The oxidation of the porous selleck screening library silicon matrix to silica decreases the effective refractive index, which causes a hypsochromic shift in the position of the maximum reflectance peak in the spectrum,

and the dissolution of the porous layer can both decrease the thickness of the layer and increase the porosity, both processes leading to a reduction in the effective optical thickness. Therefore, the PI3K inhibitor shifts in the Fabry-Perot interference fringe pattern observed in the visible reflectance spectra and the wavelength of the rugate peak maximum can be used to measure and compare the stability of different porous Si samples. The effective optical thickness of porous silicon samples can be obtained in real time using a fast Fourier transform of the reflectance spectra [1, 31]. One strategy to then compare the degradation of different porous Si surface samples

in aqueous media involves calculating the relative change in effective optical thickness defined as (2) where EOT0 is the value Selleckchem Avapritinib of EOT (Equation 2) measured when the porous Si surface is initially exposed to flowing buffer. The degradation of the pSi surface is then monitored by this relative decrease in optical thickness [32]. The degradation of the two porous Si sample types in the present study as measured by EOT changes is shown Figure 6. The data indicate that the stability of these samples decreases in the sequence: freshly etched porous Si > chitosan-coated pSi, since the initial rates of relative EOT change during the degradation are 0.217 and 0.37%/min, respectively. The degradation rate is higher for porous silicon coated by chitosan than for fresh pSi for the first 25 min, but there is a subsequent decrease in the degradation rate of the chitosan-coated sample so that at later times it degrades more slowly than fresh porous silicon, with relative EOT changes of 0.066 and 0.108%/min, respectively. The increased rate of degradation for the chitosan-coated porous silicon sample Ketotifen is in apparent contrast to the previously reported studies of chitosan-coated

porous silicon, however, those studies used hydrosilylated porous silicon or oxidized porous silicon [5, 23, 24]. The increased degradation of pSi-ch compared even to freshly etched porous silicon may be due to the amines present in chitosan, since amines can increase the rate of porous silicon hydrolysis [33, 34]. It also suggests that the chitosan layer contains cracks or fissures such that the aqueous solution readily infiltrates to the underlying fpSi layer. Figure 6 EOT changes observed during the degradation of the two porous Si sample types. Plots showing the relative change in the effective optical thickness (EOT) of the pSi samples as a function of time exposed to 1:1 (v/v) 0.5 M carbonate/borate buffer (pH 10), ethanol at 20 ± 1°C.

HH regulates embryonal patterning through gradients of its 3 isoforms, however, in some adult tissues HH is also responsible for homeostasis and has effects on cell proliferation and apoptosis. Most importantly, deregulated HH can also lead to cancer development [1, 22, 33] and cyclopamine, an inhibitor of the HH pathway, is able to reduce metastasis Selleckchem ATM Kinase Inhibitor [8, 9]. At 32˚C ts p53 adopts wt conformation and cells accumulate in G1 phase of the cell cycle. The ratio of cells in S phase was strongly reduced in all tested cells. The immortalized cells from young embryos (402/534) were

nearly completely arrested in G1 phase after 24 h at 32˚C, whereas the immortalized cells from older embryos (602/534) showed a reduction in S phase, but not in G2 phase pointing to a different regulation in both cell types. However, transformed cells

from oRECs showed a stronger response to the temperature shift. After shifting the cells back to 37˚C, transformed cells from oRECs re-entered the cell cycle much faster then buy EPZ-6438 transformed cells from yRECs. As expected, transformed cells entered the cell cycle more quickly than their immortalized counterparts. The most salient finding of our present work is the strong impact of the endogenous cell traits in o vs y RECs. Our results show that even strong oncogenes such as mutated c-Ha-RAS and mutated TP53 are not able to override the intrinsic cellular program. Taken together, our results show that MEK inhibitor transformed RECs from older embryos show a higher growth potential than their counterparts from yRECs and are less susceptible

to the action of CDK inhibitors. However, after inactivation of c-Ha-Ras with an inhibitor of farnesylation, also the transformed oRECs are strongly susceptible to growth inhibition by CDK inhibitors. If the phenotype of a certain tumor is known, this knowledge might help to develop a customized treatment for tumors with constitutively activated Ras. Acknowledgements The paper was partially AR-13324 datasheet supported by a grant from the Austrian Funding Agency FWF (P19894-B11). Open Access This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the original author(s) and source are credited. References 1. Berman DM, Karhadkar SS, Maitra A, Montes De Oca R, Gerstenblith MR, Briggs K, Parker AR, Shimada Y, Eshleman JR, Watkins DN, Beachy PA (2003) Widespread requirement for Hedgehog ligand stimulation in growth of digestive tract tumours. Nature. 425(6960):846–851PubMedCrossRef 2. Bernstein C, Bernstein H, Payne CM, Garewal H (2002) DNA repair/pro-apoptotic dual-role proteins in five major DNA repair pathways: fail-safe protection against carcinogenesis. Mutat. Res. 511(2):145–178PubMedCrossRef 3. Blagosklonny MV (2002) P53: an ubiquitous target of anticancer drugs. Int. J.

(2013) Factors driving plant rarity in dry grasslands on different spatial scales—a functional trait approach 28 dry grassland plant species Functional traits/species frequency and endangerment Traits associated with frequency and endangerment differ

on spatial scales Retain Belinostat research buy and support sheep grazing of dry grassland Avoid abandonment and fragmentation and enhance seed dispersal Comparison of species and traits between managed and unmanaged grasslands Moeslund et al. (2013) Topographically controlled soil moisture drives plant diversity patterns within grasslands Plant species richness and composition Local and regional scale Topographically controlled soil moisture plays an important role in shaping grassland plant diversity patterns both locally and regionally Consider soil moisture and its chemistry in conservation

planning, e.g. nitrogen compounds transported by water from upland arable fields Avoid planning of conservation activities in areas that does not feature optimal hydrology for grasslands Continuous monitoring of grassland restoration success Morris et al. (2013) Land use and host neighbor see more identity effects Prostatic acid phosphatase on arbuscular mycorrhizal fungal NVP-BEZ235 cost community composition in focal plant rhizosphere Arbuscular mycorrhizal fungi (AMF) Root colonization and community composition Increased mowing frequency alters AMF community composition. Increasing

frequency of mowing, grazing, and fertilization reduces AMF colonization of roots Consider how the frequency of mowing, grazing and fertilization will affect AMF, and limit these land uses when possible Increase AMF colonization of roots and stabilize AMF community composition Periodic monitoring of AMF root colonization and community composition Pipenbaher et al. (2013) Dry calcareous grasslands from two neighboring biogeographic regions: relationship between plant traits and rarity Dry grasslands Floristic and functional structure Ecologically similar meadows are not equally threatened Quick action is required when species composition start to change after abandonment Meadows, still in good conditions from physiognomic point of view, have already changed their plant composition.

Moreover, an increase of the dosage of somatostatin analogs seems to have a better control both of the disease progression and the chronic refractory diarrhea [24]. Somatostatin MK-8931 order analogues and interferon The combination of SSAs and interferon (IFN) has been used in an effort to enhance the antiproliferative effect of interferon therapy, to add the positive effect of SSAs on hypersecretory syndromes, and to reduce the dose of IFN and thus the number of IFN-related side-effects. Whether somatostatin analogues and IFN show a synergistic effect on tumour growth and in carcinoid syndrome symptom management is matter of debate. The combination therapy with somatostatin

analogues and IFN is MLN2238 mouse in BI2536 fact limited by the small number of trials, with variable results. This combination seems of benefit in patients where the usual octreotide treatment failed to achieve a biochemical and symptomatic control [93]. This combination therapy leaded to a significantly lower risk of progressive disease compared with somatostatin analogues alone, and had a higher median survival (51 vs 35 months) [94]. An anti-proliferative effect of the addition of α-interferon to octreotide was showed in a subgroup of patients with advanced metastatic disease unresponsive to octreotide monotherapy,

and prolonged survival was reported in the responder group [95]. However, most published data do not support a major effect of interferons over and above that of somatostatin analogues. In a prospective multicenter study on the effect of combination therapy, Faiss et al showed no advantage on either biochemical or antiproliferative results, while the number of side-effects increased [96]. Novel somatostatin analogues Recently the universal or “”pan-receptor”" somatostatin ligand pasireotide (SOM230) has been developed, which possess high affinity binding to SSTs 2, 3 and 5, moderate affinity for SSTR 1. Its receptor binding profile

is 30- Thalidomide to 40-times higher for SSTR 1 and SSTR 5 than octreotide. In a multicentre study on metastatic carcinoid tumours patients whose symptoms (diarrhoea and flushing) were refractory to octreotide-LAR, pasireotide at dosages between 450 μg and 1200 μg twice a day effectively controlled symptoms in 33% of these patients [97]. These results support the hypothesis that pasireotide may have potential in the treatment of these tumours. Subtypes of somatostatin and dopamine receptors may form homo- and hetero-dimers at the membrane level, and this receptor “”association”" may be induced by addition of either dopamine or somatostatin. Recently, subtype selective analogues and antagonists, as well as bi-specific and hybrid somatostatin/dopamine compounds, binding to SSTR 2, SSTR 5 and dopamine 2 receptors have been developed [98].

Further SEM investigations confirmed that these fractures and cracks have been formed during etching, but not due to the sample breaking for the SEM investigation. Slightly double bent, but isolated nanopillars were observed after etching

in the λ 3 solution (Figure 4e), while straight and short nanopillars were observed after etching in the λ 4 solution (Figure 4g). The Si nanopillars which formed after etching in the λ 1, λ 2, and λ 3 solutions possess nanoporous shells, and this can be clearly seen in the magnified SEM images (Figure 4b,d,f). It was also observed that the thickness of the shell increased from the bottom to the top of a pillar (Figure 4d,f). Figure 6 shows a cross-sectioned nanoporous Si nanopillar formed from the ATM Kinase Inhibitor molecular weight highly doped Si and a cross-sectioned Si nanopillar with nanoporous A-1210477 purchase shell formed from the lightly doped Si for comparison. Figure 4 SEM images of nanopillars formed from the lightly doped Si after 10-min etching. In (a, b) λ 1, (c, d) λ 2, (e, f) λ 3, and (g, h) λ 4 solutions. Panels b, d, f, and h show the cracked nanopillars. These cracks were formed during the breaking of the samples for the SEM investigations. Figure 5 SEM images of the fractured and

cracked Si nanopillars. (a) Formed from the highly doped Si after etching in λ 1 solution for 10 min, (b) from the lightly doped Si after etching click here in λ 2 solution for 10 min, and (c) from the lightly doped Si after etching in λ 1 solution for 10 min. Figure 6 SEM images of the cross-sectioned nanopillars. (a) Nanoporous Si nanopillars formed from the highly doped Si, and (b) Si nanopillars with solid core and nanoporous shell formed from the lightly doped Si after etching in λ 3 solution for 10 min. The pore size is clearly influenced by the doping level: around 10 nm of the nanoporous

nanopillars formed from the highly doped Si, and around 4 nm of the porous shells of the nanopillars formed from the lightly doped Si. The molar ratio λ has almost no influence on the pore size by formation of porous pillars in the highly doped Si. The pore size in Inositol monophosphatase 1 the porous shells formed in the lightly doped Si also almost does not change with molar ratio from λ 1 to λ 3. However, some chains of pores with relatively large pore size (around 10 nm) were formed in the lightly doped Si after etching in λ 4 solution for 10 min (Figure 4g,h). Some pores were also observed underneath the Au film (Figure 4g and the corresponding magnified image in Figure 7). This means that the pore formation for the lightly doped Si in the λ 4 solution is not homogenous, and in Figure 7, it is clearly seen that there are channels between the bundles of pores and the surface of the Au film. The pore formation is generally more active in the highly doped Si.

The cells were disrupted as observed microscopically to obtain total bacterial lysates that were centrifuged for 15 minutes at 13,000 rpm at 4°C. After centrifugation, the supernatant was harvested and considered as the soluble fraction of the bacterial cell lysate. The pellet was resuspended in PBS to reach the same volume as the supernatant, and was considered as the insoluble fraction. The soluble and insoluble fractions were then analysed by Western blot using polyclonal anti-DsRed antibodies

(Clontech Laboratories, Inc) recognizing the mCherry protein, as previously reported (16). Gel filtration The soluble fraction of bacterial lysate (500 μl) was injected into a HiPrep 16/60 Sephacryl S-500 HR column

(GE Healthcare). The calibration curve was obtained using thyroglobulin (669 kDa), apoferritin (443 kDa) and amylase (200 kDa). One milliliter fractions were collected and tested for the presence of the mCherry fluorochrome learn more using a fluorimeter equipped with a TxRed Ferrostatin-1 ic50 filter. Positive fluorescent fractions were then tested by Western blot analysis using anti-DsRed antibodies. Acknowledgements We thank Ariel B. Lindner for kindly providing the E. coli strain expressing the chromosomal ibpA-yfp fusion and Etienne Maisonneuve for fruitful discussions. This PF-01367338 datasheet work was supported by the FRFC (Collective Fundamental Research Fund, agreements 2.4521.04 and 2.4541.08) and by the University of Namur. C. Van der Henst and M. Deghelt held PhD fellowships from the FRIA (Industrial and Agricultural Research Training Fund). C. Charlier held a fellowship from the FRS-FNRS. Electronic supplementary material Additional file 1: Movement of IbpA-YFP in E. coli cells producing PdhS-mCherry. Time

lapse movie of E. coli cells at stationary (t12) phase, producing PdhS-mCherry (red) and IbpA-YFP (yellow). The over time interval between two pictures is 2 min. (AVI 7 MB) Additional file 2: Time course of PdhS-mCherry production and gel permeation analysis of soluble extracts. PdhS-mCherry recombinant protein is detected by Western blot in the soluble fraction of E. coli expressing pdhS-mCherry fusion, and in the insoluble fraction in cells at late stationary phase (Figure S1). Western blot and fluorescence were used to detect PdhS-mCherry in gel permeation fractions, and allow the identification of a single peak corresponding to this fusion (Figure S2). (PDF 413 KB) References 1. Speed MA, Wang DI, King J: Specific aggregation of partially folded polypeptide chains: the molecular basis of inclusion body composition. Nat Biotechnol 1996,14(10):1283–1287.PubMedCrossRef 2. Villaverde A, Carrio MM: Protein aggregation in recombinant bacteria: biological role of inclusion bodies. Biotechnol Lett 2003,25(17):1385–1395.PubMedCrossRef 3. Ventura S, Villaverde A: Protein quality in bacterial inclusion bodies. Trends Biotechnol 2006,24(4):179–185.PubMedCrossRef 4.

4 to .00156 mg ml-1 at 37°C for 1 h. The cells were peletted at 1,000 rpm for 10 min and the supernatant was collected to determine the absorbance at 450 nm using a UV Visible Spectrophotometer (Shimadzu). In negative control sets, erythrocyte suspension and PBS buffer was used whereas in positive controls, lysis buffer was used for completely

lysing the erythrocytes. The percentage haemolysis was calculated and plotted against the concentration of ACP to determine the dose cytotoxic to human erythrocytes. The percentage of intact erythrocytes was calculated using the following formula. Haemagglutination activity assay In view of the findings that dialyzed concentrate exhibits haemagglutination Selleck CH5183284 activity [72], a serial 2-fold dilution of a solution of ACP (6.4 to 0.0001 mg ml-1) was added in microtitre plates, wherein 100 μl was mixed with 100 μl of a 2.0% suspension of human red blood cells in PBS (pH 7.2) at 20°C. The results were observed after BMS-907351 molecular weight about 1 h when the blank without

dialyzed concentrate was fully sedimented to inspect whether the red blood cells had agglutinated in response to the antifungal protein. Amino acid sequencing The corresponding GF120918 supplier Protein band that showed the zone of inhibition against Candida albicans was electro blotted to a 0.45 μm Immobilon-P transfer membrane (Millipore). After blotting at 100 mA for overnight, the membrane was removed carefully from the cassette, washed three times with MilliQ water to remove glycine, and then stained for 30 sec with a freshly prepared solution of 0.1% Coomasie

brilliant blue R-250 in 40% methanol and 1.0% acetic acid. The blot was then destained in 50% methanol until bands were visible and background clear. The PVDF membrane was then dried sandwiched between clean tissue papers. The stained band of interest was tightly cut out and washed six times in MillQ water and subjected to Edman degradation. The N-terminal sequencing Fenbendazole was performed on a Protein sequencer, Model 494 Procise (Applied Biosystems, USA) with 140 C analyzer at Protein Sequencing Facility, IOWA State University, USA. The primary amino acid sequence obtained was entered into BLAST to search for peptides with similar sequences. Mass spectrometry The purified antimicrobial peptide was analyzed by matrix-assisted laser desorption and ionization–time of flight mass spectrometry by using a 4000 Q TRAP Mass Spectrometer (Proteomics International, Nedlands Australia) equipped with an ion source with visualization optics and an N2 laser (337 nm). Protein samples were trypsin digested and peptides extracted according to standard techniques [73]. All digestion reactions were done in 50 mmol NH4HCO3 (pH 8.5) at room temperature and with an enzyme-to-peptide ratio of 1:40 (wt/wt). Peptides were analyzed by electrospray ionisation mass spectrometry using the Ultimate 3000 nano HPLC system [Dionex] coupled to a 4000 Q TRAP mass spectrometer (Applied Biosystems) with a capillary cap voltage of 1,750 V.

Mutat Res 1997, 379:33–41.PubMedCrossRef 21. Goel A, PARP signaling Nagasaka T, Arnold CN, Inoue T, Hamilton C, Niedzwiecki D, Compton C, Mayer RJ, Goldberg R, Bertagnolli MM, Boland CR: The CpG Island methylator phenotype and chromosomal instability are inversely correlated in sporadic colorectal cancer. Gastroenterology 2007, 132:127–138.PubMedCrossRef

22. Leong KJ, Wei W, Tannahill LA, Caldwell GM, STI571 concentration Jones CE, Morton DG, Matthews GM, Bach SP: Methylation profiling of rectal cancer identifies novel markers of early-stage disease. Br J Surg 2011, 98:724–734.PubMedCrossRef 23. Moon JW, Lee SK, Lee JO, Kim N, Lee YW, Kim SJ, Kang HJ, Kim J, Kim HS, Park SH: Identification of novel hypermethylated genes and demethylating effect of vincristine in colorectal cancer. J Exp Clin Cancer Res 2014, 33:4.PubMedCentralPubMed

24. Bardhan K, Liu K: Epigenetics and colorectal cancer pathogenesis. Cancers (Basel) 2013, 5:676–713.CrossRef 25. Kane MF, Loda M, Gaida GM, Lipman J, Mishra R, Goldman H, Jessup JM, Kolodner R: Methylation of the hMLH1 promoter correlates with lack of expression of hMLH1 in sporadic colon tumors and mismatch repair-defective human tumor cell lines. Cancer Res 1997, 57:808–811.PubMed 26. Fu D, Calvo JA, Samson LD: Balancing repair and tolerance of DNA damage caused by alkylating agents. Nat Rev Cancer 2012, 12:104–120.PubMedCentralPubMed 27. Lavin MF: Ataxia-telangiectasia: from a rare disorder to a paradigm for cell signalling Docetaxel mw and cancer. Nat Rev Mol Cell Biol 2008, 9:759–769.PubMedCrossRef 28. Shiloh Y: ATM and related protein kinases: safeguarding genome integrity. Nat Rev Cancer BKM120 2003, 3:155–168.PubMedCrossRef 29. Huebner K, Saldivar JC, Sun J, Shibata H, Druck T: Hits, Fhits and Nits: beyond enzymatic function. Adv Enzyme Regul 2011, 51:208–217.PubMedCentralPubMedCrossRef 30. Wali A: FHIT: doubts are clear now. Scientific World Journal 2010, 10:1142–1151.PubMedCrossRef 31. Al-Temaimi RA, Jacob S, Al-Ali W, Thomas DA, Al-Mulla F: Reduced FHIT expression is associated

with mismatch repair deficient and high CpG island methylator phenotype colorectal cancer. J Histochem Cytochem 2013, 61:627–638.PubMedCrossRef 32. Portela A, Esteller M: Epigenetic modifications and human disease. Nat Biotechnol 2010, 28:1057–1068.PubMedCrossRef 33. Herreros-Villanueva M, Muñiz P, García-Girón C, Cavia-Saiz M, Del Corral MJ: TAp73 is one of the genes responsible for the lack of response to chemotherapy depending on B-Raf mutational status. J Transl Med 2010, 8:15.PubMedCentralPubMedCrossRef 34. Allocati N, Di Ilio C, De Laurenzi V: p63/p73 in the control of cell cycle and cell death. Exp Cell Res 2012, 318:1285–1290.PubMedCrossRef 35. Murphy CG, Moynahan ME: BRCA gene structure and function in tumor suppression: a repair-centric perspective. Cancer J 2010, 16:39–47.PubMedCrossRef 36.

In particular, addition of T14-DSF or C15-DSF decreased the MIC of gentamicin against B. cereus from 8.0 μg/ml to 0.0625 μg/ml, which represents a 128-fold difference selleck inhibitor (Figure 1A). Similarly, addition of DSF and related molecules to B. cereus culture also enhanced the bacterial susceptibility to kanamycin from 2- to 64-fold with T14-DSF showing the strongest synergistic activity (Figure 1B). Interestingly, kanamycin is also an aminoglycoside that interacts with the 30S subunit of prokaryotic

ribosomes and inhibits protein synthesis. Compared to the strong synergistic effect on gentamicin and kanamycin, DSF and related molecules showed only moderate effects on rifampicin, addition of these molecules increased the antibiotic sensitivity of B. cereus up to 4-fold (Figure 1C). Different from gentamicin and kanamycin, buy Fosbretabulin rifampicin inhibits the DNA-dependent RNA polymerase in bacterial cells, thus preventing gene transcription to generate RNA molecules and subsequent translation to synthesize proteins. Table 1 Chemical structure of DSF signal and its derivatives used in this study Compound Configuration Structure References T8-DSF trans 14 T10-DSF trans 14 T11-DSF trans 14 T12-DSF trans 14 T13-DSF trans 14

T14-DSF trans 14 T15-DSF trans 14 C8-DSF cis 14 C10-DSF cis 14 C11-DSF cis 14 C12-DSF cis 22 DSF cis 14 C13-DSF cis This study C14-DSF cis 14 C15-DSF cis 14 S12-DSF NT This study selleck Figure 1 Synergistic activity

of DSF and its structurally related molecules (50 μM) with gentamicin (A), kanamycin (B), and rifampicin (C) against B. cereus . For each antibiotic, a series 2-fold dilution was prepared for determination of MIC with or without DSF or related molecule. Data shown are means of two replicates and error bars indicate the standard deviations. The differences between the samples with addition of 50 μM DSF or related molecule and control are statistically significant with *p < 0.05, **p < 0.01, ***p < 0.001, as determined by using the Student t test. The synergistic activity of DSF and its structurally related molecules with antibiotics on B. cereus is dosage-dependent Megestrol Acetate To determine whether the synergistic activity of DSF with antibiotics is related to its dosages, DSF was supplemented to the growth medium at various final concentrations, and MICs of gentamicin and kanamycin against B. cereus were tested. The results showed that activity of DSF signal on B. cereus sensitivity to gentamicin and kanamycin was dependent on the final concentration of the signal molecule (Figure 2A). Addition of DSF at a final concentration from 5 – 50 μM increased the antibiotic susceptibility of B. cereus to gentamicin by 2- to 16-fold, respectively (Figure 2A). Similarly, as shown in Figure 2A, combination of different final concentrations of DSF signal with kanamycin increased the synergistic activity by 1.3- to 16-fold.

Participants Students were recruited in September 2005 via invitation/information

letters sent home by the teachers. Written consent was obtained from parents/guardians; children gave verbal and written assent. In all, 1494 students consented to participate in the study at baseline. selleck chemicals Of those, 1441 students were measured (n = 52 students were absent and n = 1 moved prior to being measured). The 1421 children who completed the question regarding their participation in organized sport that was part of the Physical Activity RGFP966 nmr Questionnaire for Children (PAQ-C) were included in the analysis. Measurement procedures Descriptive characteristics Stretched stature to the nearest 0.1 cm (Seca 214 Portable Stadiometer) and weight to the nearest 0.1 kg (Conair digital electronic scale) were each measured twice and the mean was used in the analysis. Body Mass Index

Vactosertib nmr (BMI) was calculated from height and weight as kg/m2. Overweight/obesity was calculated using age and BMI [12]. Dietary measures Two instruments were used to assess the diet of each participant. The EHSA Food Processor Nutrition and Fitness Software (v. 10.0, Salem, OR) was used to determine macronutrients (also including total calories, fibre and sugar) consumed from a validated 24-hour dietary recall [13]. As well, fruit, vegetables, milk, 100% fruit juice, sports drinks and SSBs (including flavoured milk, carbonated beverages, non-carbonated flavoured beverages, sweetened coffee and tea, and sports beverages) were hand-tallied from the dietary

recall, with serving size determined using the Canadian Nutrient File [14]. Typical frequency of fruit, vegetable, milk and 100% fruit juice consumption was assessed using a targeted Food Frequency Questionnaire (FFQ) adapted from the US National Cancer Institute’s National Institutes of Health: Eating at America’s Table Study Quick Food Scan [15]. Physical activity Physical activity and participation in organized sport was measured using a modified version for of the PAQ-C [16]. The PAQ-C is a valid and reliable tool for assessing moderate-to-vigorous physical activity (PA) over the previous 7 days [16, 17]. The physical activity score (PA score) ranges from 1 (low active) to 5 (high active) and was calculated from the mean score of nine questions related to frequency and intensity of PA. In addition, students were asked if they participated in organized sport outside of school and then to describe the sport activity and indicate the days they participate in that sport during the week. Those who reported participation in any organized sport and identified the sport and participation frequency were assigned to the ‘sport’ group and those who did not were assigned to the ‘non-sport’ group.