Highly Oriented SrTiO₃ Thin Film on Graphene Substrate

Growth of perovskite oxide thin films on Si in crystalline form has long been a critical obstacle for the integration of multifunctional oxides into Si-based technologies. In this study, we propose pulsed laser deposition of a crystalline SrTiO₃ thin film on a Si using graphene substrate. The SrTiO₃ thin film on graphene has a highly (00<i>l</i>)-oriented crystalline structure which results from the partial epitaxy. Moreover, graphene promotes a sharp interface by highly suppressing the chemical intermixing. The important role of graphene as a 2D substrate and diffusion barrier allows the expansion of device applications based on functional complex oxides

Suppression of Cpn10 exacerbates 3-NP-mediated mitochondrial dysfunction in SK-N-MC cells.

<p>(A) SK-N-MC cells were transfected with either scrambled siRNA or Cpn10 siRNA (si#1, si#2) with or without Drp1 siRNA (siDrp1) for 5 days. The cells were further exposed to 3-NP (10 mM) for 8 hr, then cells with fragmented mitochondria were counted with a fluorescence microscope. (B, C) SK-N-MC cells were transfected with either scrambled siRNA or Cpn10 siRNA (si#1, si#2) with or without Drp1 siRNA (siDrp1) for 5 days, then cells were further exposed to 3-NP (10 mM) for 8 hr. The total cellular ATP level was measured by an ATP bioluminescence detection assay (B). The intracellular ROS level was determined by a DCFH-DA fluorescence ROS detection assay (C). Data are represented as the mean ± SEM (n>3), and were considered significant at a value of *<i>p</i><0.02, **<i>p</i><0.05.</p

Down-regulation of Cpn10 promotes mitochondrial dysfunction in SK-N-MC cells.

<p>(A-C), SK-N-MC cells were transfected with a control scrambled (Sc) or Cpn10 siRNA (si #1, si #2). After 5 days, the alteration of mitochondrial membrane potential was monitored by the MitoProbe JC-1 assay (A). The cellular total ATP level was examined by an ATP bioluminescence detection assay (B). The Intracellular ROS level was measured by a DCFH-DA fluorescence ROS detection assay (C). Data are represented as the mean ± SEM (n>3), and were considered significant at a value of *<i>p</i><0.05.</p

Down-regulation of Cpn10 induces mitochondrial fragmentation in neuroblastoma cells.

<p>(A, B) SK-N-MC cells stably expressing mito-YFP (SK/mito-YFP) were transfected with either a control scrambled siRNA (Sc) or a specific siRNA against Cpn10 for 5 days. Then mitochondrial morphology (A) and mitochondrial length (B) were examined with a fluorescence microscope. Both Drp1 siRNA (siDrp1) and Opa1 siRNA (siOpa1) were used as positive controls. (C) The reduced expression of Cpn10 by siRNA was confirmed by Western blotting. (D) SK/mito-YFP cells were transfected with scrambled siRNA or Cpn10 siRNAs (si#1, si#2). And the mitochondrial fragmentation was observed by a fluorescence microscopy at the indicated time points. (E) SH-SY5Y cells were transfected with either a control scrambled siRNA (Sc) or specific siRNAs against Cpn10 (siCPN10 #1, #2). After 5 days, the cells were stained with Mito-tracker (100 nM), and the cells containing fragmented mitochondria were counted using a fluorescence microscope. Data are represented as the mean ± SEM. (n>3).</p

Loss of Cpn10 potentiates 3-NP-mediated cell death in SK-N-MC cells.

<p>(A) SK/mito-YFP cells were transfected with scrambled siRNA (Sc) or Cpn10 siRNA (si#1, si#2). After 5 days, the cells were further incubated with 3-NP (10 mM) in the presence or absence of a ROS inhibitor, NAC (1 mM) for 24 hr. Then cells were stained with Annexin V and propidium iodide to measure cell viability by a flow cytometric analysis. Data are represented as the mean ± SEM (n>3), and were considered significant at a value of *<i>p</i><0.02.</p

Inhibition of Drp1 suppresses mitochondria fragmentation induced by loss of Cpn10.

<p>(A) Drp1 siRNA was co-transfected with either scrambled siRNA (Sc) or Cpn10 siRNA (#1, #2) in SK/mito-YFP cells. 5 days later, the cells with fragmented mitochondria were counted under a fluorescence microscopy. (B) Wild type MEF (WT) and Drp1 deficient MEF (Drp1^-/-) cells were transfected with either a control scrambled siRNA (Sc) or specific siRNAs against Cpn10 (siCPN10 #1, #2). After 5 days, the cells were labeled with a fluorescence MitoTracker (100 nM) to observe mitochondrial morphology. The cells with fragmented mitochondria were counted under a fluorescence microscopy. (C) The reduced expression of Drp1 in Drp1 siRNA transfected cells and in Drp1 knock out MEF cells was confirmed by Western blotting. (D) SK/mito-YFP cells transfected with scrambled siRNA (Sc) or Cpn10 siRNA (si#1, si#2) were treated with a Drp1 inhibitor, Mdivi-1 (20 µM). The cells with fragmented mitochondria were counted under a fluorescence microscope. Data are represented as the mean ± SEM. (n>3) and were considered significant at a value of *<i>p</i><0.02.</p

hUCB-MSC-CM suppresses melanogenesis in an artificial human skin model.

<p>(A-C) MelanoDerm tissues were incubated with either growth medium (Cont) or hUCB-MSC-CM for 20 days or resveratrol (RSV) for 18 days. Then the Melanoderm tissues were observed under a microscope (A) or analyzed by Masson-Fontana staining (B). The tissues were collected to determine the total melanin content (C). RSV was used as a positive control agent. Data represent standard error of the mean (S.E.M) from three independent experiments (n = 3, p<0.05)</p

hUCB-MSC-CM suppresses α-MSH-induced melanogenesis.

<p>(A) Melan-a cells pre-treated with α-MSH (1 μM) for 24 hr were incubated with BM (medium form bone marrow mesenchymal stem cells), Adi (medium from adipocyte mesenchymal stem cells), Ker (medium from human epidermal keratinocytes), and UCB (medium from human umbilical cord blood-derived mesenchymal stem cells) for additional 24 hr. Cells were treated with arbutin (500 μM) as an anti-melanogenic agent. Then, the cells were collected (upper image) to measure cellular melanin contents (lower graph) as described in the Material and Methods section. (B) B16F1 cells pre-treated with α-MSH (1 μM) for 24 hr were incubated with BM, Adi, Ker, UBC, and arbutin (500 μM) for 24 hr. Then, the cells were collected (upper image) to examine the cellular melanin contents (lower graph). (C) Melan-a mouse melanocytes pre-treated with forskolin (20 μM) for 24 hr were incubated with BM (medium from bone marrow mesenchymal stem cells), Adi (medium from adipocyte mesenchymal stem cells), Ker (medium form human epidermal keratinocytes), or UCB (medium from human umbilical cord blood-derived mesenchymal stem cells) for additional 24 hr. Cells were treated with arbutin (500 μM) as a positive control. Then, the cells were collected to measure cellular melanin contents. (D) Normal human epidermal melanocytes were pre-treated with forskolin (20 μM) for 48 hr. The cells were further incubated with hUCB-MSC-CM or arbutin (500 μM) for 48 hr, and cellular melanin contents were measured. Data represent ± standard error of the mean (S.E.M.) from three independent experiments (n = 3,* <i>p</i><0.02).</p

Sertraline inhibits primary cilia disassembly in htRPE cells.

<p>(A and B) htRPE/Smo-GFP cells were plated in a medium without serum for 48 h. Next, the cells were further incubated with normal medium in the absence (A) or presence of sertraline (10 μM) (B). The percentage of cells with cilia was counted at the indicated time points. Data represent ± standard error of the mean (S.E.M.) from three independent experiments (n = 3,* <i>p</i> < 0.02).</p

hUCB-MSC-CM induces proteasomal degradation of MITF mediated by ERK phosphorylation.

<p>(A) Melan-a cells pre-treated with α-MSH (200 nM) for 24 hr were further incubated with hUCB-MSC-CM (UCB) in the presence or absence of PD98059 (20 μM) for 24 hr. Then, the expression of phosphorylated MITF at Serine 73 and total MITF protein was examined with Western blot analysis. (B) Melan-a cells pre-treated with α-MSH (200 nM) were incubated with UCB with or without MG132 (5 μM) for an additional 24 hr. Then the MITF level was examined by Western blot analysis. (C) Human MNT-1 melanoma cells transiently transfected with pEGFP (pCont) or pEGFP-MITF (pMITF) were treated with α-MSH (1 μM). After 24 hr, the cells were further incubated with UCB for additional 24 hr. Then the cells were harvested to measure the cellular melanin contents. The over-expression of MITF was confirmed by Western blotting with anti-GFP antibody. Data represent ± standard error of the mean (S.E.M.) from more than three independent experiments, n = 3,* <i>p</i><0.05).</p