Acid phosphatases (EC 3.1.3.2) catalyze the hydrolysis of phosphate monoesters or transfer of phosphate groups between phosphoester and alcohols. The enzymes catalyze optimally at acidic conditions and selleck chemicals llc are completely and structurally different from alkaline phosphatases (EC 3.1.3.1), which

work optimally at alkaline conditions [25–27]. Unlike the alkaline phosphatases, the acid phosphatases, do not utilize metal ions in their catalysis. They rather utilize histidine residue to form a phospho-histidine-enzyme intermediate which is essential for their catalysis. In contrast, alkaline phosphatases make use of a phospho-serine-enzyme intermediate for their catalysis and have a binuclear Zn (II) active site [26, 28]. Phosphatases are

important in the physiology of an organism as they function in many catalytic reactions relating to activation or deactivation of enzymes. Deficiencies in phosphate metabolism have been reported to be related to reduction of virulence in many bacterial species such as Listeria monocytogenes, EPZ5676 Streptococcus pneumoniae, Vibrio cholerae, Proteus mirabilis and M. tuberculosis[29–34]. The fact that histidine acid phosphatases and cofactor dependent phosphoglycerate mutases share similar catalytic amino acid residues and mechanism of catalysis warrants their placement in the same superfamily [9]. This often leads to some difficulties in predicting the function of an enzyme that belongs to the superfamily. Thus, biochemical characterization of purified enzymes PRIMA-1MET is necessary before the function of any member of histidine phosphatase superfamily can be ascertained. In this study, we report the first cloning, purification and characterization of M. tuberculosis Rv2135c. In addition, we cloned and characterized Rv0489. Its role as a cofactor dependent phosphoglycerate mutase was confirmed. Results The histidine phosphatase motif in Rv2135c Using

NCBI BLAST [35], a number of proteins with similar sequences to Rv2135c were identified. Some sequences, including Rv0489, were aligned using ClustalX2 with the results shown in Figure 1. Most of the similar sequences contain the histidine phosphatase motif of ‘RHG’ , which contributes to catalysis, at the N-terminal region. The motif becomes ‘RHA’ (at residue 7–9) in Rv2135c. This is similar to the motif found in phosphoglycerate mutase domain containing Atezolizumab protein of C. parvum (GAN CAD98474). Other conserved residues known to be involved in the catalysis of this superfamily from the analysis of others members are also present in Rv2135c. [4, 9, 36]. These include Arg57, Glu82, and a fully conserved His153 at the C-terminal region, Figure 1. Figure 1 Multiple alignment of amino acid sequences of some members of histidine phosphatase superfamily with Rv2135c. The alignment was done with ClustalX2 using the default parameters. The asterisks indicate fully conserved amino acid residues of the superfamily.

The Caspase Inhibitor VI nmr specificities of the four screening agars have been documented in previous studies focusing on the ability to detect ESBL-producing Cytoskeletal Signaling inhibitor bacteria within the Enterobacteriaceae family. These studies included none or just a few Salmonella isolates, and the specificity varied greatly. ChromID ESBL agar was included in most of the studies, and the specificity ranged

from 72.9% – 94.9% [33-36]. The specificity of the Brilliance agar ranged from 57.9%– 95.1% [33,34,36], and for BLSE agar the specificity ranged from 60.8-85.0% [34,35]. CHROMagar ESBL has been evaluated by Grohs et al. only, with a reported specificity of 72.3% [33]. However, some of the previous studies seem to have included ESBL-producing non-Enterobacteriaceae isolates as test positives, while other studies only included ESBL-producing isolates within the Enterobacteriaceae family. This difference may explain the apparent great variations in specificities reported. The frequency of human infection with Salmonella and Shigella in Norway is relatively low. Consequently, to gain proper statistical power in a real-life study evaluating screening plates for ESBL-positive strains of these two genera would be time consuming. We therefore chose

to use a suspension of a normal fecal sample spiked Vemurafenib with the ESBL- positive isolates. The quantity of ESBL-positive bacteria in the fecal samples is known to be a factor of the sensitivity of the screening agars [37]. In genuine fecal samples the quantity of bacteria varies, but Racecadotril in this study we spiked the same quantity of bacteria in all samples. Salmonella are normally lactose negative and produce neither β-galactosidase nor β-glucuronidase. Consequently, colonies of Salmonella appeared colourless on agarplates that use these enzymes in the chromogenic reactions. Shigella sonnei is both β-glucuronidase and β-galactosidase-positive and appeared much like E. coli on these screening agars. Therefore direct differentiation of Shigella sonnei and E. coli is difficult. However, none

of the manufacturers mention this similarity in their product information. On the other hand, Shigella flexneri does not express these enzymes, and will not appear like E. coli on the screening agars. This was confirmed in our testing. Obviously, testing only two Shigella flexneri isolates is insufficient to give a statistically reliable result. Three Salmonella isolates of different serovars had pink colonies on both ChromID and Brilliance agars, whereas the rest of the Salmonella isolates had colorless colonies. It is necessary for the pink color formation that the bacteria express β-glucuronidase, which is described that some Salmonella bacteria actually do [38]. The color-based identification was non-specific and comparable to expected results from using a non-chromogenic agar with the same antibacterial supplements.

Table 1 Concentration of urinary protein and creatinine   Urine protein (mg/ml) Urine creatinine (mg/dl) (A) First study  IgAN 0.55 ± 0.06 133.6 ± 7.8  MN 2.97 ± 0.68 121.4 ± 14.2  SLE 2.99 ± 0.133 116.0 ± 18.6  FGS 2.37 ± 1.05 112.7 ± 13.9  MCNS 5.03 ± 1.42 77.6 ± 33.5  DMN

2.31 ± 1.05 62.7 ± 19.8  Other kidney diseases selleck chemical 1.60 ± 0.46 106.8 ± 16.5 (B) Second study  IgAN (before treatment) 0.75 ± 0.17 134.9 ± 11.8  Inactive IgAN (after treatment) 0.63 ± 0.13 96.8 ± 16.9  Alport syndrome 1.55 ± 0.45 82.9 ± 10.7  Amyloidosis 0.71 ± 0.20 78.4 ± 13.3  MPGN 1.32 ± 0.25 111.3 ± 41.3  ANCA-related nephritis 1.37 ± 1.11 50.8 ± 3.4  TBMD 0.23 ± 0.11 124.1 ± 50.0  FGS 2.68 ± 1.46 128.1 ± 39.6  Lupus nephritis (SLE) 2.45 ± 1.71 187.4 ± 116.0  DMN 1.36 ± 0.24 76.4 ± 34.7  MN 1.63 ± 0.33 94.1 ± 17.9  Hypertensive nephrosclerosis 0.25 30.8 In

the second study (examination in other diseases groups—focused test to discriminate other diseases from IgAN), urine samples were obtained from various forms of biopsy-proven kidney disease patients exhibiting hematuria with or without proteinuria include IgAN (before treatment; 31 patients), and inactive IgAN; hematuria was no longer present after tonsillectomy with steroid pulse therapy (4 patients) [10–13], Alport syndrome (8 patients), amyloidosis (3 patients), membranoproliferative glomerulosclerosis (MPGN; 4 patients), anti-neutrophil cytoplasmic antibody (ANCA)-related nephritis (2 patients), thin basement membrane disease (TBMD; 2 patients), FGS (4 patients), SLE (2 patients), DMN (2 patients), MN (4 patients), and hypertensive nephrosclerosis (1 patient). Urinary MK-1775 in vivo protein and creatinine concentrations of each disease are shown in Table 1B. Reverse transcriptase Selleck TPX-0005 Immunoprecipitation (IP) method Anti-human IgA antibody (Cappel Co.)

was immobilized on Dynabeads® M-450 Epoxy (Invitrogen Co.) according to manufacturer’s instruction and blocked with bovine serum albumin (BSA). A Tris–HCl buffered (pH 7.5) urine sample containing 0.15 M sodium chloride (NaCl) was mixed with anti-IgA-immobilized beads or control beads (BSA-blocked beads) and incubated overnight at 4°C. After washing with phosphate-buffered saline (PBS), proteins were eluted from beads with 0.1 M citric acid buffer (pH 3.0) and dialyzed against 1/10 concentration of PBS containing 0.01% sodium azide (NaN3), and concentrated. Identification of proteins combined with IgA in urine Proteins recovered from the anti-IgA antibody affinity beads and control beads were separated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The proteins of interest were analyzed according to the method of Katayama et al. [18]. Western blot analysis The 3 μl of protein solution prepared by IP was separated by SDS-PAGE, and the proteins were then electrophoretically blotted onto a nitrocellulose filter (BA85; Schleicher & Schuell).

Detailed results are given as Electronic Supplementary Material (ESM 1). Detached-leaf assay The C. cassiicola isolates were cultivated on PDA at 25 °C with a 12 h photoperiod. The conidia were collected and resuspended in sterile water supplemented with 0.02 % Tween20 at a concentration of 5000 conidia/ml. For each Go6983 mw isolate, six leaves were inoculated,

each with ten drops of 20 μl conidia suspension applied to the abaxial surface of detached rubber tree leaflets in developmental stage C (brownish to limp green) (Hallé and Martin 1968). One additional drop of 20 μl of sterile water supplemented with 0.02 % Tween20 was added to each leaflet as negative control. The leaflets were maintained in a moist environment at 25 °C for 24 h in the dark and then under alternate light with a 12 h photoperiod. The conidial suspension was evaporated four days after the inoculation.

The lesion area per leaflet was measured manually, at 5 and 9 dpi. The entire experiment was conducted three times. The symptoms intensity (SI) was expressed as the mean lesion area ± the standard error from the 18 inoculated leaves (six leaflets per inoculation and three biological selleck chemical replicates). Detection of cassiicolin gene Wortmannin homologues Detection of cassiicolin gene homologues by PCR was conducted on the four C. cassiicola isolates (E70, E78, E79 and E139) from asymptomatic mature rubber tree leaves. The first set of primers was designed from the Cas sequence from isolate CCP (EF667973) and included CasF9, CasF11, CasF12, CasR16, CasR20 and CasR19. The second set of primers, CT1F9, CasF14, CT1R16 and CasR22, was designed from the CT1 sequence from the isolate Carbohydrate CC004 (GU373809). Primer sequences are listed in the Electronic Supplementray Material ESM 2. PCR was performed on 100 ng of C. cassiicola genomic DNA for 30 cycles

(45 s at 94 °C, 45 s at 50 °C, 45 s at 72 °C) using the same PCR components described above. Cloning of full-length Cassiicolin gene homologues The full-length sequence of the cassiicolin gene homologue Cas3 was obtained by genome walking (Sallaud et al. 2003). This method allows for amplification of the 5′ and 3′ flanking regions of a target gene. Genomic DNA from isolate E70 was digested with 30 units of a restriction enzyme generating 3′ blunt overhangs. Four restriction enzymes were tested independently: EcoRV, DraI, PvuII and StuI (New England Biolabs). The digested products were purified using the QIAquick PCR Purification Kit (Qiagen, Courtaboeuf, France) and ligated to the ADPR1/ADPR2 adaptor by T4 DNA ligase at 16 °C overnight in a final volume of 20 μl. The first PCR was performed with 1 μl of the ligation/digestion using the primer AP1, which is specific to the ADPR1 adaptor, and a primer specific to the Cas3 partial sequence obtained previously from isolate E70 using the CasF9/CasR20 primer pair.

PubMedCrossRef 69. Brodsky IE, Medzhitov R: Targeting of immune signalling networks by bacterial pathogens. Nat Cell Biol 2009,11(5):521–526.PubMedCrossRef 70. Fukano Y, Knowles NG, Usui ML, Underwood RA, Hauch KD, Marshall AJ, Ratner BD, Giachelli C, Carter

WG, Fleckman P, et al.: Characterization of an in vitro model for evaluating the interface between skin and percutaneous biomaterials. Wound Repair Regen 2006,14(4):484–491.PubMedCrossRef 71. Lenz AP, Williamson KS, Pitts B, Stewart PS, Franklin MJ: Localized gene expression in Pseudomonas aeruginosa biofilms. Appl Environ Microbiol 2008,74(14):4463–4471.PubMedCrossRef 72. Sturn A, Quackenbush J, Trajanoski Z: Genesis: cluster analysis of microarray click here data. Bioinformatics 2002,18(1):207–208.PubMedCrossRef 73. Dennis G Jr, Sherman BT, Hosack DA, Yang J, Gao W, Lane HC, Lempicki RA: DAVID: Database for Annotation, Visualization, and Integrated Discovery. Genome Biol 2003,4(5):P3.PubMedCrossRef Competing interests The authors declare that they have no competing interests. Authors’ contributions PRS was responsible PF01367338 for culturing keratinocytes and S. aureus, SDS-PAGE analysis, ELISA assays, MAPK analysis, running TUNEL assays, RNA extractions, and ARS-1620 in vitro drafted the manuscript. KM carried

out microarray sample processing and analysis. GAJ, PF, JEO, and PSS conceived of the study, participated in its design and coordination, and helped to draft the manuscript. All authors read and approved the final manuscript.”
“Background The pathogenic nature of Salmonella enterica has been shaped by the horizontal acquisition of virulence determinants

[1, 2]. In Salmonella enterica serovar Typhimurium (S. Typhimurium), many virulence genes are organized in mobile elements such as pathogenicity islands, prophages, and the Salmonella virulence plasmid [3, 4]. The increased pathogenic capacity conferred PLEK2 by such genes is dependent on their integration into ancestral regulatory networks of the cell, which can be accomplished by regulatory evolution following horizontal gene transfer [5]. The Hha/YmoA family of small nucleoid-associated proteins in Enterobacteriaceae [6] can participate in fine-tuning virulence gene expression in response to environmental cues [6, 7]. For example, YmoA regulates expression of Yop proteins, YadA adhesin, Yst enterotoxin and invasin in Yersinia enterocolitica [7–9]. Hha negatively regulates the α-hemolysin genes hlyCABD in Escherichia coli [10], hilA encoded within Salmonella pathogenicity island 1 (SPI-1) in S. Typhimurium [11] and the locus of enterocyte effacement in enterohemorrhagic E. coli [12]. A third member, YdgT, similarly represses hlyCABD in E. coli [13]. We and others have shown that Hha and YdgT are repressors of the type III secretion system (T3SS) encoded in Salmonella Pathogenicity island 2 (SPI-2), where they provide an important negative regulatory input required for virulence [14–16].

Rats too weak to feed and to stand (corresponding to stage 2) were sacrificed (atmosphere saturated with CO2). The day of euthanasia was recorded and used IGF-1R inhibitor in the survival analysis. All brains were removed and macroscopically examined when possible. It was noted if a tumor was found. Table 2 Rats staging (data not published)   Stage 5 Stage 4 Stage 3 Stage 2 Stage 1 AMN-107 chemical structure Motility Normal Normal + but not spontaneous Reduced No Stature Normal Stooped + Stooped ++ Stooped +++ Dying Piloerection No +/- +++ +++ +++ Eyes sharp Redness+ Redness ++

Eye secretions closed Statistics Survival was calculated from the day of the tumor implantation and presented as median and mean ± SE (Standard Error). Increase of life span (ILS) was calculated as follows: (Mean Survival Max – Mean Survival Min)/Mean Survival Min × 100. A Student t-test was performed to compare mean survival in the two groups, using SPSS® software and tests were considered as significant with p values < 0.05. Any rat surviving longer than 120 days was defined as a 'long survivor'. The Kaplan-Meier method was used Selleckchem 4SC-202 to plot animal survival. Animals that died during anesthesia

were not included in the survival analysis. Results Efficacy of the brain irradiation The dosimetry planning is reported in figure 3. The 95%-isodose curve covered all the brain and 95% of the volume received 95% of the total dose. In the group A, two animals died during anaesthesia induction, before the tumor cells implantation. The

brain was analyzed macroscopically in 12 animals (six in group A and six in group B). Deterioration of the brain in other animals, due to oedema, prevented analysis. For the 12 animals, a large tumor was observed in their right striatum. By day 35, all rats in group A died. Mean survival of this untreated group was 28.1 days ± 1.3. For group B, mean survival was 59.9 days ± 8.2 (Table 3). The rate of Cyclic nucleotide phosphodiesterase long survivors in this group was 20% (2/10 rats). The macroscopic examination of their brain was normal, with no sign of tumor or injection trail; therefore we did not perform a microscopic analysis. Rats treated with WBI showed an increased mean survival span (ILS) of 113% when compared to controls. Survival time was significantly longer compared to the control group (p = 0.01) (Figure 4). Figure 3 Dose distribution in the whole rat brain. Table 3 Descriptive and statistical data from the survival study depending on groups of treatment GROUPS Median of survival (days) Mean time of survival (days) ± SE Mean ILS (%) Long term survivors Maximal time of survival (days) Group A « untreated » (n = 8) 27 28.1 ± 1.3 – 0 35 Group B « WBI » (n = 10) 49.5 59.9 ± 8.2 113 2 120 WBI: Whole brain irradiation ILS: increase in lifetime span Figure 4 Survival curves depending of each group of treatment. Survival times (days) after tumor implantation have been plotted for “”untreated animals”" (Group A) and “”WBI (3 fractions of 6 Gy)”" animals (group B).

Mites were either set up as cultures in the lab or stored in 96% ethanol. DNA was extracted from single mites using the CTAB extraction method as previously described [54] or using find more the NucleoSpin Kit (Macherey-Nagel, Düren, Germany) following manufacturers’ instructions. For Wolbachia, four genes were amplified and sequenced: wsp, flsZ, groEL, and trmD. Wsp was amplified and sequenced using the primers wsp-81F and wsp-691R [70]. FtsZ and groEl were amplified and sequenced as described in Ros et al. [49]. TrmD was amplified and sequenced using the primers trmD-F 5’-GAACTATTCTCTTTGCCGGAAAAGC-3’

and trmD-R 5’-CACTGCTCAGGTCTAGTATATTGAGG-3’.These primers were designed from available Wolbachia and Rickettsia genome sequences [71–73] and were shown to buy Fer-1 reliably amplify products from strains representative of supergroups A and B (data not shown; samples kindly donated by Dr. Robert Butcher). For Cardinium, two genes were amplified: 16S rDNA and gyrB. 16S rDNA was amplified and sequenced directly using the primers CLOf and CLOr1 [2]. GyrB was amplified using primers from Groot and Breeuwer [74], cloned, and subsequently sequenced. PKC412 concentration Amplified fragments were separated from non-specific products by running the PCR products on a 1% agarose in 1x TAE gel and excising the fragments from the gel. Fragments were purified using the method of Boom et al. [75]. Products were first cloned and subsequently sequenced following the cloning protocol

described below, with 1-2 clones sequenced per sample using M13 forward and reverse primers. PCR amplifications were performed

in 25 μl reactions containing 1X Super Taq buffer (HT BioTechnology, Cambridge, UK), 0.5 mg/ml bovine serum albumin (BSA), 1.25 mM MgCl2, 0.2 mM dNTP’s, 160 nM of each primer, 1 u of Super Taq (HT BioTechnology), and 2.5 μl of DNA extract. For ftsZ, groEL, and trmD, no MgCl2 was added and for 16S rDNA no MgCl2 and BSA was added. PCR cycling profile for wsp and ftsZ was 35 cycles of 30 sec. at 95 °C, 30 sec. at 51 °C, and 1 min. at 72 °C, for groEL and trmD 35 cycles of 1 min. at 95 °C, 1 min. at 49 °C, and 1.5 min. at 72 °C, for Cardinium 16S rDNA 35 cycles of 40 sec. at 95 °C, 40 sec. at 57 °C, and 45 sec. at 72 °C, and for gyrB 35 cycles of 1 min. at 95 °C, 1 min. at 50 °C, and 1 min. at 72 °C. Products (2 μl) were visualized on a 1% agarose gel stained with ethidium bromide in 0.5X TBE buffer (45mM Tris base, 45mM Pyruvate dehydrogenase boric acid, and 1 mM EDTA, pH 8.0). PCR products were purified using a DNA extraction kit (Fermentas, St. Leon-Rot, Germany). The purified products were directly sequenced using the ABI PRISM BigDye Terminator Sequence Kit (Applied Biosystems, Nieuwerkerk a/d IJssel, The Netherlands). Both strands of the products were sequenced using the same primers as used in the PCR amplification. Sequences were run on an ABI 3700 automated DNA sequencer. All new unique sequence data have been submitted to the GenBank under accession numbers: JN572802-JN572888 (see Additional file 4).

While total bacteria and Betaproteobacteria were correlated with the presence of thymol in the leaves, the Alphaproteobacteria community was correlated with the presence of both thymol and carvacrol (more specifically in the genotype

LSID104 where carvacrol is the main essential oil component). Because Rhizobium was the predominant genus detected within the Alphaproteobacteria community, we may BTSA1 ic50 assume that it can withstand the presence of the volatile components of the essential oil. The same postulation can be made for the genera Comamonas and Acidovorax because they Napabucasin nmr were only found in samples from leaves. In contrast, no specific grouping was observed when Actinobacteria were considered. Actinobacterial communities do not seem to be influenced drastically by plant location or the presence of the essential oil in the leaves of L. sidoides. It is well documented that Actinobacteria are particularly adapted to survival in harsh environments [43], which may explain why strains belonging to the genera Curtobacterium, Microbacterium, Brevibacterium and click here Corynebacterium were isolated in this study. Corynebacterium was the only actinobacterial genus found

in the leaves (genotype LSID105). When the fungal communities were evaluated, we also observed the influence of the part of the plant sampled on their structure, as previously demonstrated for bacteria. However, the DGGE profiles were more complex, and a greater diversity of genera was observed within the fungal communities. The phylum Ascomycota was prevalent among the different fungal taxa found. Similarly, Siqueira et al. [44] isolated endophytic fungi representing different species belonging to the groups Ascomycota, Coelomycetes and Hyphomycetes from L. sidoides Cham. In Hevea

brasiliensis (rubber tree), Gazis and Chaverri [45] observed fungal communities present in the leaves that were different many from those isolated from the stem. Ascomycota was also the prevalent fungal group found. Based on PCA, fungal communities were to some extent correlated with the presence of thymol in the leaves. Conclusion On the basis of the data from bacterial and fungal communities found in the leaves and stems of different genotypes of L. sidoides, we believe that both communities are selected by the conditions found in the interior of the plant. Thus, the presence of an essential oil with antimicrobial properties in the leaves certainly represents harsh survival conditions for the endophytic microorganisms. To understand how the microbial community associated with L. sidoides contributes to the physiology of the plant is the next step to be achieved. Acknowledgements This study was supported by grants from Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq), Coordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES) and Fundação de Amparo à Pesquisa do Estado do Rio de Janeiro (FAPERJ). References 1.

2% bovine serum albumin (BSA). Immunofluorescence assays Immunofluorescent staining was performed as previously described [6]. We used the primary antibodies mentioned above, and secondary antibodies were obtained

from Beyotime (Beyotime Institute of Biotechnology, Henan, China). Fluorescent selleck chemicals images were acquired with a fluorescence microscope (Olympus Corporation, Tokyo, Japan). Statistical analysis Data were expressed as mean ± standard error (SE). In the experiments involving protein expression, values are representative of three independent experiments. We used the χ2 and Fisher’s exact test to examine the association between protein expression levels and various clinicopathological parameters. Univariate analysis was performed using the Kaplan–Meier method, and statistical significance between survival curves was assessed by the log rank test. Bivariate correlations between study Protein Tyrosine Kinase inhibitor variables were calculated using Spearman’s rank correlation coefficients. Statistical analyses were completed with SPSS 11.0 (SPSS Inc., Chicago, IL, USA) and a P-value less than 0.05 was considered statistically significant. Results Upregulation of AQP3 and associated EMT-related

proteins predict poor prognosis for GC As shown previously, GC tissues expressed significantly higher levels of AQP3 relative to normal gastric mucosa (Table  2, Figure  1). Expression of E-cadherin was down-regulated in GC tissues with respect to normal mucosa (P < 0.05) (Table  2, Figure  1). Positive signals for nuclear vimentin JNK-IN-8 research buy were detected in 15.7% (14/89) of cases, with vimentin only expressed in carcinoma tissues that over-expressed AQP3 and lacked expression of E-cadherin. Vimentin expression was not detected in normal gastric glands (Figure  1). The correlation between clinicopathological features in GC patients

and expression of E-cadherin and vimentin was evaluated (Table  1). Elevated AQP3 expression in cancer tissues was associated with Lauren classification, lymph node metastasis, and lymphovascular BCKDHA invasion (P < 0.05). Lower levels of E-cadherin expression were closely related to depth of tumor invasion, lymph node metastasis, and lymphovascular invasion (P < 0.05). Vimentin expression was significantly associated with Lauren classification, depth of tumor invasion, and lymphovascular invasion (P < 0.05). Table 2 Expression of AQP3 and E-cadherin in GC tissues and corresponding normal gastric mucosa tissues Proteins Gastric cancer tissues Gastric normal mucosa tissues X 2 P-value AQP3       0.000   Positive 65 27 32.486   Negative 24 62   E-cadherin       0.000   Positive 35 62 16.515   Negative 54 27   Figure 1 Detection of AQP3, E-cadherin, and vimentin expression in GC tissue and adjacent normal tissue by IHC. Strong AQP3 immunoreactivity was identified in poorly differentiated adenocarcinomas. E-cadherin expression was observed in normal gastric glands but not in GC tissue.

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