic cancer cells.

<p>(A) Potentiation of gemcitabine-induced cell growth inhibition by pristimerin. Cells were grown in the absence or presence of pristimerin (200 nM), gemcitabine (500 nM) or their combination for 48 h. The viability of cells was measured by CCK-8 assay as described in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>. Combination index (CI) versus fraction affected (Fa) plots obtained from median-effect analysis of Chou-Talalay. CI values: >1, antagonism; 1, additivity; <1, synergism. (B) Potentiation of gemcitabine-induced apoptosis by pristimerin. Cells were grown in the absence or presence of pristimerin (200 nM), gemcitabine (500 nM) or their combination for 48 h. Apoptosis rate was determined by flow cytometry on annexin V-FITC. *P<0.05, compared with control. **P<0.01, compared with control. ^#P<0.05, compared with single gemcitabine group.^##P<0.01, compared with single gemcitabine group.</p

Effect of pristimerin on cell cycle distribution and expression of cell cycle-related proteins.

<p>(A) Effect of pristimerin on cell cycle distribution in pancreatic cancer cells. BxPC-3, PANC-1 and AsPC-1 cells were cultured in complete medium and treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h. After treatment, cells were collected by trypsinization, washed with ice-cold PBS, and digested with RNase. Cellular DNA was stained with propidium iodide and flow cytometric analysis was performed for the detection of the percentage of cells in the different phases of the cell cycle as described in the <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>. *P<0.05, compared with control. **P<0.01, compared with control. (B) Effect of pristimerin on the protein level of cyclin D1, cyclin E, cdk 2, cdk 4, cdk 6, WAF1/p21 and KIP1/p27 in pancreatic cancer cells. As detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>, pancreatic cancer cells (BxPC-3, PANC-1 and AsPC-1) were treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h and then harvested. Total cell lysates were prepared and subjected to SDS-PAGE followed by Western blot analysis for G1 cell cycle regulatory proteins (cyclin D1, cyclin E, cdk2, cdk4, cdk6, WAF1/p21 and KIP1/p27). β-actin was detected as protein loading control. The immunoblots shown here are representative of at least three independent experiments with similar results.</p

Effect of pristimerin on NF-κB activation in pancreatic cancer cells.

<p>(A) Effect of pristimerin on protein levels of NF-κB/p65 in nuclear lysates and total cell lysates of pancreatic cancer cells. As detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>, pancreatic cancer cells (BxPC-3, PANC-1 and AsPC-1) were treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h and then harvested. Nuclear lysates and total cell lysates were prepared and subjected to SDS-PAGE followed by Western blot analysis for the protein level of NF-κB/p65, p-IκB-α (S32/36) and IκB-α. β-actin was detected as protein loading control. The immunoblots shown here are representative of at least three independent experiments with similar results. (B) Effect of pristimerin on NF-κB/p65 DNA-binding activity in pancreatic cancer cells. As detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>, pancreatic cancer cells (BxPC-3, PANC-1 and AsPC-1) were treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h and then harvested. Nuclear lysates were prepared and the NF-κB DNA-binding activity was determined using the Trans-Am NF-κB ELISA Kit. *P<0.05, compared with control. **P<0.01, compared with control.</p

Effect of pristimerin on the protein level of Bcl-xl, Bcl-2 and Bax.

<p>As detailed in <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0043826#s4" target="_blank">Materials and Methods</a>, pancreatic cancer cells (BxPC-3, PANC-1 and AsPC-1) were treated with either pristimerin (200, 400 or 600 nM) or DMSO (control) for 48 h and then harvested. Total cell lysates were prepared and subjected to SDS-PAGE followed by Western blot analysis. β-actin was detected as protein loading control. The immunoblots shown here are representative of at least three independent experiments with similar results.</p