Cummings SR, Black DM, Thompson DE et al (1998) Effect of alendronate on risk of fracture in women with low bone density but without vertebral fractures: see more results from the Fracture Intervention Trial. Jama 280:2077–2082PubMedCrossRef 177. Harris ST, Watts NB, Genant HK et al (1999) Effects of risedronate treatment on vertebral and nonvertebral fractures in women with postmenopausal osteoporosis:

a randomized controlled trial. Vertebral Efficacy With Risedronate Therapy (VERT) Study Group. JAMA 282:1344–1352PubMedCrossRef 178. Reginster AG-120 J, Minne HW, Sorensen OH et al (2000) Randomized trial of the effects of risedronate on vertebral fractures in women with established postmenopausal osteoporosis. Vertebral Efficacy with Risedronate Therapy (VERT) Study Group. Osteoporos Int 11:83–91PubMedCrossRef 179. Chesnut IC, Skag A, Christiansen C et al (2004) Effects of oral ibandronate administered daily or intermittently on fracture risk in postmenopausal osteoporosis. J Bone Miner Res 19:1241–1249CrossRef 180. Delmas PD, Recker RR, Chesnut CH 3rd, Skag A, Stakkestad JA, Emkey R, Gilbride J, Schimmer RC, Christiansen C (2004) Daily

and intermittent oral ibandronate normalize bone turnover and provide significant reduction in vertebral fracture risk: results from the BONE study. Osteoporos Int 15:792–798PubMedCrossRef 181. Harris ST, Blumentals WA, Miller PD (2008) Ibandronate and the risk of non-vertebral and clinical fractures in women with postmenopausal osteoporosis: results of a meta-analysis of phase III studies. Curr Med Res Opin 24:237–245PubMedCrossRef 182. Reginster JY, Adami S, Lakatos P et KPT-8602 al (2006) Efficacy and tolerability of once-monthly oral ibandronate before in postmenopausal osteoporosis: 2 year results from the MOBILE

study. Ann Rheum Dis 65:654–661PubMedCrossRef 183. Delmas PD, Adami S, Strugala C et al (2006) Intravenous ibandronate injections in postmenopausal women with osteoporosis: one-year results from the dosing intravenous administration study. Arthritis Rheum 54:1838–1846PubMedCrossRef 184. Reid IR, Brown JP, Burckhardt P et al (2002) Intravenous zoledronic acid in postmenopausal women with low bone mineral density. N Engl J Med 346:653–661PubMedCrossRef 185. Black DM, Delmas PD, Eastell R, Reid IR, Boonen S, Cauley JA et al (2007) Once-yearly zoledronic acid for treatment of postmenopausal osteoporosis. N Engl J Med. 356:1809–1822PubMedCrossRef 186. Lyles KW, Colon-Emeric CS, Magaziner JS et al (2007) Zoledronic acid and clinical fractures and mortality after hip fracture. New Engl J Med 357:1–11CrossRef 187. Rizzoli R, Reginster JY, Boonen S, Breart G, Diez-Perez A, Felsenberg D, Kaufman JM, Kanis JA, Cooper C (2011) Adverse reactions and drug-drug interactions in the management of women with postmenopausal osteoporosis. Calcif Tissue Int 89:91–104PubMedCrossRef 188. Pazianas M, Compston J, Huang CL (2010) Atrial fibrillation and bisphosphonate therapy.

Moreover, the migration of cells treated with both MTA1 shRNA and miR-125b inhibitor was similar to control cells (Figure  2A). Similar results were observed for the migration of SPC-A-1 cells (Figure  2B). These data demonstrate that MTA1 promotes while miR-125b inhibits NSCLC cell migration and indicate that MTA1 may promote cell migration via the downregulation of miR-125b. Figure 2 MTA1 and miR-125b have antagonistic effects on the migration of NSCLC cells. A. Wound healing assay on the migration of 95D cells transfected with MTA1 shRNA or control shRNA, together with miR-125b inhibitor or control. The percentage of the wound healing was calculated as (the width of wound at

0 h – the width of wound at 36 h)/ the width of wound at 0 h. **P < 0.01 compared to controls. B. Wound healing assay on the migration of SPC-A-1 cells transfected with MTA1 shRNA or control shRNA, together with miR-125b inhibitor or control. The percentage of the

wound healing #Selleckchem Alvespimycin randurls[1|1|,|CHEM1|]# was calculated as (the width of wound at 0 h – the width of wound at 48 h)/ the width of wound at 0 h. *P < 0.05, **P < 0.01 compared to controls. Matrigel invasion assay showed that in 95D cells, knockdown of MTA1 led to reduced cell invasion. However, cell invasion was increased in 95D cells treated with miR-125b inhibitor. Moreover, the invasion of cells treated with both MTA1 shRNA and miR-125b inhibitor was similar to control cells (Figure  3A). Similar results were observed for the invasion of SPC-A-1 cells (Figure  3B). These data demonstrate that MTA1 promotes while miR-125b inhibits

NSCLC cell selleckchem invasion and indicate that MTA1 may promote cell invasion via the downregulation of miR-125b. Figure Inositol monophosphatase 1 3 MTA1 and miR-125b have antagonistic effects on the invasion of NSCLC cells. A. Transwell invasion assay on the invasion of 95D cells transfected with MTA1 shRNA or control shRNA, together with miR-125b inhibitor or control. The invaded cells were counted from 5 random fields at 40x magnification. *P < 0.05, **P < 0.01 compared to controls. B. Transwell invasion assay on the invasion of SPC-A-1 cells transfected with MTA1 shRNA or control shRNA, together with miR-125b inhibitor or control. The invaded cells were counted from 5 random fields at 40x magnification. **P < 0.01 compared to controls. Discussion Recent studies have demonstrated the crucial role of miR-125b in tumorigenesis and metastasis [17–20]. Nevertheless, the role of miR-125b in lung cancer remains controversial. chr11q23-24 and chr21q11-21 are the region in which miR-125b-1 and miR-125b-2 are located, respectively, and they are frequently deleted in patients with lung cancer, indicating that miR-125b may function as a tumor suppressor in lung cancer [8, 21]. However, miR-125b exhibited higher expression level in non-responsive patients with cisplatin-based chemotherapy [22]. Furthermore, the high level of miR-125b was significantly correlated with poor patient survival [22, 23].

5-20 μM). We determined the cell survival rate, which was defined as the ratio of the number of living cells after 24, 48, and 72 h of incubation selleck with 1, 2.5, 5, 10 μM mevastatin, 1, 2.5, 5, and 10 μM fluvastatin or 2.5, 5, 10, and 20 μM simvastatin to the number of living cells in the control (0.1% DMSO-treated) samples. The survival rates on exposure to 1, 2.5, 5, and 10 μM of mevastatin were 81.44%, 58.41%, 31.81%, and 16.93%, respectively, at 72 h (Figure 2A). Thus, the number of U251MG cells significantly decreased at 72 h after the administration of 5 and 10 μM mevastatin. The survival rates on exposure to 1, 2.5, 5, and 10 μM of fluvastatin were 63.37%, 53.71%, 25.45%, and 24.08%, respectively,

at 72 h (Figure 2B). Thus, the

number of U251MG cells significantly decreased at 72 h after the administration of 5 and 10 μM fluvastatin. The survival rates on exposure to 2.5, 5, 10, and 20 μM of simvastatin were 65.57%, 57.59%, 25.11%, and 21.87%, respectively, at 72 h (Figure 2C). Thus, the number of U251MG cells significantly decreased at 72 h after the administration of 10 and 20 μM simvastatin. Figure 2 Effects of statins on U251MG cell viability. U251MG cells were treated check details with various concentrations of statins and trypan blue exclusion test was performed after 24, 48, or 72 h. The results are representative of 5 independent experiments. *p < 0.01 vs. controls (ANOVA with Dunnett's test). Statins-mediated activation of caspase-3 The cytotoxic effects of statins on C6 glioma cells were attributed to the induction of apoptosis, as demonstrated by the results of the following biochemical assays. We investigated the involvement of statins in caspase-3 activation. Caspase-3 activity was measured at 24 h after the addition of 5 μM mevastatin, 5 μM fluvastatin,

10 μM simvastatin to the tuclazepam C6 glioma cells. We observed that the addition of statins resulted in a Bucladesine purchase marked increase in caspase-3 activity in comparison with that in the control (0.1% DMSO-treated cells) (Figure 3A). Figure 3 Inhibition of statin-induced apoptosis in C6 glioma cells by intermediates of the mevalonate pathway. (A) Induction of caspase-3-like activity associated with statin-induced cell death. Caspase-3 activity is expressed as pM of proteolytic cleavage of the caspase-3 substrate Asp-Glu-Val-Asp-7-Amino-4-trifluoromethylcoumarin (DEVD-AFC) per h per mg of protein. The results are representative of 5 independent experiments. *p < 0.01 vs. controls (ANOVA with Dunnett’s test). (B-D) C6 glioma cells were pretreated with 1 mM mevalonic acid lactone (MVA), 10 μM farnesyl pyrophosphate (FPP), 10 μM geranylgeranyl pyrophosphate (GGPP), 30 μM squalene, 30 μM isopentenyladenine, 30 μM ubiquinone, or 30 μM dolichol for 4 h and then treated with (B) 5 μM mevastatin, (C) 5 μM fluvastatin, or (D) 10 μM simvastatin for 72 h.

All multicellular species AZD6094 molecular weight studied here are closely related, and species capable of terminal differentiation form a monophyletic group. Comparisons of our study to previous findings show high similarities. Our results agree with a comparative phylogenomics PD98059 price approach used by Swingley et al.[36], a consensus tree of concatenated sequences presented by Blank and Sànchez-Baracaldo [47], and, are highly similar to 16S rRNA analyses conducted by Schirrmeister et al.[39]. Using

a larger taxon set [39], we previously inferred polyphyletic groupings of undifferentiated multicellular species belonging to section III. This however is not deducible from the taxonomically more limited full genome data set used in the present study. In cyanobacteria 16S rRNA sequences were highly conserved within a genome. Three species showed minor nucleotide differences. The two 16S rRNA copies of Microcystis aeruginosa GS-9973 datasheet differed by four ‘single nucleotide polymorphisms’ (SNPs), in Cyanothece sp. PCC 7424 one SNP was detected, and in Nostoc punctiforme one 16S copy possessed two SNPs. The differences are

visualized in a molecular distance matrix in Figure 4. 16S rRNA copies within species were identical for the majority of taxa (shown in yellow) and can be clearly distinguished from gene copies belonging to different species. Furthermore, using the whole dataset we calculated mean distances within strains (d W ) and between strains (d B ). Results are presented in Table 2. Significance of differences in sequence distances found within and between cyanobacterial strains were estimated using bootstrap re-sampling of the original data set. Distributions

of the resulting mean distances are displayed in Additional files 4 and 5. For each distribution, an C59 nmr overall mean distance was calculated ( ). Mean distance of 16S rRNA sequences within species (d W =0.0001) is significantly smaller than between species (d B =0.14; Table 2). 95% confidence intervals of distributions obtained by re-samplings do not overlap. Although previous studies have claimed that variation within 16S rRNA sequences might affect reliability of this gene as a taxonomic marker [10, 34], this was not found for genera used in this study. Rather, the extreme sequence conservation of 16S rRNA gene copies from the same species supports 16S rRNA as a reliable genetic marker for the taxa analyzed here. Figure 4 Distance matrix of cyanobacterial 16S rRNA sequences. Distance matrix between 16S rRNA genes estimated based on K80 substitution model. 16S rRNA gene copy numbers range from one to four per cyanobacterial genomes studied. White lines separate sequence copies of different species. 16S rRNA sequences are highly conserved within species.

5 μg/ml nystatin as the wt (see Additional file 1). Conversely, Cagup1Δ null mutant strain displayed a notorious resistance to all the EBIs used, the azoles with antifungal action, clotrimazole, fluconazole and ketoconazole, and the morpholine fenpropimorph (Figure 1). The resistance of Cagup1Δ null mutant strain to clotrimazole and ketoconazole only became obvious at concentrations of 68.8 and 106.3 μg/ml respectively (Figure 1). Moreover, in the presence of 172 μg/ml clotrimazole and of 265.7 μg/ml ketoconazole

the growth of both strains was impaired (not shown). The effect of fluconazole, on the other hand, was stronger. The resistance of Cagup1Δ null mutant strain to this drug could be detected using 30.6 μg/ml (Figure 1). With regards #LB-100 nmr randurls[1|1|,|CHEM1|]# to fenpropimorph, DMXAA we verified that, in the presence of 120 and 240 μg/ml of this drug, none of the strains were able to grow (not

shown). When the dosage was reduced to 60 μg/ml, the Cagup1Δ null mutant strain was more resistant than the parental strain (Figure 1). A copy of the GUP1 gene, comprising 1.5 Kb of the promoter region and 380 base pairs of the terminator region, was introduced into the Cagup1 null mutant strain at the RPS1 locus using the Clp20 plasmid [36]. Correctly, it is possible to see in the same figure that the GUP1 complemented strain CF-Ca001, displayed a comparable behaviour to wt. Moreover, the introduction of the empty Clp20 plasmid into Cagup1Δ null mutant, or into wt, did not cause any amendment on these strains phenotypes (not shown). Figure 1 Cagup1Δ null mutant strain displays Verteporfin mw an altered sensitivity to specific ergosterol biosynthesis inhibitors. Isogenic wt, Cagup1Δ null mutant and CF-Ca001 strain were grown to mid-exponential phase in YPD medium. Ten-fold serial dilutions were spotted onto (1) YPD plates (control) and plates supplemented with (2) clotrimazole 68.8 μg/ml, (3) ketoconazole 106.3 μg/ml, (4) fluconazole 30.6 μg/ml and (5) fenpropimorph 60 μg/ml.

All plates were incubated at 30°C and photographed after 3-5 days. The gup1Δ panel photos are representative of the results obtained with the several clones (3-5) of Cagup1Δ null mutant strain tested. Furthermore, we checked if the strains had different growth rates, which could have some impact on these results. Indeed, in liquid medium (which is the only way we can compare growth velocities) the doubling time during experimental phase of the wt, mutant and complemented strains is respectively 1.27 ± 0.04 h; 1.43 ± 0.06 h and 1.25 ± 0.05 h. We also determined the mutant doubling time in the presence of fluconazole, which was lower than its value in the absence of the drug. The same happens with the wt. The doubling time during experimental phase of the wt, mutant and complemented strains in the presence of fluconazole are respectively 1.07 1 ± 0.07 h; 1.28 ± 0.09 h and 1.11 ± 0.09 h. Alternatively, we used the Methyl-Blue diffusion assay.

In-vivo micro-CT imaging was first performed at the age of 2 months (day 55 to day 61) and repeated every 4 weeks. Follow-up examinations were repetitively carried out until the animal had to be euthanized due to medical condition or termination of the study. The follow-up had to be terminated on day 146 in one animal, in the other animals between day 362 and 547. A total of 156 CT exams were carried out in this study. Isoflurane inhalation anaesthesia was administered using a nose GW786034 nmr cone. The animals were placed in prone

position on a multimodality bed that enables changes between the different imaging modalities without repositioning. A pressure transducer pad was placed under the animal’s chest for respiratory monitoring, which was used for respiratory gating and for control of anaesthesia. Micro-CT Non contrast-enhanced prospectively respiratory gated micro-CT was performed (GE Explore Locus, General Electric Healthcare, Chalfont St.

Giles, UK) with an effective pixel size of 0.094 mm (80 kV, 450 μA, 360 projections/scan, exposure time/projection 100 ms, scan technique 200°, 4 × 4 detector bin mode). The scan FOV was 32.8 mm. For respiratory gating the signal from the transducer pad was used to generate the image acquisition time points using the software ARN-509 datasheet Biovet (m2 m Imaging, Newark, NJ, USA). Images of the chest were reconstructed and calibrated to the Hounsfield scale. Expected mean radiation dose was calculated to be 197 mGy based on phantom and cadaver measurements in a previous study [10]. Histology The imaging findings were correlated to necropsy

and histology in 10 cases (8 transgenic and 2 control, see table1) by direct visual comparison. In two animals no histology was obtained. At necropsy lung surface was assessed for tumour affection and correlated to imaging. After necropsy the excised lungs were filled with Tissue-Tek O.C.T.® (Sakura, Finetek Europe, NL) and subsequently fixed in 4% buffered formalin (pH 7.2). After dehydration (Shandon Hypercenter, XP) lungs were embedded in paraffin. Sections (2 μm thick) were NCT-501 deparaffinized with xylene and H&E stained. Post-Processing For PD184352 (CI-1040) quantification of the multifocal tumours a segmentation of the aerated parts of the lungs was used as a surrogate parameter, as direct measurement was not feasible. A region-growing algorithm for micro-CT quantification of tumour load and progress for diffuse lung adenocarcinoma was established and validated earlier [11]. The open-source software MevisLab (Fraunhofer Mevis, Bremen, Germany) was applied, 20-40 seed points were used to generate the region growing segmentation with a segmentation threshold tolerance of 2% (Figure 1 and 2). For each data set 3 separate segmentations were performed and the results of the 3 measurements were averaged. Figure 1 Segmentation of aerated lung volume as a surrogate parameter to assess the multifocal tumor spread.

The deletion of fur reduced the aerobic rate of synthesis of the reporter gene by > AICAR order 2-fold compared to the parent strain (Figure 4A). 2, 2′ dipyridyl (dip) reduced the rate of synthesis of Selleckchem PD-1/PD-L1 Inhibitor 3 the reporter gene in aerobic conditions (Figure 4A). Although induction of the reporter fusion occurred earlier in the growth phase with dip treated cultures, the rate of synthesis was reduced compared to untreated parent strain. This indicates inhibition by dip (Figure 4A). As expected, the oxygen sensitive regulator Fnr did not impact regulation of ftnB in aerobic conditions (Figure 4A). This indicated that Fur is required for ftnB expression,

independent of Fnr. Data in Figure 4B show that the absence of fur resulted in a 2-fold reduction in the rate of synthesis (U/OD600) of ftnB-lacZ under anaerobic conditions. Furthermore, the ferrous iron chelator, dip, reduced the rate of anaerobic synthesis of ftnB-lacZ in the WT strain by > 2-fold (Figure 4B). In Δfur, the rate of synthesis was further reduced (> 10-fold)

when compared to the WT parent strain treated with dip (Figure 4B). In addition, the rate of synthesis in the parent strain was greatest under selleck chemicals llc anaerobic conditions due to the active roles of both Fnr and Fur (Figure 4). Collectively, full expression of ftnB is dependent on Fur in aerobic and anaerobic conditions, whereas Fnr is a strong activator in the absence of O2. Figure 4 Effects of Fur, Fnr and iron chelation

on transcription of ftnB. Transcriptional ftnB-lacZ activity was determined in 14028s (squares), Δfur (circles), and Δfnr (triangles) under (A) anaerobic, and (B) aerobic conditions in LB-MOPS-X media without (open symbols) and with (closed symbols) 200 μM of 2, 2′ dipyridyl. β-galactosidase assay was conducted throughout the growth of the culture and activity is presented in the form of differential plots with representative data shown in (A) and (B). Best-fit lines, calculated as described in the Methods, are shown in (A) and (B). For (A) and (B), representative data are shown with the differential rate of synthesis (U/OD600) ± standard deviations from three independent experiments listed. c. Regulation of hmpA The gene coding for the flavohemoglobin (hmpA), a NO· detoxifying protein [95–98], was differentially click here expressed in Δfur (Additional file 2: Table S2). Expression of hmpA is repressed by Fnr and another DNA binding protein that contains an iron sulfur cluster, NsrR [21, 95–97, 99]. Repression of hmpA by two regulators that are sensitive to RNS allows derepression of this gene under conditions of increased RNS. Indeed, regulation of hmpA-lacZ was induced ~80-fold by the nitrosating agent sodium nitroprusside in aerobic conditions (B. Troxell and H.M. Hassan, unpublished data). Under anaerobic conditions, hmpA was up-regulated 4-fold in Δfur.

In Europe, some hope is offered by the upcoming CAP reform, formally adopted by the Council

of EU Agriculture Ministers on 16 December 2013. Basic Regulations for the SC79 clinical trial reformed CAP (ec.europa.eu/agriculture/cap-post-2013) include measures aimed at the “greening” of direct payments in Pillar 1. One of these measures, the creation of ecological focus areas (EFA), intends to maintain find more at least 5 % (and possibly 7 % after 2017) of farmland for environmental purposes (Allen et al. 2012). Since EFA primarily include diverse semi-natural habitats, the maintenance of field margins should be a matter of the utmost importance. At the national level the agri-environment-climate schemes (AES) in Pillar 2 have been recognized as having the greatest potential to address many environmental concerns (Wade et al. 2008). The variety of packages see more tailored to national circumstances targeted more or less threatened species; unfortunately, evidence from Western Europe indicates that these species have rarely benefitted from such schemes (Kleijn et al. 2006). Our study is particularly relevant to the measures aimed at maintaining various strips in the field or at the edge of the field, between

the crop and the boundary (Vickery et al. 2009; Josefsson et al. 2013). In Polish AES these measures comprise the buffer zones scheme (BZ), present in the current program and until recently considered for the new version 2014-2020. Unfortunately,

in the current program payment rates in BZ scheme were very low (20–50$ per 100 m) and were in conflict with direct payments (Keenleyside 2006). In the end, BZ was the scheme with the least uptake of all packages, appealing to a mere 0.002 % of the 117,000 farmers who applied for contracts in 2012 (The Agricultural Advisory Centre in Brwinów, unpubl. data). In consequence, the abandonment of this scheme, and also the margin strip scheme developed for the new AES, are being considered in the revised program. Even though the program is still under debate, in December 2013 these particular schemes have clonidine been removed, which flies in the face of conservation evidence and thwart the principal aims of AES. We argue that retaining the BZ and the related schemes aimed at creation of the margin strips, as well as a significant increase in payments are obvious prerequisites for accomplishing environmental benefits. Several targeted field-scale measures could be designated within these schemes. As a baseline they should promote and sustain a mosaic of field margins, from herbaceous boundaries, to multilayered tree lines, with particular attention given to shrubby margins. The proportion of these margin types in the landscape and detailed management recommendations, for example, leaving the outermost strip of field free of agrochemical input, partial cutting of margin vegetation and the removal of biomass, should be additionally drawn up.

The use of digital photography for monitoring the degradation of pSi in aqueous media was validated by simultaneous

buy Olaparib spectrophotometric measurements of the pSi reflectance spectrum. Methods Preparation of freshly etched porous check details silicon chips (fpSi) Porous silicon was prepared by anodic electrochemical etching of highly doped 0.95 mΩ cm p++-type (100)-oriented silicon wafers (Virginia Semiconductor, Fredericksburg, VA, USA) in a 3:1 (v/v) mixture of aqueous hydrofluoric acid (49%) and ethanol. The fpSi samples were prepared in a Teflon etch cell that exposed 1.2 cm2 of the polished face of the Si wafer, which was contacted on the back side with a piece of Al foil. A platinum spiral was used as a counter-electrode. A rugate filter was generated using a current density modulated with 100 cycles

of a sinusoidal waveform oscillating between 15 and 108 mA/cm2, with periods on the order of 6 s depending on the desired wavelength of maximum reflectivity. After etching, the fpSi samples were rinsed with ethanol and dried in a stream of nitrogen. Preparation of porous silicon coated with chitosan (pSi-ch) A 1% chitosan solution was prepared by dissolving 10 mg chitosan from crab shells, 85% deacetylated (Sigma Aldrich, St. Louis, MO, USA) in 1 mL of 15% v/v aqueous acetic acid and stirring overnight. The fpSi sample was coated with chitosan by spin coating (Laurell WS-400B-6NPP-Lite, Laurell Technologies, PD 332991 North Wales,

PA, USA) using 150 μL of chitosan solution at a final speed of 100 rpm for 10 min and then drying at room temperature under nitrogen. The sample was then placed under vacuum to evaporate the remaining solvent. After the deposition, the pSi-ch samples were heated at 70°C on a hot plate for 10 min to cause a small amount of polymer infiltration into the pores, and this resulted in a slight red shift in the rugate reflectance peak position. Instrumental procedures The porosity and thickness of the porous silicon layers were estimated by the spectroscopic liquid infiltration method (SLIM), based on the measurement of the thin-film interference components HA-1077 mouse of the reflectance spectra of the samples before and after infiltration of a liquid (ethanol) with known refractive index [16] by using an Ocean Optics USB-2000 spectrometer (Ocean Optics, Dunedin, FL, USA) configured for specular reflectance, working in back-reflection configuration in the range 400 to 1,000 nm. The reflectance spectra were recorded at five spots distributed across each sample in order to evaluate the homogeneity of each porous silicon sample. The values of the porosity and the thickness were determined by means of the two-component Bruggeman effective medium approximation [17]. The extent of chitosan infiltration into the porous silicon sample was also evaluated from the reflectance spectrum.

Science 1994,263(5147):678–681.PubMedCrossRef 5. Oh YK, Straubinger RM: selleck inhibitor intracellular fate of Mycobacterium avium : use of dual-label spectrofluorometry to investigate the influence of bacterial viability and opsonization on phagosomal pH and phagosome-lysosome interaction. Infect Immun 1996,64(1):319–325.PubMed 6. Via LE, Deretic D, Ulmer RJ, Hibler NS, Huber LA, Deretic V: Arrest of mycobacterial phagosome maturation is caused by a block in vesicle fusion between stages controlled by rab5 and rab7. J Biol Chem 1997,272(20):13326–13331.PubMedCrossRef 7. Beuzon CR, Meresse S, Unsworth KE, Ruiz-Albert J, Garvis S, AC220 Waterman

SR, Ryder TA, Boucrot E, Holden DW: Salmonella maintains the integrity of its intracellular vacuole through the action of SifA. Embo J 2000,19(13):3235–3249.PubMedCrossRef 8. Holm A, Tejle K, Magnusson KE, Descoteaux A, Rasmusson B: Leishmania donovani lipophosphoglycan causes periphagosomal actin accumulation: correlation with impaired translocation of PKCalpha and defective phagosome maturation. Cell Microbiol 2001,3(7):439–447.PubMedCrossRef 9. Sturgill-Koszycki S, Schaible

UE, Russell DG: Mycobacterium -containing PRT062607 datasheet phagosomes are accessible to early endosomes and reflect a transitional state in normal phagosome biogenesis. Embo J 1996,15(24):6960–6968.PubMed 10. Malik ZA, Iyer SS, Kusner DJ: Mycobacterium tuberculosis phagosomes exhibit altered calmodulin-dependent signal transduction: contribution to inhibition of phagosome-lysosome Vitamin B12 fusion and intracellular survival in human macrophages. J Immunol 2001,166(5):3392–3401.PubMed 11. Li Y, Miltner E, Wu M, Petrofsky

M, Bermudez LE: A Mycobacterium avium PPE gene is associated with the ability of the bacterium to grow in macrophages and virulence in mice. Cell Microbiol 2005,7(4):539–548.PubMedCrossRef 12. Dheenadhayalan V, Delogu G, Sanguinetti M, Fadda G, Brennan MJ: Variable expression patterns of Mycobacterium tuberculosis PE_PGRS genes: evidence that PE_PGRS16 and PE_PGRS26 are inversely regulated in vivo. J Bacteriol 2006,188(10):3721–3725.PubMedCrossRef 13. Brennan MJ, Delogu G, Chen Y, Bardarov S, Kriakov J, Alavi M, Jacobs WR Jr: Evidence that mycobacterial PE_PGRS proteins are cell surface constituents that influence interactions with other cells. Infect Immun 2001,69(12):7326–7333.PubMedCrossRef 14. Delogu G, Pusceddu C, Bua A, Fadda G, Brennan MJ, Zanetti S: Rv1818c-encoded PE_PGRS protein of Mycobacterium tuberculosis is surface exposed and influences bacterial cell structure. Mol Microbiol 2004,52(3):725–733.PubMedCrossRef 15. MacGurn JA, Raghavan S, Stanley SA, Cox JS: A non-RD1 gene cluster is required for Snm secretion in Mycobacterium tuberculosis . Mol Microbiol 2005,57(6):1653–1663.PubMedCrossRef 16.