65 Ci/mmol), and [3H]-adenine ([3H]-Ade, 27.2 Ci/mmol) were purchased from PerkinElmer. [3H]-guanine ([3H]-Gua, 10.7 Ci/mmol) and [5-3H]-deoxyuridine 5’-monophosphate

([3H]-dUMP, 27 Ci/mmol) were from Moravek Biochemicals, Inc. The nucleoside and nucleobase analogs library [36] was kindly provided by Professor Pär Nordlund, from the Karolinska Institute, Stockholm, OSI906 Sweden. Phosphoribosyl pyrophosphate (PRPP), dipyridamole, tetracycline, Pexidartinib and nonradioactive Hx and Gua were from Sigma-Aldrich. Mpn culture, and the effects of nucleoside and nucleobase analogs on growth and metabolism Nucleoside and nucleobase analogs were dissolved in dimethyl sulfoxide (DMSO) as stock solutions and diluted with Mpn culture medium to the desired concentration immediately prior to use. The DMSO concentration in the final dilution was < 1%, which would not

interfere with Mpn growth. Mpn laboratory strain M129 wild type and a thyA mutant selleck inhibitor strain [31] were used in this study. Mpn was cultured at 37°C in a CO2 incubator using 75 cm2 tissue culture flasks containing 50 ml Hayflick’s medium, and harvested at day 4 when the medium color change was observed [49]. The cells were harvested and the pellet was resuspended in 6 ml fresh medium and the cfu/ml was determined by serial dilution (10-fold) and plating on broth agar plate. Colonies was counted and cfu/ml was calculated. Inhibition studies were performed in 96-well plates containing 200 μl Mpn culture (approximately

106 cfu ml-1) in Hayflick’s medium and 200 μl each compound in series dilutions (2-fold) with the growth medium, with three to four replicas. The plates were sealed with clear adhesive sheets and incubated at 37°C incubator. Absorbance ratio at 450 nm and 560 nm was used as Mpn growth index, which was measured daily, and by visual detection for at least 8 days, as previously described [32]. In the absence of inhibitor, the culture medium turned yellow on day 4. Controls were cultured in the presence of 2 μg/ml tetracycline, which showed no growth for up to 8 days. Medium was placed in four wells per plate for controls, which see more showed no color change during the incubation period. The MICs (minimal inhibitory concentration required to inhibit Mpn growth to 90%) were determined as the lowest concentration at which the growth index was ≈ 10% of the control values (at the time when the control culture medium color turned yellow), essentially as described [50]. Nucleoside and nucleobase uptake and metabolism was done with the wild type strain, which was cultured in 25 cm2 tissue culture flasks, inoculated with 1 ml stock culture (1 × 108 cfu/ml) Mpn, in the presence of tritium labeled dT, Hx, Gua, Ade or Ura (1 μCi ml-1) and the presence or absence of nucleoside and nucleobase analogs (10 μM) and incubated at 37°C for 70 hours. The cells were harvested and analyzed essentially as described [31].

Bioinformatics 2009, 25:1754–1760.PubMedCrossRef 48. Mortazavi A, Williams BA, McCue K, Schaeffer L, Wold B: Mapping and quantifying mammalian transcriptomes Trichostatin A in vivo by Alvocidib cost RNA-Seq. Nat Methods 2008, 5:621–628.PubMedCrossRef 49. Saeed AI, Sharov V, White J, Li J, Liang W, Bhagabati N, Braisted J, Klapa M, Currier T, Thiagarajan M, Sturn A, Snuffin M,

Rezantsev A, Popov D, Ryltsov A, Kostukovich E, Borisovsky I, Liu Z, Vinsavich A, Trush V, Quackenbush J: TM4: a free, open-source system for microarray data management and analysis. Biotechniques 2003, 34:374–378.PubMed 50. Schäfer A, Tauch A, Jäger W, Kalinowski J, Thierbach G, Pühler A: Small mobilizable multi-purpose cloning vectors derived from the Escherichia coli plasmids pK18 and pK19: selection of defined

deletions in the chromosome of Corynebacterium glutamicum . Gene 1994, 145:69–73.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions RS carried out the experiments and data analyses, and wrote the manuscript. KC participated in the sample preparation and preliminary examination. YS carried out RNA-sequencing. IO and SN participated in the design and coordination of the study. TF designed the experiments and participated in the data processing and manuscript preparation. All authors read and approved the manuscript.”
“Background The best-studied asymmetrically dividing prokaryote is the alphaproteobacterium Caulobacter crescentus. At each cell division, predivisional cells of C. crescentus localize different structures at the cell poles: a single flagellum see more occupies the pole that will be inherited Palmatine by the swarmer cell and pili are synthesized at this pole after division, whereas a narrow extension of the cell envelope (the stalk) tipped by an adhesive structure (the holdfast) occupies the opposite pole that

will give rise to the stalked cell. The stalked cell is able to restart the cell cycle immediately after division, whereas the swarmer cell is unable to initiate DNA replication until it differentiates into a stalked cell. The C. crescentus cell cycle and developmental program are controlled by three master regulators: CtrA, GcrA, and DnaA (for review, see [1]). These proteins are regulated such that each one reaches maximal abundance during a different stage of the cell cycle. DnaA reaches peak abundance at initiation of DNA replication occurring in stalked cells, GcrA peaks after DNA replication in early predivisional cells, and CtrA peaks in late predivisional and swarmer stages [2]. All three proteins are required for regulating transcription of different suites of genes. DnaA activates genes involved in chromosome partitioning, nucleotide biosynthesis, and DNA replication, recombination and repair [3], and initiates replication of the chromosome. DnaA is also required for transcription of gcrA[3].

GAG is commonly found in natural non-K12 E. coli isolates [19, 20]. Mutations

in rpoS have also been identified in Shiga-like toxin-producing E. coli strains [21]. Polymorphism of rpoS appears to be paradoxical to the central role that RpoS plays in survival. Mutants of rpoS can be selected under learn more nutrient limitation and exhibit enhanced metabolic potential [22], suggesting a regulatory trade-off for fitness between CFTRinh-172 datasheet stress resistance and nutrient scavenging [22]. Growth on weak acids, including succinate [23] and acetate [24], strongly selects for mutations in rpoS in laboratory E. coli strains [23]. Considering that the weak acid (e.g., acetate) concentration is relatively high in human colon (80 mM) where E. coli colonize [25, 26], E. coli may face a similar selective pressure within the host environment. Selection for loss and gain of RpoS function may be an important adaptive mechanism, like phase variation, to ensure that E. coli can survive in complex natural environments. However, whether this selection is responsible for the observed rpoS polymorphism in natural E. coli isolates remains unclear, primarily because most studies have been

done with laboratory E. coli K12 strains. The genomes of E. coli isolates differ substantially and constitute a pangenome consisting of 13,000 genes, of which 2,200 genes are check details conserved among all isolates [27]. Since RpoS mostly controls expression of genes encoding non-essential functions [8, 9, 12, 13], RpoS likely plays a considerable role in the expression of non-conserved genes in the pangenome. Given that E. coli K12 strains only possess about 1/3 of all genes found in the pangenome of E. coli [27], it is possible that rpoS selection is limited to laboratory strains. Interestingly, selection for rpoS could

not be observed in a natural E. coli isolate ECOR10 under nutrient limitation (see Fig 5 in [22]). In this study, we wished to address three outstanding questions. First, can rpoS mutants be selected in clinical strains isolated from natural environments? Of particular interest is whether this selection occurs in pathogenic strains, which may have important medical relevance because of the potential role of RpoS in bacterial pathogenesis. Second, are there other PTK6 factors involved in the selection for enhanced metabolic abilities in natural strains? Finally, is there any evidence that this selection occurs in natural environments? To address these questions, we employed a succinate selection strategy as a tool [23] and examined the selection using a group of ten representative verocytotoxin-producing E. coli (VTEC) strains from all five identified seropathotypes as our model strains. VTEC strains, including the O157:H7 serotype, are responsible for most E. coli foodborne outbreaks and can cause severe diseases, including diarrhea, hemorrhagic colitis and the hemolytic uremic syndrome [28].

The clone library analysis showed consistent decrease in the Firmicutes and consistent increase in Bacteroidetes in both the families with an increase in age (Figure  2). The family level variation in

microflora in individuals is shown in Additional file 1: Table S1. The genera which were dominant in the individual samples are represented in Figure  3. The heat map represented in Figure  3 shows that the individuals within a same family cluster together when genus level distribution of gut flora is considered. Within family T, Fecalibacterium and Roseburia dominated in subject T1 (age 14) Dialister, Prevotella dominated in subject T2 (age 42) and Prevotella in subject T3 (age 62). Within family S the genus Streptococcus and Weissella dominated in the JAK inhibitor infant and Fecalibacterium and Roseburia dominated in adult subjects (age 26 and 62 years respectively). The phylogenetic tree of the OTU’s obtained from all the subjects are represented in Additional files 2: Figures S1, Additional file 3: Figures S2, Additional file 4: Figure S3, Additional file

5: Figure S4, Additional file 6: Figure S5, Additional file 7: Figure S6. The phylogenetic trees consist of clades representing the presence of potential novel bacterial species in the gut flora of the subjects. Figure 2 Phylum level comparison of gut flora of the subjects . The Selleck TH-302 stacked bars describe the percent distribution of each phylum across the subjects. Figure Docetaxel cost 3 Genus level comparison of gut flora . The heat map represents clustering of bacterial communities across the subjects at the genus level. Family S: S1 (26 years), S2 (8 months), S3 (56 years) and Family T: T1 (14 years), T2 (42 years), T3 (62 years). Real time PCR The slopes for the standards for all the genus specific primers were in the range of −3.1019 to −3.460 with the R2 value >0.99. The PCR efficiency ranged from 96% to 106%. The qPCR quantification

confirmed that the Firmicutes number is decreasing and Bacteroidetes number is increasing with increasing age. The pattern of change in Firmicutes/Bacteroidetes ratio with age within a Family is represented in Figure  4. The copy numbers of PD0325901 supplier different genera are represented in Table  3. The copy number of Roseburia was more than Clostridium and Lactobacillus group, suggesting dominance of Roseburia in the gut flora, which is consistent with the report by Arumugam et al. showing that Fecalibacterium and Roseburia are the dominant genera in the gut flora [35]. Figure 4 Firmicutes to Bacteroidetes ratio by qPCR, A- The pattern of change in Firmicutes/ Bacteroidetes in family S and B- The pattern of change in Firmicutes/ Bacteroidetes in family T. Table 3 Copy numbers of different genera in the gut flora of individual samples Subjects S2 (8 months) S1 (26 yrs) S3 (56 yrs) T1 (14 yrs) T2 (42 yrs) T3 (62 yrs) ClEub 2.17 ± 0.9 E + 07 1.91 ± 0.01E + 08 7.85 ± 0.06E + 03 1.08 ± 0.01E + 09 2.19 ± 0.1E + 08 1.17 ± 0.01E + 08 Prev 7.83 ± 0.9 E + 07 3.55 ± 0.4E + 07 1.

strain JR [30]. In some instances G+ have been seen to dominate populations in mixed culture MFCs [30, 31]. Hence, while G+ have some capacity for electron transfer, it is apparent that the G- used here generated

much greater CB-839 nmr current in our MFC conditions. Interestingly, the current generated by P. aeruginosa in batch mode was larger than in continuous mode which may be concomitant with the gradual loss of redox shuttles AZD3965 nmr previously implicated in electron transfer by P. aeruginosa [10]. P. aeruginosa as a pure culture decreased its current production after the 48 hour timepoint (Figure 4) in continuous mode, however, in batch mode it continued to increase current. Potentially, a gradual wash-out 4-Hydroxytamoxifen nmr of redox shuttles, which can be produced by P. aeruginosa, explains the lower performance in continuous mode [32]. A comprehensive, non-MFC based study using PA01 to investigate phenotypic differentiation and seeding dispersal also

noted a halt in biofilm height after about 48 hours [33]. During that study microcolonies of 80 μm diameter became differentiated, leaving the microcolony hollow by day 3. Similarly to our current study, by 48 hours PAO1 had formed 20 ± 4 μm thick biofilms, which did not increase throughout the duration of the experiment. Although the aforementioned study used different parameters, the growth and retardation of the PA01 biofilms coincided with the timing of the assumed decreased EET activity

in our MFC. Co-culture versus pure culture current generation The three co-cultures (with E. faecium) used in this study all generated more current together then when grown as pure cultures. Although this has not yet been investigated at a deeper level, several studies have noted the coexistence between G+ and G- within the MFC environment. For example, the role of a phenazine electron shuttle has been verified in an earlier MFC study where it was observed to increase current generation in co-cultures of Brevibacillus sp. and Enterococcus sp. with Pseudomonas sp. These for studies determined that the G+ were able to use electron shuttles (mediators) produced by Pseudomonas sp [10, 28], the combination of both bacteria being the more successful one. Whether other mechanisms such as quorum regulation or the establishment of a syntrophic association is in play is yet to be investigated. In a recent study, Nevin et al., [20] described how pure culture biofilms of G. sulfurreducens were able to reach current densities of the same order of magnitude as mixed population current densities. In the latter case, the anode surface was minimized in order to ensure that the anode became the limiting factor.

The conserved carbon transfer of the underlying reactions selleck compound yields a specific labelling pattern for oxaloacetate formed by each pathway which is presented in this figure. White circles represent 12C whereas black circles indicate labelled 13C. The numbers given reflect the position of

the carbon atom within the molecule. AcCoA: acetyl-Coenzyme A; EDP: Entner-Doudoroff pathway; OAA: oxaloacetate; PYR: pyruvate; TCA: tricarboxylic acid. Conclusion Being one of the first metabolic studies of members of the Roseobacter clade using the 13C labelling experimental approach, a deeper insight into the activity of the important metabolic routes of D. shibae and P. gallaeciensis was achieved. Interestingly, the use of intracellular pathways is highly similar in the studied species D. shibae and Selleck FRAX597 P. gallaeciensis. This stands in surprising contrast to the overall differences in phenotypic behaviour exhibited by these two strains, since D. shibae is an algal-associated microorganism whereas P. gallaeciensis is free-living in marine habitats. However, this may be a first indication of more general key properties among members of the Roseobacter clade that explain their enormous success in the marine realm. Methods Strains, medium and growth conditions The strains used in this study are the genome sequenced

strains Dinoroseobacter shibae DFL12 [1] and Phaeobacter gallaeciensis DSM 17395 [14]. For cultivation of both strains a defined, synthetic seawater medium (minimal medium) was used [25], containing

the following selleck inhibitor components per litre of medium: 4.0 g NaSO4, 0.2 g KH2PO4, 0.25 g NH4Cl, 20.0 g NaCl, 3.0 g MgCl2·6 H2O, 0.5 g KCl and 0.15 g CaCl2·2 H2O, 0.19 g NaHCO3, 1 ml trace element solution and 10 ml vitamin solution. The final glucose concentration in the medium was in the range of 0.4 to 0.9 g l-1. The trace element solution contained 2.1 g Fe(SO4)·7 H2O, 13 ml 25% (v/v) HCl, 5.2 g Na2EDTA·2 H2O, 30 mg H3BO3, 0.1 g MnCl2·4 H2O, 0.19 g CoCl2·6 H2O, 2 mg CuCl2·2 H2O, 0.144 g ZnSO4·7 H2O and 36 mg Na2MoO4·2 Ureohydrolase H2O per litre. The vitamin solution for D. shibae contained the following components per litre: 0.2 g biotin, 2.0 g nicotinic acid and 0.8 g 4-aminobenzoic acid. All solutions were sterilised separately and mixed at room temperature prior to inoculation. For carbon labelling experiments 99% [1-13C] glucose (Euriso-Top, Saint-Aubin, France) was used as substrate. The cultivations were carried out on orbital shakers at 200 rpm in 500 ml shaken flasks with a culture volume of 50 ml at 37°C (D. shibae) and 28°C (P. gallaeciensis). To ensure comparable conditions between the two microorganisms and avoid any potential influencing effects of phototrophy in D. shibae, both organisms were cultivated in the light. Under these conditions, no bacteriochlorophyll is synthesised D.

Nat Genet 2001, 28: 53–57.CrossRefPubMed 33. Cha MY, Kim CM, Park YM, Ryu WS: Hepatitis B virus X protein is essential for the activation of Wnt/beta-catenin signaling in hepatoma cells. Hepatology 2004, 39: 1683–1693.CrossRefPubMed 34. Ding Q, Xia W, Liu JC, Yang JY, Lee DF, Xia J, Bartholomeusz G, Li Y, Pan Y, Li Z, et al.: Erk associates with and primes GSK-3beta for its inactivation resulting in upregulation of beta-catenin. Mol Cell 2005, 19: 159–170.CrossRefPubMed 35. Shtutman M, Zhurinsky J, Simcha I, Albanese C, Amico M, Pestell R, Ben Z, ev A: The cyclin D1 gene MLN8237 in vitro is a target of the beta-catenin/LEF-1 pathway. Proc Natl Acad Sci USA 1999, 96: 5522–5527.CrossRefPubMed

36. Tetsu O, McCormick F: Beta-catenin regulates expression of cyclin D1 in colon carcinoma cells. Nature 1999, 398: 422–426.CrossRefPubMed 37. Kawate S, Fukusato T, Ohwada S, Watanuki A, Morishita Y: Amplification of c-myc in hepatocellular carcinoma: correlation with clinicopathologic features, proliferative activity and p53 overexpression. Oncology 1999, 57: 157–163.CrossRefPubMed Competing interests selleck chemicals llc The authors SIS3 ic50 declare that they have no competing interests. Authors’ contributions XT carried out molecular studies, collected and analyzed the data, performed the statistical analysis and drafted the manuscript. JL carried out IHC studies.

MZM and CZ carried out part of real-time PCR studies. WDF collected the samples and participated in the design of the study. YMW designed the concept of this study and approved the final manuscript. All authors read and approved the final manuscript.”
“Background Nowadays breast cancer is becoming Montelukast Sodium the second leading cause of cancer deaths in females, almost 10% women have the

risk of developing breast cancer [1]. Although great improvements have been made in curing breast cancer, the overall five-year survival rate remains < 50% and many patients relapse after surgical resection because of the dispersion of undetectable cancer cells [2, 3]. Therefore, it is necessary to establish sensitive and specific techniques for the detection of occult tumor cells. A better method for early diagnosis may help in predicting recurrence and planning appropriate therapies to improve survival [4, 5]. Many investigations have indicated that epithelial cells from the initial tumor can be recognized in peripheral blood or bone marrow aspirates of patients with breast cancer [6, 7]. The detection of circulating tumor cells (CTCs) in the peripheral blood of cancer patients has been associated with recurrence and metastasis of breast cancer [8–10]. Cytokeratins (CKs), characteristic intermediate filament of epithelial cells, especially CK19, are widely used to detect tumor cells derived from epithelial tissues [11, 12].

At the time of our first report, we hypothesized that SSCMKI was needed for the phosphorylation of proteins involved in the regulation of the cell see more cycle and/or for the phosphorylation and activation of transcription factors needed

for the dimorphic transitions of the fungus. However, we mentioned that the final interpretation of our results awaited the identification of the interacting partners of SSCMKI that was also accomplished in this work. Important information related to the role of SSCMK1 in S. schenckii, was obtained with the yeast two-hybrid assay. Among the many proteins identified as interacting with SSCMK1 we identified a S. schenckii homologue of HSP90. This interaction was corroborated with Co-IP. It is a well-known fact that all organisms from bacteria to higher eukaryotes respond to elevated temperatures

by producing heat shock proteins. Two important observations Selleck VS-4718 CP673451 clinical trial regarding a connection between the heat shock response and CaMKs have been reported. In C. albicans, this kinase was shown to have a role in the capacity of fungal cells to grow at elevated temperature [48] and in Arabidopsis thaliana, CaMK-3 has been observed to be part of the heat shock response, possibly by the phosphorylation of the heat shock response factor and the induction of the transcription of the heat shock proteins [49]. In tomato (Solanum lycopersicum), LeCPK2, a CaMK, is up regulated in response to heat stress [50]. Heat shock proteins are a widespread family of molecular chaperones found in bacteria and all eukaryotic organisms. These chaperones

ensure both the folding of newly synthesized proteins and their refolding under denaturing stress conditions [51]. HSP90 has been reported to interact with protein kinases. Specifically during the cell cycle, HSP90 has been reported to intervene, together with cdc37, in the stabilization of the monomeric cdk4, prior to its interaction with cyclin D [16]. It has also been reported to interact with the protein phosphatase, calcineurin that dephosphorylates CaMKs [52, 53]. The interaction of HSP90 with protein kinases occurs at the N terminal domain of the HSP and two hypotheses has been postulated regarding the role of this HSP in the activity of protein kinases. HSP90 could facilitate the activation of the protein kinases by the induction of a conformational change Loperamide in these kinases or could maintain the phosphorylated kinases sequestered until needed [52]. Nevertheless, SSCMK1 binds to the C terminal domain of SSHSP 90 where effectors of this heat shock protein interact. This domain starts with amino acid D621 in the human homologue of HSP90. This suggests that instead of HSP90 regulating SSCMK1, the kinase could in some form or another be regulating HSP90. If this were correct, lowering the levels of SSCMK1 would affect the function of HSP90 and in turn render the cells intolerant to high temperatures as was observed by us.

MMPs contribute to this metastatic process by degrading basement membrane. In addition, MMPs can, due to their proteolytic activities, promote tumor growth by increasing the bioavailabilities of growth factors in the ECM [11]. Furthermore, it is becoming

increasingly clear that MMPs play a central role in ECM degradation [13]. Among MMPs, MMP-2 (gelatinase A) and MMP-9 (gelatinase B), are present in large quantities in cancer tissues [14, 15], and accumulating evidence indicates that MMP-2 and MMP-9 play critical role during tumor invasion and metastasis [14, 16–20]. Furthermore, Matrix metalloproteinases (MMPs) and their endogenous inhibitors participate in the invasive process of human osteosarcoma [21]. Bisphosphonates (BPs) are stable analogues of pyrophosphonate, GSK1210151A supplier and are potent inhibitors of osteoclast-mediated bone resorption. They are widely used to treat metabolic bone diseases, such as, Paget’s disease [22] and hypercalcemia [23] and to treat postmenopausal osteoporosis [24]. Recently, it was reported that BPs may significantly help control the pain associated with bone tumors [25]. Preclinical evidence suggest that BPs have direct antitumor effects on a variety of human cancer cells [26], and it is known that they

decrease cell proliferation in human osteosarcoma cell line panels, disturb the cell cycle, and PND-1186 induce the apoptosis of SaOS-2 cells [27, 28]. These findings suggest that BPs could play a beneficial Ribonucleotide reductase adjuvant role in the treatment of osteosarcoma. However, the inhibitory effects of BPs on osteosarcoma cell have not been Tanespimycin comprehensively studied, and therefore, in the present study, we examined the effects of the third-generation BPs, risedronate, on osteosarcoma cell invasion. Methods Reagents Risedronate [1-hydroxy-2-(3-pyridinyl)ethylidene]bis [phosphonic acid] was purchased from (Sanofi-Aventis, Korea). A stock solution of risedronate was prepared in phosphate-buffer saline (PBS). All other chemicals and reagents

used were of analytical grade. Cell Culture SaOS-2 and U2OS were purchased from the Korean Cell Line Bank (KCLB). Cells were cultivated in Dulbecco’s Minimum Essential Medium (DMEM) supplemented with 10% heat-inactivated fetal bovine serum (Gibco BRL, Grand Island, NY). Cultures were maintained at 37°C in a 5% CO2/95% air atmosphere. The medium was changed every 2–3 days, and cells were passaged twice a week. Risedronate treatment of SaOS-2 and U2OS cells SaOS-2 and U2OS cells were seeded in 6-well plates at a density of 2 × 105cells/well in DMEM/10% FBS overnight. The cells were then washed and treated with different concentrations of risedronate (0, 0.1, 1, 10 μM) for 48-h at 37°C in 5% CO2. Conditioned media were then collected and cells were harvested. MTT cell viability assay SaOS-2 and U2OS cells were seeded onto a 96-well culture plate at a density of 1 × 104 cells/well in 100 μl of complete DMEM.

We know CP673451 datasheet that clinical experience about one patient can change the world of medical science,

and therefore it is still important to publish case reports. For that reason, we have now decided to launch a new journal, the International Cancer Conference Peptide 17 journal (ICCJ), to accept excellent case reports, thereby contributing to clinical education and discussion. This is a unique, online journal, providing benefits such as quick review and publication, along with free color presentation of figures and videos. Additionally, in the future, readers will be able to participate in the discussions through letters and commentary in the journal’s cancer board conferences. On behalf of the Japan Society of Clinical Oncology, we sincerely look forward to your submission of cancer case reports and other contributions to the International Cancer Conference Journal (ICCJ). Journal title: International Cancer Conference Journal Editor-in-chief: Yoshiharu Sakai, MD Published format: Electronic online edition only Frequency of publication: 4 times per year (issued quarterly) Contents: Clinical Reviews or Cancer Board

Conferences, 1 or 2 per issue; Case Reports, approximately 10 per issue Initial publication: January 2012 Submission and publication cost: Free of charge, including color pages Submission guidance: Use this website the online system Editorial Manager starting in May 2011 [Inquiries] c/o Invention Center of the Kinki Districts (Kinki Chiho Hatsumei ID-8 Center), 14 Yoshidakawaramachi, Sakyo-ku, Kyoto 606-8305, Japan Fax +81-75-761-9724 E-mail: [email protected] International Journal of Clinical Oncology Editor-in-Chief Ikuo Konishi, MD”
“Background Antimicrobial resistance is an increasing challenge

of global proportions [1]. Special emphasis has been put on Gram negative bacteria producing enzymes conferring resistance against beta lactam antibiotics, such as third and fourth generation cephalosporins, monobactams and carbapenems, commonly known as extended spectrum beta-lactamases (ESBLs) [2-4]. ESBLs are associated with higher morbidity and mortality, rising health care costs [5], potential for foodborne transmission [6,7] and asymptomatic carriage [8]. ESBL-producing bacteria most often reside in the intestine of humans and animals, and may thus be difficult to control and eradicate [9,10]. Plasmid mediated ESBL genes can be transferred between different strains of bacteria and between different bacterial species and genera within the Enterobacteriaceae family [11]. Co-resistance to other groups of antibiotics is frequently observed in ESBL-producing organisms, which makes the choice of effective treatment even more limited [12]. In the Nordic countries, recent studies state that the main risk factor for acquiring ESBL-producing bacteria is travel abroad [13-15]. Asymptomatic infections with Salmonella and Shigella do occur [16,17]. When screening for fecal carriage of ESBL, the methods must ensure reliable detection also of these bacterial species.