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of cases (control group) Control group: retrospective 17 (10) 7 (none) 14 (none) 8 (none) 16 (none) 11 (none) Primary disease (no. of cases) FSGS (14/9) MCNS(3/1) MN (3) MCNS(2) IgAGN (1) FSGS (14) PSL

resistant FSGS(6) MCNS (1) MN + FSGS (1) FSGS (13) MN (3) FSGS (11) PSL, click here CyA resistant No. of Treatment 2/w × 3 1/w × 6 Total 12 2/w × 3 1/w × 7 Total 13 2/w × 3 Total 6 2-13 7.3 (average) 2/w × 3 Total 6 2/w × 3 1/w × 6 Total 12 Concomitant treatment (no. of cases) PSL 1.0 mg/kg none (4) PSL(1) PSL + CyA (2) PSL 0.8 mg/kg PSL/pulse 1.0 mg/kg PSL (14) immunosuppressant (10) PSL 1.0 mg/kg Clinical efficacy Remission 9 Partial remission 4 no effect 4 Remission 2 Partial remission 4 no effect 1 Responded 8 no effect 6 Remission 4 Partial remission 1 no effect 3 Improved 7 Unchanged 3 Worsened

3 unjudgemental 3 Remission 5 Partial remission 2 Efficacy rate 76 % 86 % 57 % 63 % FSGS 54 % 76 % Summary Reduced remission induction period Increased serum albumin Increased serum albumin Effective in younger age Amelioration of ApoB deposition BMN 673 price in glomerulus 5 in 6 cases >50 % reduction of proteinuria in 9 cases Effective in PSL resistant juvenile patients Acknowledgments The author would like to thank Drs. Soichi Sakai, Masatoshi Mune, Tsutomu Hirano, Motoshi Hattori, Kenjiro Kimura, Tsuyoshi Watanabe, Hitoshi Yokoyama, Hiroshi Sato, Shunya Uchida, Takashi Wada, Tetsuo Shoji, Tsukasa Takemura, Yukio Yuzawa, Hiroaki Oda, Kiyoshi Mori, and Takao Saito for their support as members of the click here Japanese Society of Kidney and Lipids. The author also thanks Drs. Hitomi Miyata, Mari Maeda, and Hiroyuki Matsushima for their contributions to patient

care and related studies. Conflict of interest There is no conflict of interest in the preparation and submission of this manuscript. Open AccessThis article is distributed under the terms of the Creative Commons Attribution License which permits any use, distribution, and reproduction in any medium, provided the original author(s) and the source are credited. References 1. Sulowicz W, Stompor T. LDL-apheresis and immunoadsorption: novel methods in the treatment of renal diseases refractory to conventional therapy. Nephrol Dial Transplant. 2003;18:v59–62.PubMedCrossRef 2. Moorhead JF, Chan MK, El-Nahas M, et al. Lipid nephrotoxicity in chronic progressive glomerular and tubulo-interstitial disease. Lancet. 1982;2(8311):1309–11.PubMedCrossRef 3. Ong AC, et al. Tubular lipidosis: epiphenomenon or pathogenetic lesion in human renal disease? Kidney Int. 1994;45:753–62.PubMedCrossRef 4. Sakurai M, Muso E, Matsushima H, Ono T, Sasayama S. Rapid normalization of interleukin-8 production after low-density lipoprotein apheresis in steroid-resistant nephrotic syndrome. Kidney Int Suppl. 1999;71:S210–2.PubMedCrossRef 5. Savin VJ, McCarthy ET, Sharma M. Permeability factors in focal segmental glomerulosclerosis.

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region of the main S fimbrial operon. Microb Pathog 2009, 46:150–158.PubMedCrossRef 25. Meissner A, Wild V, Simm R, Rohde M, Erck C, Bredenbruch F, Morr M, Romling U, Haussler S: Pseudomonas aeruginosa cupA-encoded fimbriae expression is regulated by a GGDEF and EAL domain-dependent modulation of the intracellular level of cyclic diguanylate. Environ Microbiol 2007, 9:2475–2485.PubMedCrossRef 26. Rosen DA, Pinkner JS, Jones JM, Walker JN, Clegg S, Hultgren SJ: Utilization of an intracellular bacterial community pathway in Klebsiella pneumoniae urinary tract infection and the effects of FimK on type 1 pilus expression. Infect Immun 2008, 76:3337–3345.PubMedCrossRef 27. Old DC, Corneil I, Gibson LF, Thomson AD, Duguid JP: Fimbriation, pellicle formation and the amount of growth of salmonellas in broth. J Gen Microbiol 1968, 51:1–16.PubMedCrossRef 28. Ryjenkov DA, Simm R, Romling U, Gomelsky M: The PilZ domain is a receptor for the second messenger c-di-GMP: The

PilZ domain protein YcgR controls motility in enterobacteria. J Biol Chem 2006, 281:30310–30314.PubMedCrossRef 29. Wilksch JJ, Yang J, Clements A, Gabbe JL, Short KR, Cao HW, Cavaliere R, James CE, Whitchurch CB, Schembri MA, et al.: MrkH, a novel c-di-GMP-dependent transcriptional activator, controls Klebsiella pneumoniae biofilm formation by regulating type Cobimetinib supplier 3 fimbriae expression. PLoS Pathogens 2011,7(8):e10002204.CrossRef 30. Yeh KS, Tinker JK, Clegg S: FimZ binds the Salmonella typhimurium fimA promoter region very and may regulate its own expression with FimY. Microbiol Immunol 2002, 46:1–10.PubMed 31. Saini S, Pearl JA, Rao CV: Role of FimW, FimY, and FimZ in regulating the expression of type 1 fimbriae in Salmonella enterica serovar Typhimurium. J Bacteriol 2009, 191:3003–3010.PubMedCrossRef 32. Romling U, Gomelsky M, Galperin MY: c-di-GMP: the dawning of a novel bacterial signalling system. Mol Microbiol 2005, 57:629–639.PubMedCrossRef

33. Weinhouse H, Sapir S, Amilcam D, Shilo Y, Volman G, Ohana P, Benziman M: c-di-GMP-binding protein, a new factor regulating cellulose synthesis in Acetobacter xylinum. FEBS Lett 1997, 416:207–211.PubMedCrossRef 34. Bokranz W, Wang X, Tschape H, Romling U: Expression of cellulose and curli fimbriae by Escherichia coli isolated from the gastrointestinal tract. J Med Microbiol 2005, 54:1171–1182.PubMedCrossRef 35. Simm R, Morr M, Kader A, Nimtz M, Romling U: GGDEF and EAL domains inversely regulate cyclic di-GMP levels and transition from sessility to motility. Mol Microbiol 2004, 53:1123–1134.PubMedCrossRef 36. Tamayo R, Pratt JT, Camilli A: Role of cyclic diguanylate in the regulation of bacterial pathogenesis. Annu Rev Microbiol 2007, 61:131–148.

The experimental traces in general represent the averages of three samples each illuminated once. The simulation

and fitting of the experimental polyphasic fluorescence induction curve with its algorithmic representation F FIA(t) was done with dedicated optimization routines. The fit parameters (rate constants, heterogeneity, fraction, etc.) of the simulation curve F FIA(t) were estimated after application of dedicated routines provided by appropriate software (Mathcad 13, MathSoft, Inc. Cambridge, MA, USA) which calculates the parameter values (vector) for which the least mean square function is minimal, where NN is the number of data points (in most experiments NN ≥50). Reduction of data points was in some cases purposely applied U0126 chemical structure for F FIA(t) curves to facilitate better comparison with the experimental curve F exp(t). Analysis with fluorescence induction algorithm It has been shown (Vredenberg and Prásil 2009; Vredenberg 2011) that

the variable fluorescence during the OJ phase in the 0.01–1 ms time range is nearly exclusively, if not completely due to the release of primary photochemical quenching q PP and is represented by F PP(t) with $$ F^\textPP selleck products (t) = 1 + nF_\textv \cdot q^\textdsq (t) \cdot [(1 - \beta ) \cdot \frack_\textL k_\textL + k_\textAB + \beta \cdot (1 + (1 - e^ - \phi k_\textL t ) \cdot e^ - k_2\textAB t )] $$ (1)in which nF v (=F m STF −F o)/F o) is the normalized variable fluorescence, \( q^\textdsq (t) = 1 – \texte^ – k_\textL t , \) β is the fraction of QB-nonreducing Leukocyte receptor tyrosine kinase RCs, Φ(0 ≤ Φ < 1)is an efficiency factor for energy trapping in semi-closed QB-nonreducing RCs, and k L, k AB, and k 2AB are the rate constants of light excitation and of oxidation of the single- and double-reduced primary quinone acceptor QA of PSII, respectively. Similarly it was shown that the variable fluorescence during the JI phase in the 1–30 ms time range is nearly exclusive due to the release of photoelectrochemical quenching q PE and is in approximation represented by F PE(t) with $$ F^\textPE (t) = 1 + nF_\textv \cdot

\ [1 - f^\textPPsc (t)] \cdot [1 - e^ - k_\textqbf \cdot t ] \cdot \frack_\textqbf k_\textqbf + k_\textHthyl + 1\ \cdot [1 - e^ - k_\textqbf \cdot t ] \cdot \frack_\textqbf k_\textqbf + k_\textHthyl $$ (2)in which f PPsc(t) is the fraction of semi-closed RCs containing QA − (see for definitions and equations Vredenberg 2011), k qbf is the rate constant attributed to that of the change in pH at the QA − QB redox side of PSII (related to the actual rate constant of proton pumping by the trans-thylakoid proton pump), and k Hthyl the actual passive trans-thylakoid proton leak (conductance). For the experiments presented in this article changes in k qbf and k Hthyl will be of prime importance to be considered.

This is a very valuable technique for porous materials [16–20] and has already been successfully applied to PSi for the study of cyclic oxidation [21, 22]. Methods PSi layers were prepared by electrochemical etching in the dark of n +-doped (100)-oriented crystalline Si wafers having 3 to 7 mΩ/cm resistivity from Siltronix (Archamps, France). The etched bulk

Si surface area is about 0.9 cm2. The etching solution was HF/H2O/ethanol in a 15/15/70 proportion, respectively, and the etching current density was 50 mA/cm2 in all cases. HF being an extremely hazardous material (e.g., see [23]), all precautions have been taken to ensure the safety of the persons involved in the porous samples preparation. GDC 0199 The Er doping was performed in constant current configuration with current densities in the 0.01 to 2.2 mA/cm2 range using a 0.11 M solution

of in EtOH. EIS measurements and Er doping processes were always performed with the same electrochemical cell used for the PSi formation. The Er solution used was also the same in both cases. The EIS measurements were made in the galvanostatic regime (GEIS) using a constant bias current in the 0.01 to 1 mA range, a frequency range from 100 kHz to 100 mHz, and an AC amplitude of 2 to 10 μA, depending on the bias current intensity. All electrochemical processes were performed using a PARSTAT 2273 potentiostat by Princeton Applied Research (Oak Ridge, TN, USA). A schematic of the cell used for the experiments can be found in [14]. Spatially resolved energy Cytoskeletal Signaling inhibitor dispersive spectroscopy (EDS) measurements for quantitative Er content determination were Niclosamide carried out using a JEOL JED 2300 Si(Li) detector in a scanning electron microscope (SEM) JEOL JSM 6490-LA (JEOL Ltd., Akishima, Japan) equipped with a W thermionic electron source and working at an acceleration voltage of 15 kV. The fitting of the reflectivity spectra was performed using the SCOUT software from W. Theiss Hard- and Software (Aachen, Germany). Results and discussion Optical characterization The presence of Er within the PSi pores induces

a modification of the optical response of the material that is correlated to the amount of Er present in the layers [14]. To gain information about the modifications of the PSi/Er doping process as a function of the doping current intensity, we performed a series of reflectivity measurements on samples where we transferred, using different current intensities, equal amounts of charge during the electrochemical process. We have then fitted the reflectivity spectra, using the SCOUT software, to obtain the variation of the optical thickness following the Er doping. Each sample has been measured before and after the doping process, so that the results are independent on small differences in the thickness from one sample to another.

Real-time PCR were performed on Stratagene Mx3000P PCR machine with the following settings: 95°C for 10 min, followed by 40 cycles of 95°C for 15 sec and 60°C for 1 min. The mutant and wild-type alleles were amplified separately, and the levels of each mutation in the sample were calculated by normalizing to standard curves. The mutation ratio was defined as [mutation ratio % = level of mutants/(level of

mutants + level of wild type allele) × 100%]. Statistical analysis Statistical analysis was carried out using SPSS version 16.0 software (SPSS Inc., Chicago, IL, US). Fisher’s exact test was used to analyze whether the different categories had LDE225 mouse different positive rates. Kappa test was used to analyze whether the two sampling regions had consistent outcomes. Wilcoxon matched pairs test was used to compare the mutation ratios from the two regions. Two-sided p < 0.05 was considered statistically significant. Results EGFR mutations in primary tumors and metastases Of the 50 cases of NSCLC that had EGFR Barasertib purchase mutations in primary tumors, exon 19 mutations (in-frame deletions only) were present

in 28 cases (56%), and exon 21 (L858R point mutations only) mutations were detected in 22 cases (44%). Mutations in exon 19 and 21 were mutually exclusive and no multiple mutations were found. Of the metastases samples, 47 were positive for EGFR mutation (94% concordance with the detection in primary tumors), and exon 19 and exon 21 mutations were detected in 26 cases (55%, 93% concordance) and 21 cases (45%, 95% concordance), respectively. Notably, all cases presented the same mutation type in the matching primary and metastatic tumors. EGFR mutation detection and the clinical characteristics were listed in Table 1. Among the 50 subjects, only 3 (6%) had different test results for EGFR mutations in primary tumor and metastases, however, the difference

was Rolziracetam insignificant (P = 0.242) as analyzed by Fisher’s exact test. EGFR mutations at different sites of primary tumors of the same patient We performed quantitative measurement of EGFR mutations at different sites of primary tumors (Table 2). The median mutation deviation for different primary sites (see footnote of Table 2 for the formula of calculation) was 18.3% (with a range of 0.0% ~ 54.3%), indicating that the results of the quantitative measurement of EGFR mutations in different sites of primary tumor in the same patient have a high level of concordance. Table 2 Quantitative measurement of EGFR mutation ratios in 3 primary tumor sites and one metastases of the same patient ID Mutation ratio (%) in different primary tumor sites Mutation ratio (%) of metastases 1 2 3 Median Deviation (%)* E001 85.9 91.1 80.1 85.9 12.8 <10 E002 39.1 25.9 44 39.1 49.8 41 E003 <10 <10 <10 <10 0.0 <10 E004 82.

As shown in Figure 2, proliferation of splenocytes stimulated with the 8-epitope mixture (mix2) was more click here significant comparing to single-epitope phages or 4-epitope mixture of OmpL1 or LipL41 alone (mix1). Evaluation of cytokine secretion in splenocytes induced by OmpL1- or LipL41-derived epitopes ELISA assay was employed to determine the in vitro polarization of

T helper cells. Cells from both OmpL1- and LipL41-immunized mice released large amount of IFN-γ but not IL-4 comparing to cells from PBS control mice (Figure 3). OmpL1173-191 epitope showed the strongest activity of stimulation, and other three OmpL1 epitopes showed similar abilities in the stimulation of IFN-γ secretion. Among the LipL41 epitopes, the secretion of IFN-γ in the cell cultures was induced by LipL41181-195, LipL41233-256 and LipL41263-282 to the similar level; all of them were stronger than LipL4130-48. When the 4 epitopes of OmpL1 were pooled together to stimulate the splenocytes, the secretion of IFN-γ cytokine in the splenocyte supernatants was mildly increased. Phages expressing each epitope of LipL41 failed to stimulate the secretion of IFN-γ or IL-4 (Figure 3B). Figure 3 Cytokine profiles of T cells from mice spleen. Splenocytes from recombinant Trichostatin A in vivo OmpL1 (A) or LipL41

(B) immunized mice were isolated 10 days after the last immunization and were stimulated with epitopes from corresponding proteins in vitro for 72 hours. Mix stand for the data from the epitope mixture of OmpL1 or LipL41 stimulating the splenocytes from OmpL1- or LipL41- immunized mice. Each value is representative of 3 mice in triplicates. Discussion Leptospira interrogans causes disease in both animals and humans throughout the world. Leptospirosis in humans may be fatal due to the involvement of severe damage to multiple organs such as liver, lung, kidney and brain and is an increasing concern to the public health [24].

L. interrogans can rapidly disseminate to multiple organs to induce programmed cell death [25, 26]. The essential properties of a vaccine are safe, immunogenic, and effective in the prevention of leptospiral infection at both acute and carrier these state. It has been a challenge to develop an effective and safe L. interrogans vaccine [27]. The currently available vaccines include multiple-valence inactivated leptospiral vaccine and subunit leptospiral vaccines [28]. However, these vaccines often have serious adverse effects [29]. And more importantly, most recombinant protein vaccines used against Leptospira in animals are serovar-specific and therefore their efficacy is limited when Leptospira of a different serovar is circulating [30]. The current emphasis in research laboratories is to discover conserved antigens that may induce long term protection across the species or serovars of Leptospira.

In all treatment conditions the highest amount of sulfide was produced

by Cyanidioschyzon, especially when cells were supplemented with sulfate during metal exposure and even more when also pretreated with extra sulfate (Figure 2B; p < 0.05). Similar trends also occurred but not to the same degree in Chlamydomonas (Figure 2A; p < 0.05). The highest amounts of metal sulfide production were 3.5 (approx. 64 fold increase) and 1.2 μmol per mg protein (approx. 4 fold increase) for Cyanidioschyzon and Chlamydomonas, respectively. ICG-001 concentration The cyanobacterium Synechococcus in the sulfate pretreated cells produced a much lower amount of metal sulfide at 0.48 μmol per mg protein (approx. 3.5 fold increase) and this required 48 h to become significantly different from the control. However, this species was exposed to only 2 μM Cd(II), one fiftieth that of the other species because it is not as tolerant to cadmium. In contrast to the two eukaryotic algal species, the cyanobacterium also made similar amounts of metal sulfides during sulfite treatments. No species made significantly more sulfide as a product of cysteine supplementation after 48 h, although Synechococcus did make significantly more after 24 h. Figure 2 Cadmium induced sulfide formation at 0 (grey), 24 (cross-hatched) and 48 h (black) for Chlamydomonas reinhardtii (A) and Cyanidioschyzon merolae (B) in 100 μM Cd(II), and Synechococcus leopoliensis

(C) in 2 μM Cd(II). Means and SE (n = 4). An asterisk indicates significantly greater than the respective Cd(II) containing control (p < 0.05). Serine acetyltransferase and O-acetylserine(thiol)lyase coupled activity Each species had significantly different initial Gefitinib in vitro SAT/OASTL activities under control conditions (ANOVA, p < 0.05; Figure 3). Exposure to Cd(II) enhanced the activity of coupled SAT and OASTL over controls with no added metal after

48 hrs to 2.0, 1.7, and 3.2 fold in Chlamydomonas (Figure 3A), Cyanidioschyzon (Figure 3B), and Synechococcus (Figure 3C), respectively. This treatment Metformin molecular weight also resulted in the highest enzyme activities in each of the species. The only other Cd(II) treatments that were higher than the controls in all three species were the simultaneously sulfate fed, and the pre- and simultaneously sulfite fed cells. The pre- and simultaneously cysteine-fed Chlamydomonas and Synechococcus had the lowest activities (ANOVA, p < 0.05), although this was not the case for Cyanidioschyzon. In the latter species the treatments with the lowest activities did not differ from the control, and the pre- and simultaneously cysteine-fed cells were significantly different from the control (ANOVA, p < 0.05). Figure 3 Effect of cadmium on coupled serine acetyl-transferase and O -acetylserine(thiol)lyase activity in Chlamydomonas reinhardtii (A), Cyanidioschyzon merolae (B), and Synechococcus leopoliensis (C) exposed to 100, 100, and 2 μM Cd(II), respectively, when supplemented with sulfur containing compounds.

The protein content was determined according to Bradford’s method (Bradford 1976), with bovine serum albumin used as a standard. Protein samples (30 μg) were boiled with 2 Gamma-secretase inhibitor × sample buffer containing 5% β-mercaptoethanol for 5 min, separated by size on 15% polyacrylamide gel under SDS denaturing conditions, and transferred to a nitrocellucose membrane at 90 V for 2 h. The nitrocellulose membranes were stained with ponceau S to assess the efficiency of transfer. Non-specifi c binding was blocked by incubation in block buffer (5% non-fat dry milk, 0.05% Tween-20, 1 × tris-Cl-buffered saline) overnight at 4°C, The membranes were hybridized

with mouse monoclonal antibody recognizing SMAD4 (sc-7966, Santa Cruz Biotechnology, Inc., Santa Cruz, CA),

then incubated with a horseradish peroxidase-labeled goat anti-mouse IgG (1: 500). The bound secondary antibody was detected by enhanced chemiluminescence (Amersham Life Science, Little Chalfont, UK). Housekeeping protein β-actin was used as a loading control. Positive immunoreactive bands were quantified densitometrically (Leica Q500IW image analysis system) and expressed as ratio of SMAD4 to β-actin in optical density units. 2.5 Statistical analysis Caspase inhibition All computations were carried out using the software of SPSS version13.0 for Windows (SPSS Inc, IL, USA). The rank sum test was used to analyze the ranked data. The measurement data were analyzed by one-way ANOVA. Randomized block design ANOVA was used to analyze the statistical difference among different tissue types. In the analysis of glioma morbidity for all patients, we used the Kaplan-Meier estimator and univariate Cox regression analysis to assess the marginal effect of each factor. The differences between Phospholipase D1 groups were tested by log-rank analyses. The joint effect of different factors was assessed using multivariate Cox regression. A Spearman’s analysis was carried out to analyze the correlation between SMAD4

mRNA and protein expression levels. Differences were considered statistically significant when p was less than 0.05. 3. Results 3.1 SMAD4 protein levels in glioma tissues by immunohistochemistry assay and survival analysis SMAD4 expression was studied in a total of 252 glioma specimens of which 113 were low grade glioma (grade I and II) and 139 were high grade (grade III and IV). About 42 specimens taken from normal brain tissue served as control group. Based on immunohistochemistry analysis, positive staining for SMAD4 was mainly observed in the cytoplasm and to a lesser degree in the nuclei of cancer cells. The representative photographs were shown in Figure 1. Among the glioma specimens, 138 (54.8%) glioma specimens were positively stained, and 114 (45.2%) glioma specimens were negatively stained.

66, 1.69 and 1.48 in comparison to animals fed the control diet on days 2, 5 and 9 post infection, respectively (p < 0.05). Animals fed the 20% rice bran diet showed a reduction in Salmonella fecal shedding by a log10 value check details of

2.13, 1.69, 2.04 and 1.73 in comparison to the animals fed the control diet on days 2, 5, 7 and 9, respectively. No significant difference was observed in Salmonella fecal shedding between the 10 and 20% rice bran diet groups. These data demonstrate that pre-feeding dietary rice bran for one week reduced the susceptibility of mice to oral infection with the Salmonella pathogen as measured by fecal shedding. Figure 1 Effect of dietary rice bran on Salmonella fecal shedding of mice. Fecal shedding was examined in Salmonella infected animals fed control, 10% and 20% rice bran diet for 3 weeks (one week prior and 2 weeks post challenge). Data are shown as mean ± standard deviation of mean

log10 CFU per gram of feces (n = 5 mice/diet group), and data are representative of three independently conducted experiments. Repeated measures ANOVA and post hoc Tukey’s test were applied. Significance is shown by * (P < 0.05) and ** (P < 0.01). Effect of dietary rice bran on serum cytokines Previous research demonstrated that in response to primary Salmonella infection, the host immune system releases massive amounts of the cytokines MG-132 purchase such as TNF-α, IFN-γ and IL-12 locally and systemically [24]. The local inflammatory response has been shown to shift the microbiota composition allowing Salmonella the opportunity to efficiently colonize in the gut [25]. Therefore, due to the fact that rice bran mediated a decrease in fecal shedding, we next measured the cytokine level

in the serum of mice consuming either the 10 or 20% rice bran diets (Figure 2). Mice fed the 10% rice bran diet for 7 days had decreased serum levels of TNF-α, IFN-γ, and IL-12 by 60.4, 136.3 and 27.6 pg/ml respectively in comparison Nintedanib (BIBF 1120) to animals on the control diet (p < 0.05). Additionally, mice fed the 20% rice bran diet showed decreased levels of serum IFN-γ in comparison to control animals (p < 0.05). These data suggests that rice bran induced suppression of systemic cytokine production may play a role in reducing the colonization of Salmonella. Figure 2 Effect of dietary rice bran on serum TNF- α, IFN-γ and IL-12 levels in Salmonella infected mice. Blood was drawn at days 0, 7 and 14 following Salmonella infection and serum was analyzed for TNF- α (A), IFN-γ (B) and IL-12 (C) levels in control, 10% and 20% rice bran diet groups. Data are shown as mean ± standard deviation of mean (n = 3 mice/diet group). Significance was measured by two-way ANOVA and Bonferroni post hoc test. Effect of dietary rice bran on fecal Lactobacillus spp Members of the genus Lactobacillus are potent commensal bacteria with potential for eradication of Salmonella infection [26].