OMVs are spherical

portions of bacterial envelope containing outer membrane protein and lipid as well as soluble material contained BGJ398 in the lumen or bound to the external surface [2, 3]. The role of OMVs in intercellular transport and signaling by pathogenic bacteria has been the subject of numerous studies [3]. However, only a few reports investigated more generally beneficial roles for OMVs that would explain their development in non-pathogenic Gram-negative bacterial species. Of these, some have described a role for OMVs in countering environmental stress and stressors. For instance, one report demonstrated that OMVs are induced by and protect bacteria from toluene exposure [4], and others reported that OMVs contribute to the formation

of Selleckchem Small molecule library biofilms which have a well-known role in bacterial resistance to harsh environments [5, 6]. In addition, Grenier et al discovered that OMVs from Porphyromonas gingivalis could protect cells against chlorhexidine, as well as provide degradative enzymatic activities to neutralize the killing abilities of human serum [7, 8]. Furthermore, mutations resulting in hyper-production of OMVs were found to be advantageous when E. coli was challenged with otherwise lethal environmental stresses, including antimicrobials and ethanol, a general denaturant [4, 9]. Natural antibiotics are common antimicrobial stressors encountered by bacteria in the environment as well as during infection of a host. Antimicrobial peptides (AMPs) are a key human defense to bacterial infections, as well as a defense employed by other Gram-positive and Gram-negative bacteria [10, 11]. Antimicrobial peptides have also been found in a growing variety of other host organisms, including mice, insects, and

frogs [12–15]. Few, however, acknowledge the sub-inhibitory concentrations of these defensins that pathogens commonly encounter on the epithelial surfaces, or in the environment [10, 16]. The most common mechanism of action for these AMPs is alteration of bacterial Methocarbamol membrane permeability, typically by pore formation [15, 17, 18]. Because of their generic target and their speed of action, AMPs have recently been revisited in the quest to develop novel antibiotics against Gram-positive and Gram-negative pathogens [14, 19–22]. Currently, AMPs are used as a last line of defense against some multi-drug resistant pathogens [22–24]. Most bacterial AMP-resistance is characterized by lipid modifications to alter the charge of the outer membrane [25–27]. However these resistance pathways cannot fully explain the extent of resistance seen in Gram-negative bacteria [16]. We hypothesize that OMVs may act as a modulating intrinsic defense against AMPs as well as other outer membrane acting stressors, and that this defense may help to explain the gap in our current understanding of how Gram-negative bacteria respond to these compounds.

The strains were propagated in LB broth or LB agar at 37°C. Table 3 List of strains used in this study. strain strain ID SPI present SPI absent reference S. Enteritidis 147 Nal wild click here type 7F4 1, 2, 3, 4, 5 none [28] S. Enteritidis 147 Nal ΔSPI1 4A10 2,3,4,5 1 [30] S. Enteritidis 147 Nal ΔSPI2 5D10 1,3,4,5 2 [30] S. Enteritidis 147

Nal ΔSPI3 6A9 1,2,4,5 3 [30] S. Enteritidis 147 Nal ΔSPI4 4B10 1,2,3,5 4 [30] S. Enteritidis 147 Nal ΔSPI5 4J1 1,2,3,4 5 [30] S. Enteritidis 147 Nal ΔSPI1-5 5E9 none 1,2,3,4,5 [30] S. Enteritidis 147 Nal SPI1o 5G10 1 2,3,4,5 [30] S. Enteritidis 147 Nal SPI2o 5H9 2 1,3,4,5 [30] S. Enteritidis 147 Nal SPI3o 5J10 3 1,2,4,5 [30] S. Enteritidis 147 Nal SPI4o 5D9 4 1,2,3,5 [30] S. Enteritidis 147 Nal SPI5o 5H10 5 1,2,3,4 [30] S. Enteritidis 147 Nal Δlon 16H2 1, 2, 3, 4, 5 none [33] S. Enteritidis 147 Nal ΔrfaL 14E5 1, 2, 3, 4, 5 none [33] Experimental infection of mice In all the experiments, six-week-old Balb/C mice were orally infected with 104 CFU (equivalent to 100 × LD50 of the wild type strain) of the wild type strain or each of the mutants in a volume of 0.1 ml using a gastric gavage without any neutralisation of gastric acid prior the

infection. In the first animal infection, 12 groups of 10 mice each were infected with all the SPI mutants and wild type S. Enteritidis. A negative control group consisted of 3 uninfected animals. On day 5 post-infection, 3 mice from each group including GDC 941 all non-infected control mice were sacrificed and used for the determination of bacterial counts in liver, spleen and caecum, two-color flow cytometry of splenic lymphocytes, histology in liver and caecum, and lymphocyte proliferation assay. The remaining 7 mice were left for monitoring of feacal shedding and mortalities until day 21 post infection when the experiment was terminated. Faecal shedding was monitored on a daily basis by transferring the mice into a clean plastic box and collecting pooled fresh droppings 30 minutes later. Bacterial counts in liver, spleen, caecal content and faecal droppings

were determined using a standard plating method described previously [31]. For the purposes of statistical analysis, a viable count of log10 < 2.5 (limit for direct plate detection) obtained buy C59 from a sample positive only after enrichment was rated as log10 = 1.0 whereas samples negative for S. Enteritidis after enrichment were rated as log10 = 0. During the post mortem analysis, liver and caecal samples were also taken for histological examinations. The samples were fixed in 10% neutral buffered formalin for 24 h, embedded in paraffin wax, sectioned at 5 μm, and stained with haematoxylin-eosin. In the second animal infection, 3 mice per group, including 3 non-infected mice, were infected with the wild-type S. Enteritidis, or with ΔSPI2, lon or rfaL mutants. In this experiment, four-colour flow cytometry detecting CD3, CD19, CD14 and CD16 in splenic lymphocytes was performed.

Considering only predicted sites with scores above the numerically calculated cutoff score (7.95),

we were able to find 44 putative σ54-binding sites or σ54-dependent promoters that could potentially direct the transcription of a gene in the correct orientation. Their sequences with the associated genes or putative operons are summarized in Table 3. DNA sequence logo derived from these 44 predicted RpoN-binding sites shows two blocks of conserved sequences containing the highly frequent GG and GC dinucleotides (Figure 2), consistent with -24/-12-type promoters recognized by RpoN in most of bacterial groups [18]. Table 3 Predicted RpoN-binding sites in X. fastidios a genome. Gene ID Position* Sequence Score Product XF2542 -76 TGGCACACCTTCTGCT 12.38 fimbrial protein XF1354 -122 TGGTACGGTATTTGCT 11.58 MarR family transcriptional MG-132 mw RAD001 regulator XF0158 -127 CGGCACGTGTGTTGCT 11.32 hypothetical protein (XF0158-59-60) XF1842# -46 TGGTATGCCAATTGCT 10.52 glutamine synthetase XF0623 -246 TGGCACGGGAATTGAA 10.62 hypothetical protein XF0220 -129 TGGGATGGTTCTTGCT 10.46 proline dipeptidase XF0178 -177 TGGCATGCCAAATGCA 10.39 conserved hypothetical protein (XF0178-79) XF0414 -189 TGGCGAGCATCTTGCA 10.29 hypothetical protein (XF0414-15) XF1850 -7 CGGCACATGCGTTGCT 10.26 hypothetical protein (probable transposase)

XF1471 -230 CGGCACGGAATTCGCA 10.22 hypothetical protein XF1315 -116 AGGCACTGCGGTTGCA 10.10 hypothetical protein (XF1315-relA-XF1317-18) XF0746 -227 TGGCACTGCCAATGCA 9.93 hypothetical protein XF1121 -82 CGGCACGACCCCTGCC 9.42 5,10-methylenetetrahydrofolate reductase XF0010 -63 TGGTCCGGCCAGTGCA 9.36 biopolymer transport ExbB protein (exbB-exbD-exbD2-XF0013) XF0507 -213 CGGCGCGGGTTTCGCT 9.29 hypothetical protein (XF0507-08) XF1784 -151 TGGCACGTCAAGCGCA 9.26 hypothetical protein (ParB-like nuclease domain) (XF1784-83-82-81) XF1943

-342 CGGCACGCTGATGGCA 9.20 histone-like protein XF0305 -65 GGGCACCATATTTGCT 9.14 NADH dehydrogenase subunit A (nuoABCDEFGHIJKLMN) XF1249 -207 CGGCCCGCAGCATGCT 8.97 hypothetical protein XF1749 -27 TGGCGCGGCGTTTCCT 8.92 MFS transporter selleck products (XF1749-48-47-46) XF0290 -30 CGGCACTGCCACTGCA 8.90 aconitate hydratase XF2580 -109 CGGCACGGAGGCGGCA 8.81 30S ribosomal protein S2 XF2639 -43 TGGCGCGCCACTTTCT 8.79 preprotein translocase subunit SecE (secE-nusG) XF0177 -161 TGGCCTGCATTTGGCA 8.79 hypothetical protein XF2260 -305 TGGAACAGAAGGTGCT 8.75 alanyl dipeptidyl peptidase XF1213 -151 CGGCTCCCCTCTTGCT 8.74 GTP-binding elongation factor protein XF2724 -28 TGGCACAGTGCCAGCA 8.69 type I restriction-modification system (XF2724-23-22-21) XF2677 -164 GGGCGTGATGCTTGCA 8.65 L-ascorbate oxidase XF1609 -164 TGGCAGGTGTTGTGCT 8.60 MFS glucose/galactose transporter (XF1609-10-11) XF2745 -15 CGGCGTGGCCGGTGCA 8.59 hypothetical protein XF0695 -50 AGGCGCGCCGTTCGCA 8.59 hypothetical protein XF1355 -223 TGGCAGTGCCGGTGCA 8.

Cancer Res 2005,

65:10862–10871.PubMedCrossRef 63. Toda S, Uchihashi K, Aoki S, Sonoda E, Yamasaki F, Piao M, Ootani A, Yonemitsu N, Sugihara H: Adipose tissue-organotypic culture system as a promising model for studying adipose tissue biology and regeneration. Epigenetics Compound Library manufacturer Organogenesis 2009, 5:50–56.PubMedCrossRef 64. Sung SY, Chung LW: Prostate tumor-stroma interaction: molecular mechanisms and opportunities for therapeutic targeting. Differentiation 2002, 70:506–521.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions RR, VC and CM performed most of the experiments. MJO performed the zymography, assisted with the cell tracking experiment and edited the manuscript. MF assisted with some of the in vitro experiments and edited the manuscript. AF, PP, CL, FL, AM, VS, JSM, JO and FP collected adipose tissue and clinicopathologic patient information and edited the manuscript. RR and RM performed the statistical analysis. RR, CM, AMP, CL and RM designed the experiments and edited the manuscript. RR wrote the manuscript. All authors read and approved the final manuscript.”
“Background B Lymphocyte Stimulator (BLyS), a key member of the tumor necrosis factor superfamily, binds to three receptors: B-cell maturation antigen (BCMA),

transmembrane activator and CAML Autophagy Compound Library cost interactor (TACI), and B cell-activating factor receptor (BAFF-R). BLyS promotes survival of splenic immature transitional and mature B cells [1]. Over-expression of BLyS has been associated with multiple myeloma (MM) [2], Systemic lupus erythematosus (SLE) [3] and B cell lymphoma [4]. It has also been reported that this ligand/receptor dyad plays a critical role in the growth and survival of malignant plasma cells and B cells [5]. Recent studies in ductal breast cancer patients have learn more suggested a role of BLyS in the development of breast cancer. But its molecular

mechanisms remain to be elucidated [6]. Hypoxia plays a significant role in the pathogenesis of heart disease, cancer, neuron death, etc. [7]. Inflammatory factors have been shown to be transcriptional regulated by hypoxia induced factor-1α (HIF-1α) or NF-kappa B in hypoxic conditions [8]. The expression of BLyS is up-regulated by hypoxia, while the mechanism is still uncertain. We hypothesized that HIF-1α or NF-kappa B pathway might be responsible for the up-regulation. In addition, the inflammatory factors such as TNF-α, IL-1α lead to increased cancer cell migration [9]. Therefore, the human breast cancer cell migration in response to BLyS and possible molecular mechanisms were explored in this study.

This suggests that overfeeding on sugar results in body fat gains in contrast to consuming

a natural food comprised of unprocessed carbohydrate and fat. Furthermore, there may be no difference in overfeeding on fat or carbohydrate in terms of fat storage [13]. Presently, the effects of protein overfeeding in resistance-trained individuals is unknown. Therefore, the purpose of this investigation was to determine the effects of a high protein diet on body composition in resistance-trained men and women in the absence of changes in training volume. Methods Subjects Forty resistance-trained subjects volunteered for this investigation. Subjects were unequally randomized to a control (CON n = 10) or high selleckchem protein diet (HP n = 20) group. The purpose of unequal randomization was to take into account the loss of subjects from potential lack of compliance due to the high protein diet as well as gaining additional information on the treatment itself [14]. Participants were otherwise healthy resistance-trained men Y27632 and women who had been resistance training regularly for the last 8.9 ± 6.7 years and an average of 8.5 ± 3.3 hours per week. Individuals in the control group were instructed to maintain the same dietary and training habits over the course of the study. On the other hand, the subjects in the high

protein diet group were instructed to consume 4.4 grams of protein equal to 4.4 g/kg/d. All procedures involving human subjects were approved by Nova Southeastern University’s Human Subjects Institutional Review Board in accordance with the Helsinki Declaration, and written informed consent was obtained prior to participation.

Food diary, workout Log, body composition Subjects kept a daily diary of their food intake via a smartphone app (MyFitnessPal®). The use of mobile apps for diet self-monitoring have been previously used [15]. If they did not use the mobile app, subjects instead kept a paper diary and their daily food intake was measured via the Nutribase® program. In order to maintain a high protein diet, subjects consumed commercially available whey and casein protein powder (MusclePharm® and Adept Nutrition [Europa®]). Otherwise, the rest of their dietary protein was obtained from their normal food intake. Height was measured using standard anthropometry and total body weight was measured using a calibrated Montelukast Sodium scale. Body composition was assessed by whole body densitometry using air displacement via the Bod Pod® (COSMED USA, Concord, CA). All testing was performed in accordance with the manufacturer’s instructions. Briefly, subjects were tested while wearing only tight fitting clothing (swimsuit or undergarments) and an acrylic swim cap. The subjects wore the exact same clothing for all testing. Thoracic gas volume was estimated for all subjects using a predictive equation integral to the Bod Pod® software. The calculated value for body density used the Siri equation to estimate body composition.

After washing and blocking, the membranes were exposed in 1:2000-diluted serum for 1 h. The membranes were treated with 1:5000-diluted alkalinephosphatase-conjugated goat anti-human IgG (Jackson ImmunoResearch Laboratories, West Grove, PA). After incubation in a color development MAPK Inhibitor Library manufacturer solution containing 0.3 mg/ml of nitroblue tetrazolium chloride (Wako Pure Chemicals) and 0.15 mg/ml of 5-bromo-4-chloro-3-indolylphosphate (Wako Pure Chemicals), positive reactions were detected. Positive clones were re-cloned twice to obtain

monoclonality. Sequence analysis of identified clones Monoclonalized phage cDNA clones were converted to pBluescript phagemids through in vivo excision using ExAssist helper phage (Stratagene, La Jolla, CA). Plasmid DNA was obtained from an E. coli SOLR strain transformed by the phagemid. The inserted cDNAs were sequenced using the dideoxy chain termination method and the sequences were analyzed for homology with a public database GS-1101 price provided by the National Center for Biotechnology Information (NCBI). Production of glutathione S-transferase (GST) fusion proteins cDNA inserts of these clones incorporated in pBluescript were cleaved by EcoRI and XhoI generally and cloned into the EcoRI-XhoI site of pGEX-4 T-3, pGEX-4 T-2, and pGEX-4 T-1 vectors (Amersham Bioscience, Piscataway, NJ) that express recombinant

GST fusion proteins. E. coli JM109 cells containing pGEX clones (A600 = 0.3–0.5) were cultured in 200 ml of Luria broth (LB), and lysed through sonication. The lysate was then centrifuged and the

GST-fusion proteins in the supernatants were purified by glutathione-Sepharose. These samples were centrifuged and affinity-purified with glutathione-Sepharose. ELISA Purified recombinant proteins diluted at 10 μg protein/ml in PBS were added to each well of 96-well plates and incubated at room temperature overnight. As a control, the same amount of GST was applied. Sera diluted at 1:100 in PBS with 10% FBS were added to the wells and incubated for 1 h. The wells were exposed to 1:2 000-diluted horseradish peroxidase-conjugated goat anti-human IgG antibody (Jackson ImmunoResearch Laboratories, Amine dehydrogenase West Grove, PA). Then, 100 μl of a peroxidase substrate (o-phenylenediamine, 0.4 mg/ml) containing 0.02% (v/v) H2O2 were added. Absorbance at 490 nm was determined using a microplate reader (Emax, Molecular Devices, Sunnyvale, CA). Construction of SH3GL1 deletion mutants Some deletion constructs of SH3GL1 were obtained through digestion with restriction enzymes or the inverse PCR method. The SEREX-identified phage clone was containing a full-length coding sequence of SH3GL1 (1–368 amino acids), that comprised Bin-Amphiphysin-Rvs (BAR) domain (amino acid positions between 5 and 242) in the N-terminal portion, coiled-coil (CC) domain (amino acid proteins between 180 and 250) at the middle, and the SH3 domain (amino acid positions between 309 and 364) in the C-terminal portion.

This reporting bias is related to common method variance. One limitation was that the data on depression was based on self-reporting, which provides a range of depressive symptoms but not a depression diagnosis. Second, the bystanding to bullying

question was very general, and different types of bullying were not specified. Third, our bullying data were pooled from self-reporting. Validated instruments were used to measure depressive symptoms (HAD-scale). One limitation of the study was the very low number of women in the study and the still lower number of cases among women. Recommendations Our data suggests that frequent bystanding to bullying may be a warning Selleck Roxadustat sign for developing future symptoms of depression. Our study gives grounds for actively collecting information on bullying behavior as part of screening during health control AZD6244 in vitro in occupational health services. Moreover, bullying should be the focus of preventive work in the industry. In conclusion, the results support the notion that bullying is not only a dyadic target-bully issue to

be resolved. It has to be seen as a triadic relationship between bully, victim, and bystander and as a structural, organizational problem where many bystanders as well as targets suffer and are at risk of future health problems. Bystanders and the whole organization are involved in the process of bullying behavior, and, in turn, intervention programs should be focused on the whole workplace system. Acknowledgments We are grateful to the research and project groups in the AHA study who have been indispensable in the completion of the study. We acknowledge the financial support of AFA-Insurance, Stockholm, Sweden (AFA, the grant number: 110092). The authors declare that they have no conflict of interest. Open Access This article is distributed

under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided Ergoloid the original author(s) and the source are credited. References Agudelo-Suarez A, Gil-Gonzalez D, Ronda-Perez E, Porthe V, Paramio-Perez G, Garcia AM, Gari A (2009) Discrimination, work and health in immigrant populations in Spain. Soc Sci Med 68(10):1866–1874CrossRef Barling J (1996) The prediction, experience and consequences of workplace violence. In: VanderBos GR, Bulatoao EQ (eds) Violence on the job. American Psychological Association, Washington, pp 29–50 Beale D, Hoel H (2010) Workplace bullying, industrial relations and the challenge for management in Britain and Sweden. Eur J Ind Relat 16(2):101–118CrossRef Bergstrom G, Bjorklund C, Fried I, Lisspers J, Nathell L, Hermansson U et al (2008) A comprehensive workplace intervention and its outcome with regard to lifestyle, health and sick leave: the AHA study.

A third dose of the same beverage and volume was provided after the second blood draw. At the completion of the lifting session, participants rested quietly for 90 min. The third blood sample

was collected at the 90-min recovery point. Saliva and blood collection and analyses Unstimulated saliva was collected into sterile 15-ml centrifuge tubes at baseline, immediately after exercise, and at 90 min recovery. For collection, subjects were instructed to continually spit into the tubes over a timed 4 min period for a resting sample. Saliva volume was measured to the nearest Ridaforolimus datasheet 0.1 ml, and then the samples were frozen at −20°C for later analysis of IgA concentration, flow rate and osmolality. Salivary IgA concentrations were measured in triplicate (coefficient of variation (CV) = 3.1%) by enzyme linked immunosorbent (ELISA) assay. Briefly, microplates (Dynex Immulon-I) were coated with 100 μl of 2μg/ml goat anti-human IgA (Southern Biotech, #2050-01) and incubated overnight at 4°C. The following day, the plates were brought to room temperature, washed 3x with PBS (Cellgro) and blocked with 200 μl of SuperBlock (Pierce). Then the plates were washed 3x with PBS-Tween (Sigma). Saliva samples were thawed to room Nutlin-3a temperature, and then centrifuged at 1,500g for 10 min. The supernatant was diluted 1:500, added to the plates in 100 μl volumes

in triplicate, and incubated for 1 h at room temperature. The plates were then washed 3x with PBS-Tween (Sigma), following which 100 μl anti-human

IgA Horseradish Peroxidase (Southern Biotech, #2050-05) diluted 1:5,000 was added to the wells. The plates were again incubated for 1 h at room temperature. The plates were washed, and 100uL of substrate (Bio-Rad, #172-1067) was added to the wells. Following 30 min room temperature incubation, the plates were read on a Labsystems Multiskan MCC/340 microplate reader (Fisher Scientific, Pittsburgh, PA) at 630nm. Standards of known concentrations of purified IgA were assayed on each microplate, and absolute concentrations (μg·ml-1) were calculated from the standard curve. Saliva osmolality was measured in duplicate (CV = 1.3%) by a freezing point Sulfite dehydrogenase depression osmometer (Advanced Digimatic Osmometer, Advanced instruments, Needham MA). Blood samples were drawn at baseline, immediately post-exercise, and after 90 min of recovery. All three blood samples were drawn with the participants in a seated position. Vacutainers without additive (dry) were used for interleukin (IL)-2, IL-5 levels and serum cortisol levels. Vacutainers containing sodium fluoride potassium oxalate were used for plasma lactate levels. The blood samples for IL-2 and IL-5 were allowed to stand for 30 min after the blood draw, and then centrifuged for 10 min at 3,200 rpm. The resulting serum was frozen at −40°C and stored for later analysis.

Apaydin I, Konac E, Onen HI, Akbaba M, Tekin E, Ekmekci A: Single nucleotide polymorphisms in the hypoxia-inducible factor-1alpha (HIF-1alpha) gene in human sporadic breast cancer. Arch Med Res 2008, 39 (3) : 338–345.CrossRefPubMed 15. Kim HO, Jo YH, Lee J, Lee SS, Yoon GS-1101 molecular weight KS: The C1772T genetic polymorphism

in human HIF-1alpha gene associates with expression of HIF-1alpha protein in breast cancer. Oncol Rep 2008, 20 (5) : 1181–1187.PubMed 16. Horree N, Groot AJ, Van Hattem WA, Heintz AP, Vooijs M, Van Diest PJ: HIF-1A gene mutations associated with higher microvessel density in endometrial carcinomas. Histopathology 2008, 52 (5) : 637–639.CrossRefPubMed 17. Konac E, Onen HI, Metindir J, Alp E, Biri AA, Ekmekci A: An investigation of relationships between hypoxia-inducible factor-1 alpha gene polymorphisms

and ovarian, cervical and endometrial cancers. Cancer Detect Prev 2007, 31 (2) : 102–109.CrossRefPubMed 18. Fransen K, Fenech M, Fredrikson M, Dabrosin C, Soderkvist P: Association between ulcerative growth and hypoxia inducible factor-1 alpha polymorphisms in colorectal cancer patients. Mol Carcinog 2006, 45 (11) : 833–840.CrossRefPubMed 19. Kuwai T, Kitadai Y, Tanaka S, Kuroda T, Ochiumi T, Matsumura S, Oue N, Yasui W, Kaneyasu selleck inhibitor M, Tanimoto K, Nishiyama M, Chayama K: Single nucleotide polymorphism in the hypoxia-inducible factor-1alpha gene in colorectal carcinoma. Oncol Rep 2004, 12 (5) : 1033–1037.PubMed 20. Ollerenshaw M, Page T, Hammonds Avelestat (AZD9668) J, Demaine A: Polymorphisms in the hypoxia inducible factor-1alpha gene (HIF1A) are associated with the renal cell carcinoma phenotype. Cancer Genet Cytogenet 2004, 153 (2) : 122–126.CrossRefPubMed 21. Clifford SC, Astuti D, Hooper L, Maxwell PH, Ratcliffe PJ, Maher ER: The pVHL-associated SCF ubiquitin ligase complex: Molecular genetic analysis of elongin B and C, Rbx1 and HIF-1α in renal cell carcinoma. Oncogene 2001, 20: 5067–5074.CrossRefPubMed 22. Ling TS, Shi RH, Zhang GX, Zhu H, Yu LZ, Ding XF: Common single nucleotide polymorphism of hypoxia-inducible

factor-1 alpha and its impact on the clinicopathological features of esophageal squamous cell carcinoma. Chin J Dig Dis 2005, 6 (4) : 155–158.CrossRefPubMed 23. Thakkinstian A, McElduff P, D’Este C, Duffy D, Attia J: A method for meta-analysis of molecular association studies. Stat Med 2005, 24 (9) : 1291–1306.CrossRefPubMed 24. Egger M, Davey Smith G, Schneider M, Minder C: Bias in meta-analysis detected by a simples, graphical test. BMJ 1997, 315: 629–634.PubMed 25. Bax L, Yu LM, Ikeda N, Tsuruta H, Moons KGM: Development and validation of MIX: comprehensive free software for meta-analysis of causal research data. BMC Med Res Methodol 2006, 6: 50.CrossRefPubMed 26. Bax L, Yu LM, Ikeda N, Tsuruta H, Moons KGM: MIX: comprehensive free software for meta-analysis of causal research data. Version 1.7. [http://​mix-for-meta-analysis.​info] 2008. 27.

93 wt%,

which was much lower than that for the catalytic pyrolysis of L. japonica only (50.32 wt%). Co-pyrolysis also considerably increased the contents learn more of light hydrocarbons and mono-aromatics that have high economic values. The main hydrocarbon species obtained from the catalytic co-pyrolysis were gasoline-range (C5-C9) and diesel-range (C10-C17) species, whereas non-catalytic co-pyrolysis produced mainly wax species (C17 or larger). The production of these valuable species was attributed to the catalytic conversion of oxygenates, acids, and heavy hydrocarbons occurring on the acid sites inside the large pores of Al-SBA-15. Acknowledgement This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2012R1A1B3003394). References 1. Lee HY, Jeon JK, Park SH, Jeong KE, Chae HJ, Park YK: Catalytic pyrolysis of Laminaria japonica over nanoporous catalysts using Py-GC/MS. Nanoscale Res Lett 2011, 6:500. 10.1186/1556-276X-6-500CrossRef 2. Lee HY, Choi SJ, Park SH, Jeon JK, Jung SC, Joo SH, Park YK: Catalytic conversion of Laminaria japonica over beta-catenin mutation microporous zeolites. Energy 2014, 66:2–6.CrossRef 3. Jeon MJ, Jeon JK, Suh DJ, Park SH, Sa YJ, Joo SH, Park YK: Catalytic pyrolysis of biomass

components over mesoporous catalysts using Py-GC/MS. Catal Today 2013, 204:170–178.CrossRef 4. Wang P, Zhan S, Yu H, Xue X, Hong N: The effects of temperature and catalysts on the pyrolysis of industrial wastes (herb residue). Bioresour Technol 2010, 101:3236–3241. 10.1016/j.biortech.2009.12.082CrossRef 5. Park HJ, Heo HS,

Yoo KS, Yim JH, Sohn JM, Jeong KE, Jeon JK, Park YK: Thermal degradation of plywood with block polypropylene in TG and batch reactor system. J Ind Eng Chem 2011, 17:549–553. 10.1016/j.jiec.2010.11.002CrossRef 6. Ryu JS, Kim KS, Park SJ: A study on copyrolysis and heating value of wood chip composites as cogeneration plant fuel. J Ind Eng Chem 2012, Dapagliflozin 18:2024–2027. 10.1016/j.jiec.2012.05.022CrossRef 7. Miskolczi N: Co-pyrolysis of petroleum based waste HDPE, poly-lactic-acid biopolymer and organic waste. J Ind Eng Chem 2013, 19:1549–1559. 10.1016/j.jiec.2013.01.022CrossRef 8. Grieco EM, Baldi G: Pyrolysis of polyethylene mixed with paper and wood: Interaction effects on tar, char and gas yields. Waste Manage 2012, 32:833–839. 10.1016/j.wasman.2011.12.014CrossRef 9. Bernardo M, Lapa N, Gonçalves M, Menders B, Pinto F, Fonseca I, Lopes H: Physico-chemical properties of chars obtained in the co-pyrolysis of waste mixtures. J Hazard Mater 2012, 219–220:196–202.CrossRef 10. Zanella E, Zassa MD, Navarini L, Canu P: Low-temperature co-pyrolysis of polypropylene and coffee wastes to fuels. Energy Fuel 2013, 27:1357–1364. 10.1021/ef301305xCrossRef 11. Abnisa F, Wan Daud WMA, Ramalingam S, Azemi MNBM, Sahu JN: Co-pyrolysis of palm shell and polystyrene waste mixture to synthesis liquid fuel.