Functionalized Nylon 6 Fabric as an Efficient and Recyclable Catalyst for Knoevenagel Condensation

Nylon 6 fabrics were chemically modified via reduction with BH3 for being functionalized as heterogeneous base organocatalysts for Knoevenagel condensation. The results of FTIR, XPS, and SEM indicated the successful modification of nylon 6 fabrics. With a low catalytic dosage of 6.6 mol % and a short reaction time (2 h), the fabric catalysts were well applicable to Knoevenagel condensation of a wide range of substrates and up to 98% yield could be obtained. In addition, the fabric catalysts have some beneficial advantages in terms of easy separation, good reusability, and recyclability (up to 10 times)

Functional Study of miR-27a in Human Hepatic Stellate Cells by Proteomic Analysis: Comprehensive View and a Role in Myogenic Tans-Differentiation

<div><p>We previous reported that miR-27a regulates lipid metabolism and cell proliferation during hepatic stellate cells (HSCs) activation. To further explore the biological function and underlying mechanisms of miR-27a in HSCs, global protein expression affected by overexpression of miR-27a in HSCs was analyzed by a cleavable isotope-coded affinity tags (cICAT) based comparative proteomic approach. In the present study, 1267 non-redundant proteins were identified with unique accession numbers (score ≥1.3, i.e. confidence ≥95%), among which 1171 were quantified and 149 proteins (12.72%) were differentially expressed with a differential expression ratio of 1.5. We found that up-regulated proteins by miR-27a mainly participate in cell proliferation and myogenesis, while down-regulated proteins were the key enzymes involved in de novo lipid synthesis. The expression of a group of six miR-27a regulated proteins was validated and the function of one miR-27a regulated protein was further validated. The results not only delineated the underlying mechanism of miR-27a in modulating fat metabolism and cell proliferation, but also revealed a novel role of miR-27a in promoting myogenic tans-differentiation during HSCs activation. This study also exemplified proteomics strategy as a powerful tool for the functional study of miRNA.</p></div

Additional file 1 of Panobinostat (LBH589) combined with AM1241 induces cervical cancer cell apoptosis through autophagy pathway

Additional file 1: Figure S1. Synergistic effect chart of AM1241 and LBH589 combined treatment on SiHa cervical cancer cells. Synergistic effect charts of SiHa cervical cancer cells were calculated using (A) ZIP, (B) HSA, (C) Bliss, and (D) Loewe reference models. These data were obtained using the SynergyFinder software. The synergistic effect is manifested as a ZIP synergy score of more than 1, and Loewe, Bliss, and HSA synergistic scores of more than 0 (n=5)

Functional Categories of Up-regulated Proteins in LX2/miR-27a Compared with LX2/miR-neg (H/L ≥1.5).

<p>Proteins from LX2/miR-27a were labeled with heavy isotope (H) tagging and those from LX2/miR-neg were labeled with light isotope (L) tagging. Data were from two independent cICAT-based quantitative analyses.</p><p>Functional Categories of Up-regulated Proteins in LX2/miR-27a Compared with LX2/miR-neg (H/L ≥1.5).</p

Supplementary Data from Mathematical Modeling Provides Evidence for Niche Competition in Human AML and Serves as a Tool to Improve Risk Stratification

Supplementary Methods, Supplementary Figures 1-7 and Supplementary Tables 1-3.</p

Involvement of FLH1 in miR-27a related HSCs proliferation and migration.

<p>Knockdown of FLH1 suppressed cell proliferation in LX2/miR-27a transfectants. (A) EdU cell proliferation assay. EdU was detected by Apollo 567 fluorescent dye (red) and nuclei were counterstained with Hoechst 33342 (blue) (original magnification ×200). (B) Statistical results of three independent experiments. The results are expressed as the labeling index according to the following formula: number of EdU-positive nuclei x 100/number of total nuclei. FHL1 was required for increased migration in LX2/miR-27a transfectants. (C) Migration assays. LX2/miR-27a transfectants were plated on 8-lm pore size Transwell inserts for 16 hours. The number of migrated cells was counted manually (original magnification ×200). (D) The statistical results of three independent experiments. Each image is a representative of three independent experiments. ***P<0.001, **P<0.01 compared with LX2/miR-neg.</p

Establishment and biological characters of LX2/miR-27a, LX2/miR-neg stable transfectants.

<p>(A) Almost all cells in the positive clone expressed EmGFP (green), original magnification ×200. (B) The expression of miR-27a in LX2/miR-27a, LX2/miR-neg stable transfectants. (C) Over-expression of miR-27a promoted LX2 cell proliferation. (D) miR-27a over-expression facilitated LX2 migration. <i>**P<</i>0.01 compared with LX2/miR-neg.</p

Overall distribution of miR-27a regulated proteins in LX2 cells.

<p>(A) Cell location and (B) Functional distribution of all the 134 differentially expressed proteins.</p

Predicted miR-27a Targets among Down-regulated Proteins in LX2/miR-27a Identified by cICAT.

<p>* P_CT, the probability of conserved targeting.</p><p>Predicted miR-27a Targets among Down-regulated Proteins in LX2/miR-27a Identified by cICAT.</p

Protein samples from LX2/miR-27a and LX2/miR-neg were compared by cleavable isotope-coded affinity tag (cICAT)-based quantitative proteomic analysis - identification and quantitation of ATP-citrate synthase.

<p>(A) Total ion chromatogram (TIC) indicating cICAT-labeled peptides eluting from a reverse phase column. (B) Expanded MS spectrum view of a pair of peaks showing the differential expression between peptides labeled with the isotopically light and heavy cICAT reagent. (C) MS/MS spectrum analysis of the light-cICAT labeled triply charged peptide (681.4 <i>m/z</i>) showed in (B) led to identification of a peptide with sequence GVTIIGPATVGGIKPGCFK (<a href="mailto:ICAT-C(C)@17" target="_blank">ICAT-C(C)@17</a>), unique to the ATP-citrate synthase (ACLY), a predicted target of miR-27a. The labels b and y designated the N- and C- terminal fragments, respectively, of the peptide produced by breakage at the peptide bond in the mass spectrometer. The number represents the number of N- or C- terminal residues present in the peptide fragment. (D) Venn diagram depicting the overlap of proteins identified in two independent cICAT experiments. Numbers in parentheses indicate the number of identified proteins for each sample. To examine the biological reproducibility, linear regression analyses were performed on H/L ratios (LX2/miR-27a/LX2/miR-neg) of two independent analyses. Pearson correlation coefficient between samples 1 and 2 was 0.8039, P<0.01.</p