Soluble proteins were purified from bacterial lysates by glutathione-affinity chromatography

as previously described [29], then analysed by sodium-dodecyl-sulphate (SDS) polyacrylamide gel electrophoresis (PAGE). GST-fused proteins from inclusion bodies (insoluble fraction) were dissolved in a CAPS buffer (CAPS 50 mM, DTT 1 mM and Sarkosyl 0.3%), hence denaturing the proteins [30]. The dissolved and denatured protein was dialyzed overnight against 20 mM Tris–HCl pH 8.5. Insoluble proteins dissolved in CAPS buffer/dialysed are referred CT99021 to as ‘CAPS-denatured proteins’ throughout the text. Purified proteins were quantified by two different methods: (i) a Bradford assay at 595 nm and (ii) UV spectrophotometry at 280 nm (extinction coefficient determined from aa sequences of each fusion protein). Concentration measurements were consistent using both methods. Relative amounts of proteins to be injected were based on copy number considerations in a BTV particle, as determined by X-ray crystallography (780 copies for VP7, 360 copies for VP5 and 180 copies for VP2 [1]). Seven

groups of six Balb/c mice were injected subcutaneously at days 0, 14 and 28 with 100 μl of soluble protein/Montanide ISA 50V emulsion (Table 1). Three groups of six Balb/c mice were injected subcutaneously at days 0, 14 and 28 with 100 μl of CAPS-denatured protein/Montanide ISA 50V emulsion (Table 1). A group of six Balb/c mice were injected subcutaneously at days 0, 14 and 28 each with 100 μl of Zulvac-4® Bovis. Sera were used for normalisation of ELISA results. A group of six control Balb/c mice which were not immunised with any of the antigens was click here also included. Six groups of six IFNAR−/− mice were injected subcutaneously at days 0, 14 and 28 with: a mixture of VP2 Bay 11-7085 domain 1 (VP2D1) and VP2 domain 2 (VP2D2) in Montanide, then challenged with (i) BTV-4 or (ii)

BTV-8; or a mixture of VP2D1 + VP2D2 + VP5Δ1–100/Montanide, then challenged with (iii) BTV-4 or (iv) BTV-8; or a mixture VP2D1 + VP2D2 + VP5Δ1–100 + VP7/Montanide, then challenged with (v) BTV-4 or (vi) BTV-8 (Table 1). Blood samples were collected at day 0 and day 28. The mice received an intravenous lethal [31] challenge on day 40, with 103 pfu of BTV-4-italy03 (homologous-challenge), or 10 pfu of BTV-8-28 (heterologous-challenge). Blood was collected on the day of challenge (day 40), then at days 2, 3, 4, 5, 7, 10 and 12 p.i. Sera were tested for anti-VP2, anti-VP5 and anti-VP7 antibodies by ELISA and immunofluorescence and for NAbs by PRNT. Two groups of six IFNAR−/− mice were injected subcutaneously with VP5Δ1–100 on days 0, 14 and 28. These groups were not challenged with BTV-4 or BTV-8. Two additional groups of six IFNAR−/− mice were immunised with VP7 on days 0, 14 and 28, then challenged at day 40 with either BTV-4 or BTV-8. Two groups of non-immunised mice were used as positive controls, to confirm lethality of BTV-4 or BTV-8 challenge-strains.

After embedding in paraffin Selleckchem Bosutinib wax, thin sections of 5 μm thickness of liver tissue were cut and stained with haematoxylin–eosin. The thin sections of liver were made into permanent slides and examined23 under high resolution microscope with photographic facility and photomicrographs were taken as shown in Fig. 5, Fig. 6 and Fig. 7. Results were presented as mean ± S.D and total variation present in a set of data was analysed through one-way analysis of variance (ANOVA). Difference among means had been analysed by applying Tukey’s multiple comparison test at 95% (p < 0.05) confidence

level. Calculations were performed with the GraphPad Prism Program (GraphPad Software, Inc., San Diego, USA). The effect of aqueous extract of S. cumini seed on blood glucose levels is shown in Fig. 1. The mean level of glucose in the control group of mice was evaluated to be 74.33 ± 7.31 mg/dl (range 65–85) whereas it was 222.5 ± 22.52 mg/dl (range values 198–250) in alloxanized group. After the treatment of mice with the seed extract of S. cumini the glucose level decreased down to 91 ± 7.82 mg/dl having a range of 82–99 mg/dl. These variations in glucose concentrations are evident from Fig. 1. The significant increase in glucose concentration in the diabetic animals BGB324 clinical trial than that of the control mice is evident on alloxanization. However, the oral administration

of aqueous extract of S. cumini significantly reduced the glucose level in serum when compared with alloxan induced diabetic mice. In Control group

of mice SGOT activity was found to be 25 ± 5.06 IU/ml having the range of 20–32 IU/ml. In diabetics, its activity got raised to 50 ± 6.87 IU/ml with values ranging from 40 to 59. However, extract treatment of this group for three weeks resulted in decrease of SGOT activity to 35.83 ± 5.98 having values ranging from 25 to 41 IU/ml. These variations are depicted by the box-plot in Fig. 2. In control mice group SGPT activity was found to be 20.71 ± 4.96 having range values between 15 and 26.54 IU/ml which got raised to 53.83 ± 6.70 (range values 45–63) IU/ml in diabetic mice. However, after the treatment of mice with the seed extract of S. cumini, the activity decreased down to 30.83 ± 4.87 (ranging between 25 and 38) IU/ml. These values are Liothyronine Sodium compared by the box-plot as evident in Fig. 3. Bilirubin level of control mice was observed to be 0.53 ± 0.054 mg/dl (values ranging between 0.44 and 0.60) which got increased to 0.82 ± 0.093 mg/dl in alloxan induced diabetic mice. Bilirubin contents ranged from 0.70 to 0.90 in diabetic mice. However, after the treatment of diabetic mice with the seed extract of S. cumini, the bilirubin level decreased down to the mean value of 0.65 ± 0.053 having values ranging from 0.59 to 0.72 mg/dl. These variations along with statistical significance are depicted by box-plot as shown in Fig. 4.

In the final step various boronic acids were coupled with 4-bromo-3,5-diarylisoxazole derivative using Suzuki condition and microwave irradiation to afford 3,4,5-triarylisoxazole (6) derivatives [Scheme 1]. The obtained yields of final compounds are mentioned in Table 1. click here All reagents were purchased from Aldrich and used

as received. Dry THF, Ethanol, Toluene were supplied by Spectrochem. All chemistry was performed under a nitrogen atmosphere using standard techniques. All the NMR spectra were measured using either Bruker AMX 400 instrument with 5 mm PABBO BB-1H tubes. 1H and 13C NMR spectra were measured for approximately 0.03 M solutions in d6-DMSO at 400 MHz with TMS as internal reference. The IR spectra were measured as potassium bromide pellets using a Perkin–Elmer 1600 series FTIR spectrometer. LCMS were obtained using Agilent 1200 series LC and Micro mass zQ spectrometer. Column chromatography was performed Selleck C646 using a silica gel (230–400 mesh). To a solution of 2,4-difuororbenzaldehyde (25.0 g, 176.05 mmol) in THF/Water (1:1, 400 mL) was added NaHCO3 (29.5 g, 351.19 mmol)

in one lot. Hydroxylamine hydrochloride7 (24.5 g, 352 mmol) was added portion wise and then RM was stirred at RT for 2 h. RM was diluted with diethyl ether (200 mL) and the organic layer was separated, washed with water and saturated brine solution, dried over Na2SO4, evaporated under reduced pressure. Yield Methisazone of the product was 26.0 g (94%) as white solid. M. pt: 127.9–129.2 °C. Mol. Wt: 157.12; LCMS: 158.3(M++1). 1H NMR

(CDCl3, 300 MHz) δ 8.33(s, 1H), 7.69(m, 1H), 6.89(m, 2H). 13C NMR (CDCl3, 300 MHz): 165.6, 162.77, 159.2, 143.5, 128.2, 116.18, 112.26, 104.65. To a solution of 2,4-difluorobezaldehyde oxime (25.0 g, 159.23 mmol) in dichloromethane/aqueous 10% NaHCO3 (3:2, 500 mL), was added bromine8 (25.5 g, 159.37 mmol) drop wise at 0 °C. Once the bromine colour disappeared, styrene was added at 0 °C and then the RM was stirred at RT for 12 h. The organic layer was separated, washed with saturated brine solution, dried over Na2SO4, evaporated under reduced pressure. Crude product was triturated with petroleum ether; solid obtained was filtered and dried. Yield of the product was 36.0 g (87.3%) as white solid. M. pt: 66.6–67.7 °C. Mol. Wt: 259.25, LCMS: 260.1 (M+1). 1H NMR (CDCl3, 400 MHz); δ 7.92(m, 1H), 7.36(m, 5H), 6.97(m, 1H), 6.89(m, 1H), 5.76(q, J = 5.26 Hz 1H), 3.85(m, 1H), 3.45 (m, 1H). 13C NMR (CDCl3, 300 MHz): 165.6, 162.77, 159.2, 152.16, 140.59, 130.33, 128.77, 125.86, 112.34, 104.66, 82.86, 44.63. To the solution of 3-(2,4-difluorophenyl)-5-phenyl-4,5-dihydroisoxazole (25.0 g, 96.52 mmol) in carbon tetrachloride (300 mL) was added N-bromosuccinimide9 (25.0 g, 140.45 mmol), in one lot at RT and then reaction mass was heated to 80 °C for 5 h.

“
“Urology Practice focuses on clinical trends, challenges and practice applications in the four areas of Business, Health Policy, the Specialty and Patient Care. Information that can be used in everyday practice will be provided to the Urology community via peer-reviewed clinical practice articles (including best practices, reviews, clinical guidelines, select clinical trials, editorials and white papers),

“research letters” (brief original studies with an important clinical message), the business of the practice of urology, urology health policy issues, urology education and training, as well as content for urology care team members. Contributions from all sub-specialty societies within urology as well as those outside of urology will be considered. Original work published in Urology http://www.selleckchem.com/products/erastin.html Practice includes primary clinical practice articles and addresses a wide array of topics categorized as follows: Business of Urology – articles address topics such as practice operations and opportunities, risk management, reimbursement (Medicare,

Medicaid and private insurers), contracting, new technology and financial management. Health Policy – articles address topics such as organization, financing and delivery of health care services from governmental and private payer policy perspectives, governmental and legislative activities influencing urology care, government affairs and policy analyses. the Specialty – articles Isotretinoin address topics such as education and training, ABU certification, implementation of clinical guidelines and best practices

across all sub-specialty societies within urology and all specialty areas Trichostatin A outside urology relative to contributions to the practice of urology. Patient Care – articles address topics such as treatment choices, best practices, reviews, detailed analysis of clinical guidelines, evidencebased quality of care, select clinical trials, clinical implications of basic research, international health care and content for urology care team members. All communications concerning editorial matters should be sent to: Urology Practice The Journal is organized into the four aforementioned major areas of clinical practice. Authors should indicate the most appropriate category for each manuscript during the submission process. Please indicate if it is not clear which category applies to your manuscript. The editors may re-categorize your manuscript after acceptance. Authors must submit their manuscripts through the Web-based tracking system at https://www.editorialmanager.com/UP. The site contains instructions and advice on how to use the system, guidance on the creation/scanning and saving of electronic art, and supporting documentation. In addition to allowing authors to submit manuscripts on the Web, the site allows authors to follow the progression of their manuscript through the peer review process.

The latter step is a concentration gradient-driven process, see more influenced by the drug molecular characteristics and impeded by diffusional resistances of the microchannels and the tissues beneath [20] and [25]. In a recent study, we reported on the effect of MN array characteristics and application variables on the

in vitro transdermal delivery of Rh B encapsulated in PLGA NPs across full thickness MN-treated porcine skin [10]. In the present work, we aimed at providing more knowledge on the contribution of characteristics of nanocarrier and encapsulated dye to MN-mediated transdermal delivery of nanoencapsulated R428 dyes. The skin model used was full thickness porcine ear skin (approximately 1164 μm-thick), a well-established model representing full skin resistance and possessing characteristics similar to those of human skin [35]. Rh B or FITC-loaded NPs prepared at a relatively high emulsion homogenization speed (15,000 rpm)

with 1% w/v DMAB were generally monodisperse with PDI < 0.2 and positively charged due to adsorption of the cationic surfactant. Zeta potential values exceeded 30 mV (36.1–67.6, Table 1), indicating physical stability [36]. This was obvious in TEM images of sample NPs (Fig. 3). FITC NPs prepared with PVA as emulsion stabilizer were negatively charged (−4.5 mV, Table 1). Reduction in the particle size of 20% w/w Rh B-loaded PLGA 50:50 NPs (F1–F3) in the range 422.3–155.2 nm (Table 1) resulted in a significant increase in permeation of Rh B across MN-treated skin (Fig. 4). For instance, a 2.7-fold reduction in the mean diameter of F3 compared to F1 NPs led to a fivefold increase in Q48. It has been demonstrated that permeation characteristics of a NP through microchannels were significantly affected by NPs size relative to the pore size [37]. As the width

of MN-created microchannels is usually in the micron range [23], that is, significantly larger than the size range of test NPs in the present study, and NPs size dependence of Rh B skin permeation can be explained by faster release of the encapsulated the water soluble Rh B from smaller size NPs with larger surface to volume ratio. Particle size is a factor known to affect drug release from polymeric NPs [38]. Further, translocation of PLGA NPs across full thickness human abdominal skin was shown to be NPs size dependent, despite the larger microchannel size [22] and [23]. Combined findings suggest deeper and more extensive influx of smaller NPs through MN-created channels leading to enhanced transdermal delivery of the water soluble dye released at the deeper NPs deposition sites.

Reactogenicity of the formulations containing pneumococcal proteins alone (dPly and dPly/PhtD) was low, and generally in a similar range as previously reported

for other investigational pneumococcal protein vaccines containing dPly [23], PhtD [24] or a combination of PhtD and pneumococcal choline-binding protein A (PcpA) [25]. Initial immunogenicity assessments in this small group of adults showed an increase in anti-PhtD and/or anti-Ply antibody GMCs following each investigational vaccine dose. Coadministration of dPly with PhtD did not negatively affect anti-Ply antibody responses. There was a trend toward higher anti-Ply SCH727965 chemical structure antibody GMCs for dPly/PhtD than for dPly alone. Our results thus confirm the immunogenicity of both antigens, in-line with previous studies [26] and [27], and suggest that PhtD enhances the anti-Ply immune response. One prospective study reported an increase over time in the levels of natural antibodies against five pneumococcal proteins (including PhtD and Ply) in young children with nasopharyngeal colonization and acute otitis media [26]. Adults have been shown to have circulating memory CD4+ T cells that can be stimulated by PhtD, Ply and other protein vaccine candidate antigens [27].

Young children have a more limited response, indicating that their vaccination would likely require several priming doses to stimulate CD4+ T-cell responses [27]. Before vaccination, all participants already had anti-Ply and anti-PhtD antibody concentrations above the assay cut-off. This Autophagy Compound Library molecular weight Carnitine dehydrogenase high pre-vaccination seropositivity rate most likely reflects previous pneumococcal exposure. In infants and toddlers, increases in naturally-acquired antibody levels against several pneumococcal protein surface antigens

(including PhtD) and Ply have been reported with increasing age (from 6 months to 2 years) and exposure (nasopharyngeal carriage, acute otitis media) [26], [28], [29] and [30]. Otitis-prone children and children with treatment failure of acute otitis media also mount a lower IgG serum antibody response to pneumococcal proteins [31]. Several studies have indicated a protective role of naturally acquired anti-Ply antibodies [32], [7] and [33], while antibodies against PhtD prevent pneumococcal adherence to human airway epithelial cells [16]. The presence of these antibodies, as seen in our participants, could thus be contributing to the protection of healthy young adults against pneumococcal disease. Our immunogenicity results must be interpreted with caution due to the small number of participants and the fact that protective levels of antibodies to pneumococcal proteins have not yet been determined. Additionally, our study was performed in adults aged 18–40 years; these results serve as a safety assessment before progressing to a pediatric population but may not reflect the safety, reactogenicity and immunogenicity data from other age groups.

The above findings show that ROS plays an active role in TNF-α release and NFkB activation. Our present study gives the supporting evidence for the induction and activation of NFkB in group II. Present work support Tung et al and Khan et al work.17 and 18

It was found that NFkB expression and TNF-α release was attenuated substantially by BP treatment thus reducing inflammatory response implicated in 5-FU induced renal toxicity. Selleck PD0325901 To summarize we found that BP ameliorated molecular targets implicated in the toxicity of 5-FU administration in animal model. Hence further investigations need to be done to be made useful for human use. The authors are thankful to UGC, New Delhi India under SAP of Departmental Research Support Vemurafenib chemical structure II and BSR for the award of project to carry out the study. All authors have none

to declare. “
“N-acyl sulfonamides and carbamates are important synthetic building blocks towards the synthesis of bio-active molecules. 1, 2 and 3N-acyl sulfonamide moiety is a common structural moiety and has emerged as an important feature for biological activity in drug synthesis. Several recently developed drugs, including therapeutic agents for Alzheimer’s disease, 4 inhibitors for tRNA synthetase as antibacterial agents 5 and prostaglandin Fla sulfonamides for the potential treatment of osteoporosis, 6 were incorporated these moieties and acyl sulphonamides are known as Anti-Proliferative agents. 7 Similarly, N-acyl carbamates have undergone a rapid development as pesticides 8 and 9 and pharmaceuticals 10 due to the discovery of their biological activity. Furthermore N-acylation of sulfonamides and carbamates is an important transformation since it affords products of significant potential for use in biological applications as described. 11 and 12 This transformation is also a useful tool for lead optimization and lead generation. 13 and 14 Despite the extensive number of Lewis acid-catalyzed acylations of protic nucleophiles such

as alcohols, amines and thiols, 15 and 16 the N-acylation of less nucleophilic sulfonamides and carbamates has not received much attention. To our knowledge there are only a few reports in the literature describing the N-acylation of sulfonamides and carbamates under acidic medium. 17 However, strong acidic conditions, Isotretinoin namely, concentrated H2SO4 (3 mol%) or Fe-exchanged Montmorillonite K-10 or HBr/AcOH and higher temperature (60 °C) are typically needed to achieve conversion. Thus, the investigation of other Lewis acids as efficient catalysts under mild reaction conditions is required for this transformation. General experimental procedure for N-acylation of sulfonamides and carbamates: To a mixture of sulfonamide (1.0 mmol) and anhydride (1.5 mmol), 5 mol% of anhydrous CeCl3 was added and the reaction was stirred for the given time (see Table 1 for N-acylation of sulfonamides and Table 2 for N-acylation of carbamates).

ATP-sensitive K+ channels were inhibited by including 5 mM Mg-ATP in the pipette solution. All chemicals including the www.selleckchem.com/products/17-AAG(Geldanamycin).html (+)MK801 and (−)MK801 enantiomers were purchased from Sigma Chemical. We used the conventional whole-cell configuration of the patch clamp technique to record membrane currents and Em

by using an EPC8 (HEKA, Mahone Bay, Canada) patch clamp amplifier. Data were digitized using custom-built software (R-clamp, by Dr. Ryu SY) at a sampling rate of 5 kHz, low-pass filtered at 1 kHz, and then stored on a computer. Voltage pulse generation was also controlled using R-clamp software. Patch pipettes were pulled from borosilicate capillary tubes (Clark Electromedical Instruments, Pangbourne, UK) by using a PP-83 puller (Narishige, Tokyo, Japan). We used patch pipettes with a resistance of 2–4 MΩ when filled with the pipette solution listed above. Recordings were started 4–6 min after establishing the whole-cell configuration to allow adequate cell dialysis of the pipette solution. The liquid–liquid junction potential between the NT and pipette solutions (calculated from ion mobilities) was approximately −4.5 mV PARP inhibitor at 25 °C. This junction potential was not corrected for when analyzing data. Therefore, the true Em values might be 4–5 mV more negative (hyperpolarized) than those reported here. All experiments were conducted at room temperature

(20–25 °C). Origin 6.0 software (Microcal Software, Inc., Northampton, MA, USA) was used for data analysis. Half-inhibition concentration (IC50) and Hill coefficients (n) were obtained by fitting concentration–response data to the Logistic function in the Origin software. Activation kinetics was calculated by fitting the data to a single exponential. The time course of current inactivation was also fitted to a single exponential function. Steady-state activation curves were fitted with the following Boltzmann equation: y = 1/1 + exp (−(V−V1/2)/k),where k is the slope factor, V is the

test potential, and V1/2 is the voltage at which half-maximal conductance is obtained. The steady-state voltage dependence of inactivation was investigated using a double-pulse voltage protocol; peak currents were measured by applying a of 250-ms test potential to +40 mV, and 10-s preconditioning pulses were varied from −60 to +50 mV (in 10-mV steps) in the presence and absence of MK801. The resulting steady-state inactivation data were fitted to the following Boltzmann equation: y = 1/[1 + exp (V− V1/2)/k],where V is the preconditioning potential, V1/2 is the potential corresponding to the half-inactivation point, and k is the slope value. The results are shown as means ± SEM. Paired or independent Student’s t tests were used to test for significance as appropriate, and P < 0.

An extrarenal pelvis should be in a surgeon’s differential for abdominal masses when imaging is not conclusive in the contrary. “
“Augmentation cystoplasty using an intestinal tract is indicated for patients with a deterioration of bladder storage function resistant to pharmacologic or other conservative interventions. For example, patients with LY2109761 neurogenic

bladder caused by spinal cord injury, contracted bladder caused by urogenital tuberculosis, or interstitial cystitis are candidates for augmentation cystoplasty. Malignant transformation of primary or substitutional bladder epithelium after augmentation cystoplasty is rare and needs a long postoperative period.1 However, these malignant tumors are frequently aggressive www.selleckchem.com/products/Cyclopamine.html and associated with a poor prognosis,2 and the mechanisms of carcinogenesis are unclear. We previously reported a case of a 62-year-old woman with tubulovillous adenoma that developed 44 years after ileocystoplasty.3

Two more years later, she developed bladder adenocarcinoma. The adenoma-carcinoma sequence has been implicated in the multistep processes of intestinal carcinogenesis in colon cancer.4 To the best of our knowledge, this is the first case report to provide histopathologic evidence of the adenoma-carcinoma sequence in the bladder after augmentation cystoplasty. A 16-year-old female patient underwent right nephrectomy for renal tuberculosis. Augmentation ileocystoplasty for tuberculosis contracted bladder was performed at 18 years. Left nephrostomy was required at 38 years because of hydronephrosis and repeated pyelonephritis. In March 2005, 44 years after ileocystoplasty, the patient presented at our hospital with gross hematuria. Cystoscopy revealed MYO10 multiple papillary tumors in the region of the ileovesical anastomosis. Transurethral resection of the bladder tumor (TURBT) was performed. Histopathologic examination revealed tubulovillous adenoma (Fig. 1A). The tumor recurred 4 times, necessitating repeated TURBT in April 2005, November 2007, March 2008, and October 2008. Histopathologic diagnosis was tubulovillous adenoma at the

second TURBT in 2005, but the diagnosis of well-differentiated adenocarcinoma, pTa, (Fig. 1B) was made at the third TURBT in 2007, 46 years after ileocystoplasty. The fourth and fifth TURBT also revealed well-differentiated adenocarcinoma. In January 2009, radical cystectomy with ileal conduit diversion was performed because of incomplete resection during the fifth TURBT. Macroscopic findings (Fig. 2A) and histologic examination (Fig. 2B) revealed that the tumor developed around the region of ileovesical anastomosis. Histopathologic diagnosis was well-differentiated adenocarcinoma, pTa, u-rt0, u-lt0, ur0, ew0, ly0, v0, pN0 (Fig. 2B). The postoperative course was uneventful, and the left nephrostomy catheter was removed.

, 2012 and Cohen et al.,

2013). In addition to individual-level tray data, the aggregated waste was bagged and weighted using a calibrated scale. All data were collected by trained observers using standardized forms (see Fig. 1). Two members of the team, masters-level health educators with experience working with schools, were permanent members across all schools. Between two and four additional members, trained graduate student interns or the principal investigators, were also present during data collection. The permanent members received training on the detailed study protocol from a Ph.D.-level former food service director INCB018424 prior to any data collection. The permanent members then trained the additional members by having them shadow them for a day prior to letting them collect plate waste data. The study protocol and all study materials were reviewed and approved by the University of California, Los Angeles and the Los Angeles County Department of Public Health Institutional Review Boards prior to

field implementation. Food production record data and plate PD-1/PD-L1 inhibitor 2 waste data were linked using descriptions of the food items served for the specific date and lunch service period. When discrepancies in items served were found between the two data sources, the stock descriptions from the plate waste data were used. For the purposes of the study, the analysis focused only on fruit and vegetable waste as the outcomes of interest. For each school, production and plate waste values were pooled across the five day observation period. The number of entrées served was used as a proxy for the number of meals served. Descriptive statistics of production waste (percent of food items prepared but never served) were analyzed by food type (fruit or vegetable). Two Linifanib (ABT-869) values were calculated using the plate waste

data: 1) whether or not the student took the item(s) and, 2) among students who took the item(s), the amount of food that was eaten, dichotomized as to whether the student ate any of the item(s) or threw the item(s) away without eating a single bite. Missing data, as a result of students removing identification numbers from their lunch trays or disposing of their lunch waste outside of the cafeteria, were included in the denominator when calculating percentages. Fruit and vegetable plate waste were also analyzed by race/ethnicity and sex. In addition to descriptive statistics, four simple logistic regression analyses, adjusted for school-level clustering, were performed to examine differences in consumption among sexes and race/ethnicities. The logistic regressions tested (separately) for differences between males/females and races (Latinos, African-Americans, or other) on: a) whether students selected the fruit/vegetable item, and b) whether the student ate any of the fruit/vegetable item. All analyses were performed using Stata version 12.1 (StataCorp LP, College Station, Texas).