Additional file 1: of Quality assessment of systematic reviews on total hip or knee arthroplasty using mod-AMSTAR

Appendix 1. Protocol: the protocol of this study. (Protocol). (DOCX 27 kb

Additional file 4: of Quality assessment of systematic reviews on total hip or knee arthroplasty using mod-AMSTAR

Appendix 4. Data extraction table: Extraction items and results of each study. (Data extraction table). (XLSX 21 kb

Additional file 3: of Quality assessment of systematic reviews on total hip or knee arthroplasty using mod-AMSTAR

Appendix 3. AMSTAR score and list of included reviews: mod-AMSTAR score for each study and reference information of all included studies. (AMSTAR score and list of included reviews). (DOCX 58 kb

Prdx6 could interact with C/EBPβ <i>in vivo</i>.

<p>Immunoprecipitation was performed in PK15 cells using anti-Prdx6 and anti-IgG antibodies. Total Protein was used as input. The protein from Normal rabbit IgG group was used as negative control. (A) Detection of C/EBPβ protein in immunoprecipitation. (B) Detection of CREB protein in immunoprecipitation.</p

The porcine Prdx6 gene promoter was analyzed by computational analyses together with luciferase reporter system.

<p>(A) Conserved sequences of transcription factor binding sites of <i>Prdx6</i> promoter. The aligned region is conserved among pig, human and bovine. (B) Six promoter constructs were transfected into C2C12, 3T3-L1 and PK15 cell lines, and assayed for luciferase activity. The pGL3-Control and pGL3-Basic were the positive and negative control respectively. Green, orange, blue, red and bright blue dots on the left panel represented the C<b>/</b>EBPβ, MyoD, CREB, Sp1 and HSF binding sites predicted on TFsearch or TESS websites, respectively. Data are expressed as means ± SD of three replicates. (C) Four further deletions (D5.1, D5.2, D7, and D8) were transfected into C2C12 cells and assayed for luciferase activity.</p

Identification of <i>Prdx6</i> TSS using 5′ RACE.

<p>(A) The <i>Prdx6</i> mRNA expression profile was analyzed by RT-PCR. (B) 5′ RACE PCR product of 632bp was visualized in 1.5% agarose gel. (C) Eighteen sequencing results of <i>Prdx6</i> 5′ RACE clones are listed and the major TSS adenine was defined as +1.</p

Model for mechanisms of Prdx6 participates in adipogenesis, muscle differentiation or regeneration.

<p>C/EBPβ or CREB-mediated up-regulation of Prdx6 may participate in adipogenesis, muscle differentiation or regeneration through two pathways: (1), Prdx6 inhibits adipogenesis and muscle differentiation by scavenging ROS; (2), Prdx6 interacts with C/EBPβ to participate in adipogenesis and muscle regeneration.</p

C/EBPβ and CREB could up-regulate the <i>Prdx6</i> expression.

<p>(A) The Prdx6 deletions were co-transfected with relative overexpressed vector or pcDNA3.1 empty vector. The promoter activity was measured and the results were expressed as means± SD of three replicates. (B) Schematic structure of site-direct mutants of <i>Prdx6</i> promoter linked to pGL3-Basic vector. (C) Wild-types and mutants of the <i>Prdx6</i> deletions were transfected into C2C12 cells, and luciferase activity was detected and the results were expressed as means± SD of three replicates. (D) The <i>Prdx6</i> mRNA expression level was detected by RT-PCR after overexpression of each transcription factor into PK15 cells, data were showed as means± SD of three replicates. (E-G) The transfection efficiency of C<b>/</b>EBPβ, CREB or HSF1 overexpression vector and their effect on target Prdx6 protein expression level were determined by western blot. (H-I) The interference efficiency of Knockdown of C<b>/</b>EBPβ or CREB and their effect on target Prdx6 protein expression level were determined by western blot. Quantification results of western blot represented by ratio of C<b>/</b>EBPβ, CREB, HSF1 or Prdx6 to β-actin protein expression level (Image J software).</p

C/EBPβ and CREB bind to <i>Prdx6</i> promoter region <i>in vitro</i> and <i>in vivo</i>.

<p>(A) Binding of CREB with <i>Prdx6</i> promoter was detected by EMSA with C2C12 cell nuclear extracts. Probes of CREB binding sites were labeled with biotin and the mutated nucleotides were depicted in red color. Lane1 was a blank control that did not add nuclear extracts; Lane2 was experimental group. For Lane3 and 4, a 1-fold excess of unlabeled or mutant probe was added to the reaction complex. The Lane5 was added 2μg anti-CREB antibody in the complex. The DNA-protein complex and the super-shift bands were indicated by arrows (B) ChIP assay of CREB binding to the <i>Prdx6</i> promoter in PK15 cells. (C) The interaction of C<b>/</b>EBPβ with <i>Prdx6</i> promoter was detected by EMSA with the porcine IMF cell nuclear extracts. The Lane1-5 experimental groups are similar to figure 4A. (D) Binding of C<b>/</b>EBPβ on the <i>Prdx6</i> promoter was determined by ChIP assay.</p

New developments in non-exosomal and exosomal ncRNAs in coronary artery disease. Supplementary material.

Supplementary figures 1 and 2    Supplementary material Table S1. Findings of miRNAs in coronary artery disease    Supplementary material Table S2. Findings of lncRNAs in coronary artery disease    Supplementary material Table S3. Findings of circRNAs in coronary artery disease    Supplementary material Table S4. Findings of exosomal-derived ncRNAs in coronary artery disease</p