8, were added to the medium. All cultures were mixed using a magnetic stirrer. Escherichia coli strains were grown in LB medium or on agar plates containing LB medium and antibiotics of interest at 37°C. RNA and DNA isolation N2-fixing cell cultures were harvested in room temperature for DNA isolation as previously described [5] with the exception that 2 M instead of 3 M of NaAc was used. RNA

was extracted from both N2-fixing and non N2-fixing cultures by centrifugation of the cells (4,500 × g for 10 in) in room temperature followed by resuspension in 1 ml TRIzol reagent (Sigma). The cells were then disrupted with 0.2 g of acid washed 0.6-mm-diameter glass beads by using a Fast-prep (Precellys®24) at a speed of 5.5 for 3 × 20 s, keeping the samples on ice in between runs. Phases were separated by centrifugation selleck chemicals llc at 15,000 × g for 10 min at 4°C and the cleared solution was then transferred to new tubes and incubated at room temperature for 5 min. 0.2 ml of chloroform were added

to the samples which were thereafter gently turned by hand for 15 s followed by DNA Damage inhibitor a 2 min incubation at room temperature. The samples were then centrifugated at 15,000 × g for 15 min at 4°C and the upper obtained liquid phase was transferred to new tubes. The precipitation of the RNA was performed by adding 0.25 ml isopropanol and 0.25 ml of salt solution (0.8 M Sodium citrate and 1.2 M NaCl) followed by incubation

at room temperature for 10 min. The RNA was then collected by centrifugation 15,000 × g for 10 min at 4°C and washed with 75% ethanol before treatment with DNase I (GE Healthcare) in 20 μl Dnase buffer (40 mM EPZ015938 in vivo Tris-HCl, 6 mM MgCl2, pH 7.5) for 30 min at 37°C. A phenol: chloroform extraction was performed and the RNA was precipitated in 2.5 volume of ice-cold ethanol (99.5%) and 0.2 volume of cold LiCl (10 M). After precipitation Mirabegron at -20°C over night the samples were centrifuged at 20,000 × g, washed and resuspended in DEPC-treated distilled H2O. Identification of transcriptional start points (TSP) TSP studies were performed using RNA from N2-fixing cultures and the “”5′RACE System for Rapid Amplification of cDNA Ends”" kit (Invitrogen) according to manual. Resulting bands were cloned into the pCR 2.1-TOPO vector (Invitrogen) and transformed into DH5α competent cells, all according to instructions from the manufacturer. The obtained vectors were purified by the “”Genelute Plasmid Mini-prep Kit”" (Sigma-Aldrich) followed by sequencing (Macrogen Inc). In the case of hoxW in Nostoc PCC 7120, the primers used for the reactions were modified and designed according to the TAG-method [66] and only the first of the two nested PCRs described in the “”5′RACE System for Rapid Amplification of cDNA Ends”" kit manual was performed (Table 1). Table 1 Primers used in this study.

Immediately after arrival at the finish line, the identical measurements were repeated. Between the pre-race and post-race measurements, the athletes selleck chemicals recorded their intake of food and drinks using a prepared paper

and pencil. At each of the 17 aid station they noted both the kind and the amount of ingested food and fluids. At these aid stations, liquids and food were prepared in a standardized manner, i.e. beverages and food were provided in standardized size portions. The drinking cups were filled to 0.2 L; the energy bars and the fruits were halved. The athletes also recorded additional food and fluid intake provided by their support crew, as well as their intake of salt tablets and other supplements. The compositions of fluids and solid food were estimated using a food table [35]. Statistical analysis Data are presented as mean and standard deviation (SD). Selleckchem HDAC inhibitor Pre- and post-race results

were compared using paired t-test. Pearson correlation analysis was used to check for associations between the measured and calculated parameters. Statistical significance was accepted with p www.selleckchem.com/Wnt.html < 0.05 (two-sided hypothesis). Results Seventy-six of the 80 subjects completed the 100-km ultra-marathon within 731 (130) min, running at an average speed of 8.4 (1.4) km/h. Their training and previous experience is presented in Table 1. Four subjects failed to finish the 100-km race due to overuse injuries of the lower limbs and were withdrawn from the study. Table 2 shows the pre- and post-race measurements and their changes. Body mass decreased significantly by 1.8 (1.4) kg from 76.1 (9.8) kg pre-race to 74.3 (9.9) kg post-race (p < 0.0001), representing a 2.4% decrease in body mass. The volume of the foot remained unchanged (p > 0.05). In detail: in 20

runners, the foot volume increased, in 18 runners the volume showed no change and in 38 runners foot the volume decreased Phosphoglycerate kinase (Figure 1). Table 2 Results of the physical, haematological and urinary parameters before and after the race.   Pre-race* Post-race* Absolute change* Percent change* p-value** Body mass (kg) 76.1 (9.8) 74.3 (9.9) -1.8 (1.4) -2.4 (1.8) < 0.0001 Volume of the right foot (mL) 1,118 (225) 1,073 (227) -45 (201) -2.7 (18.2) > 0.05 Haematocrit (%) 44.8 (3.3) 43.6 (2.9) -1.2 (2.7) -2.3 (5.8) 0.0005 Plasma [Na+] (mmol/l) 137.0 (2.7) 138.6 (2.6) +1.6 (3.1) +1.2 (2.3) < 0.0001 Urine specific gravity (g/ml) 1.015 (0.008) 1.024 (0.008) +0.009 (0.008) +0.87 (0.79) < 0.0001 * n = 76, mean and (SD), ** by paired t-test Figure 1 Range of changes in foot volume. Haematocrit decreased (p = 0.0005), plasma volume increased by 5.3% (11.9) and urine specific gravity increased (p < 0.0001). Plasma [Na+] increased significantly (p < 0.0001) by 1.2% from 137.0 (2.7) mmol/l to 138.6 (2.67) mmol/l, with a mean difference of 1.6 (3.1) mmol/l. Pre-race, 10 subjects showed plasma [Na+] < 135 mmol/L with values between 131 mmol/L and 134 mmol/L.

Taken together, these observations suggest

structural and functional similarities Selleckchem WH-4-023 between BMAA0649 and members of the Oca family of autotransporters. Hence, we designated this ORF of B. mallei ATCC23344 boaA (B urkholderia Oca-like adhesin A ). Table 1 lists characteristics of the boaA gene and its encoded product. Figure 1 Structural features of the boaA and boaB gene products. Different regions of the predicted B. mallei ATCC23344 BoaA (A), B. pseudomallei K96243 BoaA (B) and B. pseudomallei K96243 BoaB (C) proteins are depicted with the positions of residues defining selected domains. The horizontal brackets outline selected regions of the BoaA and BoaB proteins and the percent identity between these regions is learn more shown below the brackets. Transporter modules (OM anchors) and helical linkers were identified using the PSIPRED secondary structure prediction algorithm. The colored boxes show the relative position and number of repeated SLST motifs. Table 1 Characteristicsa PCI-34051 of boaA and boaB genes and their encoded products Strain Gene Chromosome Locus tag GenBank accession # ORF (nt) Predicted protein (aa) MW (Da) Potential signal sequence cleavage siteb B.mallei                    ATCC23344 boaA 2 BMAA0649 YP_105401.1 4608 1535 140,689 WA18▼GV    NCTC10247 boaA 2 BMA10247_A1776 YP_001078959.1 5301 1766 162,744 WA77▼GV B. pseudomallei

                   K96243 boaA 2 BPSS0796 YP_110805.1 4962 1653 151,565 WA18▼GV    DD503 boaA ND – EF423807 4680 1559 143,209 WA18▼AL    1710b boaA 2 BURPS1710b_A2381 YP_337531.1 4881 1626 149,383 WA10▼AL    K96243 boaB 1 BPSL1705 YP_108306.1 STK38 4821 1606 148,811 VA23▼GT    DD503 boaB ND – EF423808 4965 1654 154,117 VA71▼GT    1710b boaB 1 BURPS1710b_2168 YP_333563.1 4965 1654

154,059 VA71▼GT aSequence analyses were performed using Vector NTI (Invitrogen) and online tools available through the ExPASy Proteomics Server. bThe putative signal sequence cleavage site was determined using the SignalP 3.0 server ND = not determined The published genome of B. pseudomallei K96243 was also found to specify a boaA gene product (BPSS0796, Fig 1B) that is 92.7% identical to that of B. mallei ATCC23344. Oligonucleotide primers were designed to amplify the entire boaA gene from the B. pseudomallei strain used in our laboratory, DD503, and sequence analysis of this amplicon predicted a gene product that is 94.4% and 90.6% identical to BoaA of B. mallei ATCC23344 and B. pseudomallei K96243, respectively. Database searches with the NCBI genomic BLAST service also identified boaA in several B. pseudomallei and B. mallei isolates. All nine B. mallei and 23 B. pseudomallei strains for which sequences are available through this service were found to have the gene. Characteristics of some of these ORFs are listed in Tables 1 and 2.

927). For the subgroup analyses by histology, the Egger see more test was also not significant (p = 0.311) and for the subgroup

analyses by smoking status, the p value of Egger test was 0.552. The funnel plots (Figures 4, 5, and 6) did not exhibit any patent asymmetry. These results indicated there was no evidence of publication bias in our meta-analysis. Figure 4 Begg’s funnel plot of XRCC3 Thr241Met polymorphisms for the (C/T + T/T) versus vs C/C for all studies. Figure 5 Begg’s funnel plot of XRCC3 Thr241Met polymorphisms for the (C/T + T/T) versus vs C/C stratified by histological types of lung cancer. Figure 6 Begg’s funnel plot of XRCC3 Thr241Met polymorphisms for the (C/T + T/T) versus vs C/C stratified by smoking status of population. Discussion It is well recognized that there is a range of individual susceptibility to the same kind of cancer even with identical Selleck PF-6463922 environmental exposure. Host factors, including polymorphisms of genes

involved in carcinogenesis may have accounted for JAK inhibitor this difference. Therefore, genetic susceptibility to cancer has been a research focus in scientific community. Recently, genetic variants of the DNA repair genes in the etiology of several cancers have drawn increasing attention. As it is known that individual studies with a small sample size may have not enough statistical power to detect a small risk factor, in this meta-analysis, we involved a total of 4123 lung cancer cases and 5597 controls and explored the association between the XRCC3 Thr241Met polymorphisms and lung cancer risk. Our results indicated that XRCC3 Thr241Met polymorphism was not significantly associated with the susceptibility to lung cancer. Additionally, no significant associations were also found in the stratified analysis by ethnicity, Liothyronine Sodium histological types or smoking status. Population stratification is a troubling issue and can lead to spurious evidence on the association between markers and a disease, implicating the disparate effects of environment and ethnic differences on genetic background

[32]. In this meta-analysis, ethnicity stratification of differences between Asians and Caucasians was not found. Tobacco smoke contains many known carcinogens and pro-carcinogens, such as benzopyrene and nitrosamine. Our meta-analysis results showed no significantly risks were found to be associated with the XRCC3 Thr241Met polymorphisms and lung cancer risk in smokers or non-smokers. There were only small number of studies examined the association between the XRCC3 Thr241Met gene polymorphism and lung cancer risk in smokers or non-smokers; moreover, the p value of Q test for heterogeneity test was significant. Considering the limited studies and P value of Q-test for heterogeneity test included in this meta-analysis, our results should be interpreted with caution.

Med Sci Sports Exerc 2000, 32:1412–1418.PubMedCrossRef 25. Tipton KD, Wolfe RR: Exercise, protein metabolism, and muscle growth. Int J Sport Nutr Exerc Metab 2001, 11:109–132.PubMed 26. Churchward-Venne TA, Burd NA, Mitchell CJ, West DWD, Philp A, Marcotte GR, Baker SK, Baar K, Phillips SM:

Supplementation of a suboptimal protein dose with leucine or essential amino acids: effects on myofibrillar protein synthesis at rest and following resistance selleck products exercise in men. J Physiol 2012, 590:2751–2765.PubMedCrossRef 27. Winter JN, Fox TE, Kester M, Jefferson LS, Kimball SR: Phosphatidic acid mediates activation of mTORC1 through the ERK signaling pathway. Am J Physiol Cell Physiol BIBW2992 mw 2010, 299:C335-C344.PubMedCrossRef 28. Hoffman JR, Kang J: Strength changes during an inseason resistance training program for football. J Strength Cond Res 2003, 17:109–114.PubMed 29. Hoffman JR, Wendell M, Cooper J, Kang J: Comparison between linear and nonlinear inseason training programs in freshman football players. J Strength Cond Res 2003, 17:561–565.PubMed 30. Miletello WM, Beam JR, Cooper ZC: A biomechanical analysis of the squat between competitive collegiate,

competitive high school, and novice powerlifters. J Strength Cond Res 2009, 23:1611–1617.PubMedCrossRef 31. Blazevich AJ, Gill ND, Bronks R, Newton RU: Training-specific muscle architecture adaptation after 5-wk training

in athletes. Med Sci Sports Exerc 2003, 35:2013–2022.PubMedCrossRef Anacetrapib 32. Santtila M, Kyrolainen H, Hakkinen K: Changes in maximal and explosive strength, electromyography, and muscle thickness of lower and upper extremities induced by combined strength and endurance training in soldiers. J Strength Cond Res 2009, 23:1300–1308.PubMedCrossRef 33. Earp JE, Joseph M, Kraemer WJ, Newton RU, Comstock BA, Fragala MS, Dunn-Lewis C, Solomon-Hill G, Penwell ZR, Powell MD, Volek JS, Denegar CR, Häkkinen K, Maresh CM: Lower-body muscle structure and its role in jump performance during squat, countermovement, and depth drop jumps. J Strength Cond Res 2010, 24:722–729.PubMedCrossRef Competing interests MP and RJ have been named as inventors on pending patents by Chemi Nutra. MP and RJ are independent paid consultants to Chemi Nutra. All other authors declare that they have no competing interests. Authors’ contributions JRH was the primary investigator, supervised all study recruitment and data/specimen analysis. JRH, MP and RJ designed study, JRH and JRS performed the statistical analysis, JRH supervised the Rabusertib manufacturer manuscript preparation, JRS, DRW and RJ helped drafting the manuscript. DRW, AJW, MSF, GTM, AMG, NSE, WPM and TCS assisted with data collection and data analysis. All authors read and approved the final manuscript.

The amount of spores that needs to be added to yield this Cq should be determined for each new batch as it will vary with each new spore stock, and the DNA Selleckchem Akt inhibitor extraction protocol used. The observed inhibition highlights that multiplex qPCR can be problematic if it is used for the detection of mixed pathogens present in different quantities as amplification of targets from a dominant organism could inhibit the detection of an uncommon pathogen. Assays for the detection of single targets from multiple pathogens simultaneously, such as that described for B. anthracis, F. tularensis and Y. pestis detection [23], should therefore be carefully evaluated for this inhibition effect.

Environmental testing Application of the multiplex qPCR assays directly on human specimens or environmental samples could save time and prevent loss of DNA during extraction. However, we use the assays only after a selleck products DNA extraction protocol, in order to prevent unanticipated inhibition by diverse matrices.

Our laboratory has compared several commercially available DNA extraction kits for use in a BSL3 facility, and selected one that combined efficient DNA extraction with ease-of-use and applicability in the restricted BSL3 environment. We click here have been using the developed qPCRs for the analysis of samples suspected for the presence of these pathogens with B. thuringiensis spores added before DNA extraction under BSL3 biosafety conditions. Hundreds of samples containing all sorts of solid materials and liquids have been analyzed without yielding false positive readings. Conclusion The multiplex qPCR assays that were developed for B. anthracis, F. tularensis and Y. pestis allow the rapid detection of 3 pathogen-specific targets simultaneously without compromising sensitivity.

Together with the application of an internal control for both DNA extraction and DNA amplification, this assures highly reliable detection, while template consumption and laboratory effort is kept at a minimum. These considerations Endonuclease are particularly advantageous in the context of biothreat samples which may be used for additional tests and for surge capacity during an outbreak. The detection of multiple targets decreases the chance of false-positive and false-negative results and provides additional information about virulence. Methods Selection signature sequences An initial selection of potential signature sequences for specific detection of B. anthracis, F. tularensis and Y. pestis was based on previous reports and on the availability of sequences through public databases (NCBI/EMBL). The selection was based on functional and on technical criteria. Since 4 reporter dyes can be reliably differentiated by using qPCR instruments, and 1 channel was reserved for the internal control, we selected 3 signature sequences per organism.

8a). However, in CCl4-AZD2171 treated rat liver sections, there was little evidence for expression of rPGRMC1 in cells within the scar region other than likely non-specific binding of secondary antibody to occasional inflammatory cells, whereas hepatocytes showed enhanced expression (Fig. 8a and 8b). To firmly establish that rat liver myofibroblasts in vivo do not express rPGRMC1, fibrotic liver sections were co-stained for the expression of α-smooth muscle actin and rPGRMC1. Figure 9b and 9c shows that there was no co-staining of α-smooth muscle

actin in liver myofibroblasts with rPGRMC1, which was restricted to hepatocytes in fibrotic liver sections. Identical staining was obtained in sections from animals treated with CCl4 or CCl4 and 4A3COOHmethyl (data not included). Figure 7 4A3COOHmethyl administration and LY3023414 liver fibrosis in a rat CCl 4 model of liver fibrosis. Four animals/group (control or 4A3COOHmethyl) or VS-4718 six animals/group (CCl4 or CCl4 + 4A3COOHmethyl) were treated as outlined in the Methods section. Mean and standard deviation serum ALT (a); Mean and standard deviation collagen 1A1 mRNA levels (b); typical views of liver sections stained for sirius red, with a 100 μm scale bar (b); quantitative image analysis for fibrosis

– data are the mean and standard deviation percentage sirius red staining from at least 4 separate animals in each treatment with at least 10 randomly selected fields examined for each animal (c). Figure

8 Rat liver myofibroblast do not express rPGRMC1 Teicoplanin in vivo – Part A. Low power views (a) and high power views (b) of liver section immunohistochemically stained for rPGRMC1 using IZAb upper panels or identical staining without addition of IZAb (no 1° Ab control) from olive oil control or CCl4 treated animals (note CCl4 + 4A3COOHmethyl treated animals gave similar results). PT, portal tract; CV, central vein; scar, primary location of scar matrix and liver myofibroblasts; ns non-specifically bound secondary antibody. Figure 9 Rat liver myofibroblast do not express rPGRMC1 in vivo – Part B. High powered views show positive staining of non-parenchymal cells in control liver sections (a); co-staining sections from indicated treatment groups – DNA with DAPI (blue), α-sma (green) and PGRMC1 with IZAb (red) with merged panel (b); high powered view of merged liver section from CCl4-treated rat liver (c). PV, periportal venule; PA, periportal arteriole; BD, bile duct. Discussion Steroid hormone interaction with nuclear receptor proteins has been characterized over several decades. Steroids pass through plasma and/or nuclear membranes and interact with intracellular receptor proteins from the steroid/nuclear receptor gene super-family (such as the PXR), representing the canonical (genomic) mode of action for steroid hormone signalling [30].

Briefly, the same organs from the same group were pooled and ground to a fine powder in a mortar containing liquid nitrogen. The fine powder was dissolved and

further processed in CCLB solution in the assay kit. The resultant supernatants were collected and subjected to determination of relative light units (RLU, synergy 2, Biotek, Germany), along with a group of standard samples in the kit. The amount of luciferase in each sample was calculated on the basis of the standard curve. Detection of apoptosis and microvessel density (MVD) On day 24 after mouse inoculation with melanoma cells, subcutaneous tumors from Ad-PEDF, Selleckchem BVD-523 Ad-null and NS treated mice were collected, fixed, embedded in paraffin, and cut into

3–5 μm sections. The apoptotic cells within the tumor tissue were evaluated using the DeadEnd Colorimetric Terminal Deoxynucleotidyl Transferase-Mediated dUTP Nick-End Labeling (TUNEL) System (Promega, Corporation, Madison, Wisconsin, USA) following the manufacturer’s protocol. Ten high power fields on each slide and three slides from each animal were examined. Apoptosis index was calculated by dividing the number of apoptotic cells by the total number of cells in the field. The method reported by Weidner et al was adopted to quantify MVD in tumor tissues [17]. Briefly, 5 μm tumor sections were stained for the epithelial cell marker, CD31. The procedure of immunostaining Crenigacestat cost for CD31 was previously described in detail [18]. The following antibodies and reagents were used: goat anti-mouse CD31 mAb (1:200, Santa Cruz Biotechnology,

Santa Cruz, Leukocyte receptor tyrosine kinase California, USA), biotinylated polyclonal Compound Library rabbit anti-goat (1:100, Santa Cruz Biotechnology, Santa Cruz, California, USA), ABC kit (Boster biological engineering company, Wuhan, China) and DAB visualization system (ZSJQ Biotechnology, Beijing, China). The resultant sections were first examined at low magnifications (×40 and ×100) to identify the vascular-rich area in the tumor. Within this area, the CD31-positive microvessels were counted in a single high-power (×200) field. Any CD31 stained single or cluster of cells was considered a single countable microvessel. Adjacent sections were stained with hematoxylin and eosin (H&E) and examined for tissue structure and histological morphology. Each group contains 2 mice, and 3 sections from each mouse. Alginate-encapsulated tumor cell assay The alginate-encapsulated tumor cell assay was used to measure tumor angiogenesis in vivo, as previously described [14, 18]. Briefly, B16-F10 or CT26 cells in 1.5% (m/v) sodium alginate solution (Sigma-Aldrich, St. Louis, Missouri, USA) was dropped into a swirling 0.25 M CaCl2 solution to prepare alginate beads (1 × 105 cells/bead). Four resultant beads were implanted s.c. on both dorsal sides of BALB/c female mice (2 beads/side).

Supplementations provide a nonpharmacological therapy, and has been

gradually received attention in literatures. Nepicastat protein hydrolysates can stimulate protein synthesis and inhibit protein breakdown, and therefore, improve the net muscle protein balance after exercise [10, 15]. It is also reported that whey protein hydrolysate can ameliorate drug-induced oxidative stress [16]. However, it remains to be elucidated whether the protein hydrolysates supplementation in a short term improves the protein retention and oxidative stress of skeletal muscle following JPH203 exhaustive exercise. Therefore, we hypothesized that an additional hydrolyzed protein supplementation could enhance the muscle protein content and eliminate the oxidative stress products by regulating the plasma amino acid spectrums in rats following exhaustive exercise. Methods Experimental design Rats were randomly divided into four groups (n = 6 per group): a control group fed standard diet without exercise (SD), exercise (EX), exercise plus standard diet for 72 h (EX + SD), or exercise plus standard diet supplemented with hydrolyzed protein (2 g/kg/d) for 72 h (EX + HP). Animals were

maintained in individual cages and fed a standard chow diet and water ad libitum. All rats of the EX, EX + SD and EX + HP groups received a single bout of exhaustive swimming on the first day in the experimental period (time 0 hour). EX was sacrificed immediately following exercise. The animals of the other groups had open access to a standard rodent chow diet and water ad libitum throughout Selleck VRT752271 the study. A standard lab rat diet was rich in dietary fiber, trace elements, and intact protein (18 g/100 g fodder) including 1.76 g leucine and 5 g crude fiber per 100 g fodder. Additionally, the EX + HP group received a supplementation of protein hydrolysate (6.67 ml/kg body weight) by oral gavage once per day, while EX + SD received the same value of purified water via oral gavage. The protein hydrolysates (HYDROPROTEIN,

Shen Yi Food Nutrition, Zhuji, ZJ.) contain 60% hydrolyzed whey protein as its source of nitrogen, providing a rich source of leucine (4.67 g/100 g powder) (powder, 50 g/per bag). The protein consists of 100% content of di- Methamphetamine and tripeptides. It was dissolved in purified water (Nestle Company, USA) and the final protein concentration was 0.3 g/ml. After 72 hours of feeding following exercise, both EX + SD and EX + HP groups were sacrificed for sample collection. Subjects Twenty-four 7-week-old (250 g) specific pathogen-free male Sprague Dawley male rats were used and individually housed in a metabolic cage at the Jinling hospital Animal Research facility at Nanjing, Jiangsu province. They were placed in a room maintained at 22°C with a 12: 12-hour light: dark cycle and provided with rodent chow and water ad libitum.

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