Additional file 1 of De novo assembly of the complete mitochondrial genome of sweet potato (Ipomoea batatas [L.] Lam) revealed the existence of homologous conformations generated by the repeat-mediated recombination

Additional file 1: Table S1. The primers design for repeats mediate the homologous recombination I. batatas. Table S2. Microsatellite repeats in the mitogenome. Table S3. Dispersed repeats in the mitogenome. Table S4. The DNA transfer in the mitochondrial genome of I. batatas. Table S5. The RNA editing events prediction in the I. batatas. Figure S1. The graph-based mitochondrial genome of I. batatas. Figure S2.The raw Gel diagram of agarose gel electrophoresis

MicroRNA let-7c Inhibits Cell Proliferation and Induces Cell Cycle Arrest by Targeting CDC25A in Human Hepatocellular Carcinoma

<div><p>Down-regulation of the microRNA let-7c plays an important role in the pathogenesis of human hepatocellular carcinoma (HCC). The aim of the present study was to determine whether the cell cycle regulator CDC25A is involved in the antitumor effect of let-7c in HCC. The expression levels of let-7c in HCC cell lines were examined by quantitative real-time PCR, and a let-7c agomir was transfected into HCC cells to overexpress let-7c. The effects of let-7c on HCC proliferation, apoptosis and cell cycle were analyzed. The in vivo tumor-inhibitory efficacy of let-7c was evaluated in a xenograft mouse model of HCC. Luciferase reporter assays and western blotting were conducted to identify the targets of let-7c and to determine the effects of let-7c on CDC25A, CyclinD1, CDK6, pRb and E2F2 expression. The results showed that the expression levels of let-7c were significantly decreased in HCC cell lines. Overexpression of let-7c repressed cell growth, induced cell apoptosis, led to G1 cell cycle arrest in vitro, and suppressed tumor growth in a HepG2 xenograft model in vivo. The luciferase reporter assay showed that CDC25A was a direct target of let-7c, and that let-7c inhibited the expression of CDC25A protein by directly targeting its 3ʹ UTR. Restoration of CDC25A induced a let-7c-mediated G1-to-S phase transition. Western blot analysis demonstrated that overexpression of let-7c decreased CyclinD1, CDK6, pRb and E2F2 protein levels. In conclusion, this study indicates that let-7c suppresses HCC progression, possibly by directly targeting the cell cycle regulator CDC25A and indirectly affecting its downstream target molecules. Let-7c may therefore be an effective therapeutic target for HCC.</p></div

Pedigree of the family with spondyloepiphyseal dysplasia congenita showing affected cases (fully shaded).

<p>N: normal; M: the <i>COL2A1</i> c.620G>A (p.Gly207Glu) mutation.</p

Effect of let-7c on CDC25A protein expression in HCC xenograft tumors.

<p>Immunohistochemical analyses show the effect of let-7c on CDC25A protein expression in HCC xenograft tumors infected with lentiviral pLenO-RFP-Let-7c or the pLenO-RFP negative control.</p><p>Effect of let-7c on CDC25A protein expression in HCC xenograft tumors.</p

Phase-Change Composites Composed of Silicone Rubber and Pa@SiO₂@PDA Double-Shelled Microcapsules with Low Leakage Rate and Improved Mechanical Strength

A kind of silicone rubber (SR)/paraffin (Pa)@silicon dioxide (SiO2)@polydopamine (PDA) phase-change composite was prepared in this work. The double-shelled Pa@SiO2@PDA phase-change microcapsules were constructed by oxidative self-polymerization of dopamine (DA) in Tris-HCl buffer solution. The effect of the DA content on the properties of Pa@SiO2@PDA microcapsules and SR/Pa@SiO2@PDA composites was researched. Due to the protective effect of SiO2, PDA layer, and SR matrix, the SR/Pa@SiO2@PDA composites have good leak-proofing performance, and the leakage rate of SR/Pa@SiO2@PDA-2 is as low as 0.45%. Phase-change enthalpies of the Pa@SiO2@PDA microcapsules and SR/Pa@SiO2@PDA composites are reduced slightly with increasing DA content. Meanwhile, the composites displayed improved mechanical strength. The tensile strength of SR/Pa@SiO2@PDA-2 can be up to 0.560 MPa, which is 1.85 times higher than the tensile strength of pure SR/Pa@SiO2 because the interface compatibility between Pa@SiO2 microcapsules and SR is improved through hydrogen bonding between the abundant groups on the PDA surface and the matrix. Moreover, the rough surface of the PDA-modified microcapsules also enhances the interface interaction through physical “interlocking”. The new kind of SR/Pa@SiO2@PDA composite can be used for thermal management

Presentation1_Integration of Distinct Analysis Strategies Improves Tissue-Trait Association Identification.pdf

Integrating genome-wide association studies (GWAS) with transcriptomic data, human complex traits and diseases have been linked to relevant tissues and cell types using different methods. However, different results from these methods generated confusion while no gold standard is currently accepted, making it difficult to evaluate the discoveries. Here, applying three methods on the same data source, we estimated the sensitivity and specificity of these methods in the absence of a gold standard. We established a more specific tissue-trait association atlas by combining the information captured by different methods. Our triangulation strategy improves the performance of existing methods in establishing tissue-trait associations. The results provide better etiological and functional insights for the tissues underlying different human complex traits and diseases.</p

CDC25A induces the G1-to-S phase transition in HCC cells.

<p>(A,B) Western blotting of CDC25A protein expression in HepG2 cells infected/transfected with lenti-CDC25A, lenti-control, CDC25A-siRNA or negative control-siRNA. (C) Western blot analysis of CDC25A expression in SMMC-7721 cells and SMMC-7721-let-7c stable cells with or without CDC25A* reintroduction. (D,E) Infection/transfection of HepG2 cells with lenti-CDC25A, lenti-control, CDC25A-siRNA or negative control-siRNA was performed to investigate the effects of CDC25A on the HCC cell cycle. Representative images are shown. (F) Cell cycle assays of SMMC-7721 cells or SMMC-7721-let-7c stable cells with or without CDC25A* reintroduction. Restoration of CDC25A significantly induced the G1-to-S phase transition in SMMC-7721 cells. Representative images are shown. *CDC25A was reintroduced without its 3′-UTR to prevent the expression of CDC25A from being inhibited by let-7c.</p

Let-7c agomir inhibits tumor growth in a xenograft mouse model of HCC in vivo.

<p>(A) Photographs of tumor-bearing mice in the fifth week after injection with let-7c agomir (Left) or negative control (Right). (B) From seventh day after the injection, measurements of tumor size were taken every 7 days for 5 weeks. Effects of let-7c agomir on the xenograft mouse model are shown. Data are shown as the mean ± S.D. The statistical difference was analyzed by the two-sample t test. (C) Photographs of tumors that developed in the mouse model of HCC treated with let-7c or the negative control are presented. The two smallest tumors with the let-7c treatment are indicated by red arrows, and the two smallest tumors in the negative control group are indicated by blue arrows.</p

Let-7c targets CDC25A in HCC cells.

<p>(A) Firefly luciferase reporter vectors containing the CDC25A wild-type (pmiR-CDC25A-3′-UTR-wt) or mutant (pmiR- CDC25A-3′-UTR–mut) 3′-UTR were generated and co-transfected into HepG2 cells along with either the let-7c agomir or negative control to identify CDC25A targets. The 3′UTR of CDC25A mRNA contained two complementary sites for the seed region of let-7c. (b) Wild: wild-type; Mut: mutated. The seed sequence is underlined. (B) Relative luciferase activity was analyzed after the reporter plasmids or control reporter plasmid were co-transfected with let-7c into HEK-293 cells. Representative experiments are shown. (C) Western blot assays of the endogenous CDC25A protein level in HepG2 cells transfected with the let-7c agomir, negative control or let-7c inhibitor. (D) Real-time PCR assay of CDC25A mRNA expression in HepG2 cells transfected with the let-7c agomir or negative control.</p