Acknowledgments The research is supported by the Veterans General Hospitals University System of Taiwan Joint Research Program under contract nos. VGHUST101-G4-3-1 and VGHUST101-G4-3-2 and by the National Science Council of Taiwan under contract no. NSC-100-2221-E-008-016-MY3. The authors also thank the Center for Nano Science and Technology at National Central University and Clinical Research Core Laboratory at Taipei Veterans General Hospital for the facility support. References 1. Johansson CB, Albrektsson T: A removal torque and histomorphometric study of commercially pure niobium and titanium implants in rabbit bone. Clin Oral Implan Res 1991, 2:24–29.CrossRef

2. Small molecule library nmr Abrahamsson Sapanisertib mw I, Zitzmann NU, Berglundh T, Wennerberg A, Lindhe

J: Bone and soft tissue integration to titanium implants with different surface topography: an experimental study in the dog. Int J Oral Maxillofac Implants 2001, 16:323–332. 3. Olmedo D, Fernández MM, Guglielmotti MB, Cabrini RL: Macrophages related to dental implant failure. Implant Dent 2003, 12:75–80.CrossRef 4. Buser D, Schenk RK, Steinemann S, Fiorellini J, Fox C, Stich H: Influence of surface characteristics on bone integration of titanium implants. A histomorphometric study in miniature pigs. J Biomed Mater Res 1991, 25:889–902.CrossRef 5. Hansson S, Norton M: The relation between surface roughness and interfacial shear strength for bone-anchored implants. A mathematical model. J Biomech 1999, 32:829–836.CrossRef 6. Davies JE: Understanding peri-implant endosseous healing. J Dent Educ 2003, 67:932–949. 7. Oliveira PT, Nanci A: Nanotexturing ��-Nicotinamide of titanium-based surfaces upregulates expression of bone sialoprotein and osteopontin by cultured osteogenic cells. Biomaterials 2004, 25:403–413.CrossRef 8. Mendonça G, Mendonça DBS, Aragão FJL, Cooper LF: Advancing dental implant surface technology–from micron- to nanotopography. Avelestat (AZD9668) Biomaterials 2008, 29:3822–3835.CrossRef 9. Yang WE, Hsu ML, Lin MC, Chen ZH, Chen LK, Huang HH: Nano/submicron-scale TiO 2 network on titanium surface for dental implant

application. J Alloy Compd 2009, 479:642–647.CrossRef 10. Dong W, Zhang T, Epstein J, Cooney L, Wang H, Li Y, Jiang YB, Cogbill A, Varadan V, Tian ZR: Multifunctional nanowire bioscaffolds on titanium. Chem Mater 2007, 19:4454–4459.CrossRef 11. Chiang CY, Chiou SH, Yang WE, Hsu ML, Yung MC, Tsai ML, Chen LK, Huang HH: Formation of TiO 2 nano-network on titanium surface increases the human cell growth. Dent Mater 2009, 25:1022–1029.CrossRef 12. Su Z, Zhou W: Formation, morphology control and applications of anodic TiO 2 nanotube arrays. J Mater Chem 2011, 21:8955–8970.CrossRef 13. Chen JG, Chen CY, Wu CG, Lin CY, Lai YH, Wang CC, Chen HW, Vittal R, Ho KC: An efficient flexible dye-sensitized solar cell with a photoanode consisting of TiO 2 nanoparticle-filled and SrO-coated TiO 2 nanotube arrays.

Methods Bacterial isolates and isolation of isogenic

morphotypes Five B. pseudomallei isolates were examined in this study. Isolates 153, 164 and the reference isolate K96243 were cultured from cases of human melioidosis in Thailand, and isolates B3 and B4 were cultured from uncultivated land in northeast Thailand [19]. The colony morphology of all five parental isolates was type I, and isogenic types II and III were generated from type I of each strain using nutritional limitation [11]. Briefly, a single colony of type I on Ashdown agar was inoculated into 3 ml of TSB and JAK inhibitor incubated at 37°C in air in static conditions for 21 days. Bacterial culture was diluted and spread plated onto Ashdown agar. Morphotypes were identified using a morphotyping algorithm [11]. Isogenic types II and III generated from each parental type I were isolated from the plates of each strain. Growth curve analysis JQ1 concentration Growth curves were performed for the 3 isogenic morphotypes of each of the 5 B. pseudomallei isolates. A colony of B. pseudomallei was suspended in sterile phosphate buffered saline GSK2245840 concentration (PBS). The bacterial suspension

was adjusted to an optical density (OD) at 600 nm of 0.15 and diluted 100 times. One hundred microlitres of bacterial suspension was added to 10 ml of TSB and incubated at 37°C in air with shaking at 200 rpm for 28 h. At 2 h intervals, 100 μl of bacterial culture was removed, serially diluted 10-fold in PBS, and the bacterial count determined by plating on Ashdown agar in duplicate and performing a colony count following incubation at 37°C in air for 4 days. Doubling time

was calculated. Cell line and culture conditions Human monocyte-like cell line U937 (ATCC CRL-1593.2) originating from a histiocytic lymphoma was maintained in RPMI 1640 (Invitrogen) supplemented with 10% heat-inactivated fetal bovine serum (PAA Laboratories), 100 units/ml of penicillin and 100 μg/ml of streptomycin (Invitrogen) and cultured at 37°C in a 5% CO2 humidified incubator [20]. Before exposure to B. pseudomallei, 1 × 105 U937 cells per well were transferred to a 24 well-tissue culture plate (BD Falcon) and activated by the addition of 50 ng/ml of phorbol 12-myristate 13-acetate (PMA) (Sigma) over 2 days [20]. The from medium was then replaced with 1 ml of fresh medium without PMA and incubated for 1 day. The differentiated macrophage was assessed by macrophage-like morphology [21]. Following washing 3 times with 1 ml of Hank’s balance salt solution (HBSS) (Sigma), 1 ml of fresh medium was gently added to the macrophages. Interaction of B. pseudomallei isogenic morphotypes with human macrophages The interaction assay was performed as previously described [11]. B. pseudomallei from an overnight culture on Ashdown agar was suspended in PBS, the bacterial concentration adjusted using OD at 600 nm and then diluted in PBS and inoculated into wells containing differentiated U937 cells to obtain an MOI of approximately 25 bacteria per cell.

They also suggest that genes with relatively stable expression are more likely to evolve slowly when compared with VEG. Gene expression level and functional necessity GDC-0068 cell line independently influence core genome stabilization It is well established that the core genome contains more indispensible genes that play central metabolic roles [11, 12]. This results in a lower mutation rate than in the flexible genome. To define essential genes, we searched for homologs of all PDGFR inhibitor MED4 coding

genes in the Database of Essential Genes (DEG8.0), a database that collects all indispensible genes measured in laboratory by far [39]. Using BLASTx (E-value = 1 × 10-4), we found homologs for 871 MED4 coding genes. A total of 767 genes were distributed in the core genome, representing 61.3% of core genes. This was a significantly higher proportion of genes than those distributed in the flexible genome (14.6%; P < 0.001; Figure 4a). These data support the hypothesis that core genes are responsible for central cell metabolism in Prochlorococcus. Figure 4 Gene necessity analysis and COG functional enrichment of HEG. All coding-sequence genes were searched on the Database of Essential Genes (DEG8.0 [39]) using BLASTx Captisol solubility dmso (E-value = 1 × 10-4). (a) Comparison of the DEG-hit genes in the core and flexible genomes. (b) Comparisons of gene expression subclasses

between DEG-hit and DEG-miss genes. (c) COG functional enrichment of HEG in the core genome. Statistic significance was

performed by Fisher’s exact test (one-tailed). P-value ≤ 0.05 was indicated in figure. COG, clusters of orthologous groups; Core, the core genome; DEG-hit, genes with homologs identified in the database; DEG-miss, genes without any known homologs; Flexible, the flexible genome; Unk, unknown function. We also compared the expression levels of the core MED4 genes that had homologs in the DEG database (DEG-hit) with those genes that did not have any known homologs (DEG-miss). HEG, LEG, and NEG had no enrichment for either DEG-hit or DEG-miss genes (P > 0.1; Figure 4b). Although the MEG subclass had a Amisulpride significantly higher rate of DEG-hit genes (P < 0.001; Figure 4b), the mean expression level of the DEG-hit genes (mean RPKM = 602.62) was not significantly different from that of the DEG-miss genes (mean RPKM = 874.81; Student’s t-test, two-tailed P = 0.084). Therefore, as previous works reported [14, 40, 41], this suggests that essential genes are not necessarily highly expressed and that gene expression levels relatively independently affect sequence evolution in Prochlorococcus MED4. We also performed functional enrichment analysis on each gene expression subclass. As most of the genes in the flexible genome have no COG categories [42], we mainly focused on the core genes’ expression subclasses, especially the HEG.

For the sensitivity testing of the prototype system, the bloods were infected with five dilutions of the log-phase culture

suspension at a final volume of 20 μL. The first dilution contained 50 copies in 1 μL template DNA (2.5×104 CFU/mL blood), the second contained 10 copies (5×103 CFU/mL blood), the third 5 copies (2.5×102 CFU/mL blood) and the fourth 2 copies (5×102 CFU/mL blood). The red blood cells were disrupted by lysis buffer [35], the bacterial and fungal cell wall lysed using the freezing-thawing method. After digestion with Proteinase K, the DNA was extraction carried out as reported previously [36]. Bacterial and fungal primer design, FRET probes Two primer pairs were used for multiplex amplification of bacterial and fungal DNA. The bacterial primer pair was PLK1 (TAC GGG AGG CAG CAG) forward and PLK2 (TAT TAC CGC GGC TGC T) reverse, which are highly conserved

in different groups of bacteria [9] and amplify the 16S Captisol nmr rRNA sequence. Nepicastat mw The PLK2 reverse primer was modified and used without the inner fluorescence labelling. Originally, the labelled primer excited the Gram JPH203 specific probes. We applied the non-specific SYBR Green dye for excitation; it also serves for visualization of the fungal amplicons. This primer-pair produces a 187 bp fragment in each species. Previously hybridization probes were used for the Gram classification [10]. ISN2 (5′-CCG CAG AAT AAG CAC CGG CTA ACT CCG T-3′) labelled with LCRed 640 was specific for G-, and ISP3 (5′-CCT AAC CAG AAA GCC ACG GCT AAC TAC GTG-3′) labelled with Cy5.5 was specific for G + bacteria, and the [10] ISP2 probe was labelled with LCRed705 at the 5′ end. The producers offered Cy5.5 dye instead of LCred705. This modified probe was used in our experiments. The ITS86 forward (GTG AAT CAT CGA ATC TTT GAA C) and the ITS 4 reverse (TCC TCC GCT TAT TGA TAG C) primers were used for detection

of the fungi. These primers amplify a 192–494 bp sequence of ITS2 region, which is a highly variable part between the 5.8S and 28S rRNA sequence [37]. Mastermixes/excitation dyes Different, non-specific intercalating dyes are used for real-time PCR investigations. Most of these are Metalloexopeptidase accessible in ready-to-use, mastermix formulae. Our goal was to choose the best dye for excitation of the labelled probes. The tested dyes were LCGreen “LightCycler® 480 High Resolution Melting Master” (Roche Diagnostic GmbH, Mannheim, Germany); SybrGreen “LightCycler® 480 DNA Master SYBR Green I”, (Roche); “IQ™ SYBR® Green Supermix” (Bio-Rad Laboratries, Inc., Hercules, CA, USA); “Maxima™ SYBR Green qPCR Master Mix no ROX” (Fermentas, Vilnius, Lithuania); and EvaGreen (“LC-FastStart DNA Master Hybridization Probes” (Roche) combined with EvaGreen dye (Biotium Inc., Hayward, CA, USA) and “Sso Fast™ EvaGreen® Supermix” (BioRad). All mastermixes were used according to the manufacturer’s instructions.

Controls experiments were performed identically in presence of irrelevant immunoglobulins (normal mouse total Ig). In another set of experiments, it was evaluated the effect of mAb MEST-1 and -3 on P. brasiliensis mycelium to yeast transformations, and as expected, selleck compound it was not observed a significant inhibition, since these antibodies do not react or react weakly with mycelium forms. Thus, 50 μg/ml of MEST-1 and MEST-3 inhibited, respectively, 6% and 9% the transition from mycelium to yeast of P.

brasiliensis. Figure 7 shows the differentiation of P. brasiliensis mycelia forms grown in presence (Panel B) or not (Panel A) of MEST-3 for 48 h at 37°C. In order to illustrate the differentiation inhibition, but not picturing the real inhibition percentage, Figure 7B pictured a field with high concentration of hyphae form. Figure 7 Effect of mAb MEST-3 on yeast formation. P. brasiliensis hyphae fragments were suspended in 1 ml of PGY medium and supplemented or not with mAb MEST-3 (50 μg/ml). Cells were placed on a 24-well plate at 37°C, and after 96 h of incubation, hyphae differentiation

into yeast (M→Y) forms was observed under microscope. Panel A shows M→Y differentiation in free-mAb medium, Panel B shows M→Y differentiation in medium containing MEST-3, and Panel C shows the mycelia growth of hyphae fragments LY2874455 cell line maintained at 23°C for 96 h in free-mAb medium. Discussion mAb MEST-3 specificity Methamphetamine In this paper, we describe the characterization of MEST-3, an

IgG2a monoclonal antibody directed to the structure (Manpα1→3Manpα1→2IPC) from GIPC Pb-2 of P. brasiliensis. Among different methyl-glycosides, disaccharides and glycosylinositols, only Manpα1→3Manp and Manpα1→3Manpα1→2Ins inhibited MEST-3 binding to Pb-2 in solid-phase RIA. Furthermore, MEST-3 was unable to recognize, by solid-phase RIA or HPTLC-immunostaining, the intact GIPC Ss-M2 (Manpα1→3Manpα1→6IPC), thus suggesting that α1→6 linkage of the subterminal mannose unit to inositol represents a sterical hindrance for antigen recognition by MEST-3. Therefore, the minimum epitope required for optimum binding of MEST-3 to Pb-2 and similar GIPCs, would comprise the two linear mannose residues in specific linkage and the myo-inositol residue as follows: Manpα1→3Manpα1→2Ins. By indirect immunofluorescence, it was observed that MEST-3 is reactive only with yeast forms of P. brasiliensis, H. capsulatum and S. schenckii, which is in agreement with previous data describing the crypticity of GIPC Pb-3 and GlcCer in mycelium forms of P. brasiliensis [13, 24]. Accordingly, despite the detection of the GIPC Pb-2 extracted from hyphae of P. brasiliensis by HPTLC and HPTLC Eltanexor immunostaining with mAb MEST-3, it should be noted the complete lack of MEST-3 reactivity by immunofluorescence with fixed mycelia forms.

Hence, in order to overexpress and purify pneumococcal SmpB, its coding region was cloned in fusion with pneumococcal ssrA (the gene encoding tmRNA) to allow co-expression of both. smpB was amplified by PCR with primers rnm010 and rnm011, which contains a 3’ extension complementary to the 5’-end of ssrA. ssrA was amplified using the primer pair smd057/smd058. The two PCR fragments were then mixed and used as template in a PCR with primers LY333531 mouse rnm010 and smd058. The resulting PCR product was digested with NdeI and BamHI (Fermentas), and cloned into the pET-15b vector (Novagen) previously cleaved with the same restriction enzymes. This construction, named pSDA-02, was first obtained in E. coli DH5α and

then transferred to E. coli BL21(DE3) to allow the expression of His-SmpB. This construct was confirmed by DNA sequencing. Overexpression and purification of proteins RNase R from S. pneumoniae was purified as previously described [30]. For purification of SmpB, BL21(DE3) cells containing pSDA-02

plasmid were grown at 37°C in 250 ml of LB medium supplemented with 100 μg/ml Amp to an OD600 of 0.5. Overexpression Protein Tyrosine Kinase inhibitor of SmpB was then induced by addition of 1 mM IPTG; induction proceeded for 3 hours at 37°C. Cells were harvested by centrifugation and stored at −80°C. Purification was performed by histidine affinity chromatography using HisTrap Chelating HP columns (GE Healthcare) and AKTA HPLC system (GE Healthcare) as follows. Frozen cells were thawed and resuspended in lysis buffer (50 mM HEPES pH 7.5, 1 M NH4Cl, 5 mM MgCl2, 2 mM β-mercaptoethanol, 10 mM imidazole). Cell suspensions were lysed using a French Press at 9000 psi in the presence of 1 mM PMSF. The crude extracts were treated with Benzonase (Sigma) to degrade the nucleic acids and clarified by a 30 min centrifugation

at 10000 xg. The clarified extracts were then loaded onto a HisTrap Chelating Sepharose 1 ml Farnesyltransferase column equilibrated with buffer A (20 mM sodium phosphate pH 7.4, 0,5 M NaCl, 20 mM imidazole). Protein elution was achieved by a continuous imidazole gradient (from 20 mM to 500 mM) in buffer A. The fractions containing the purified protein were pooled together and concentrated by centrifugation at 4°C in an Amicon Ultra Centrifugal Filter Device with a molecular mass cutoff of 10 kDa (Millipore). Protein concentration was determined using the Bradford method [59]. SmpB and RNase R purified proteins were loaded in a SDS-PAGE gel and Coomassie blue stained for band excision (data not shown). Bands corresponding to a total of 500 μg of each protein were used to raise antibodies against the respective pneumococcal proteins (Eurogentec). RNA extraction and northern blotting Overnight cultures of S. pneumoniae TIGR4 wild type and mutant AZD6244 nmr derivatives were diluted in pre-warmed THY to a final OD600 of 0.1, and incubated at 37°C until OD600 ~ 0.3. At this point, cultures were split in two aliquots and each aliquot was further incubated at 15°C or 37°C for 2 h.

In surgery, a common trunk program of 3 years,

which Selleck EX-527 includes a 9-month primary health care rotation, was designed to familiarize the resident with basic surgical techniques while working in a central or district hospital under the supervision of a more senior surgeon and learning to perform independently the more common basic surgical emergency operations such as appendectomies, incarcerated hernia operations, fixation of ankle fractures etc. After the common trunk period, another 3-year period in one of the university hospitals is required in one of the following fields: gastroenterological surgery, cardiothoracic surgery, check details vascular surgery, urology, orthopedics and traumatology, hand surgery, plastic surgery, pediatric surgery, MK5108 concentration and general surgery. The new law created 2 new specialties, vascular surgery (separated from cardiothoracic surgery) and general surgery (an independent specialty). Oral and maxillofacial surgery and neurosurgery are also main specialties with a 6-year training program but are not following the common trunk training program of other fields of surgery. Theoretical

education of 100 hours and a national examination are part of all specialization programs. There is no emergency surgery specialty in Finland. Surgeons specialized in orthopedics and traumatology look after most of the polytrauma patients, whereas visceral injuries are largely managed by organ-specific specialists, at least in bigger hospitals. Future directions The current specialization system is in harmony with the European Union requirements and will guarantee the supply of well-trained surgeons for specialized elective surgery.

However, it is seriously deficient in providing surgical competence for managing Dynein acute surgical problems, in terms of knowledge, decision making and technical skills. General surgical knowledge and skills are eroding rapidly and this has caused great concern among the surgical profession in Finland. Inevitably this will lead to increasing centralization of trauma and emergency surgery services, a trend that is already visible in many parts of the country. A new law on medical education is under preparation and will probably be effective within the next 1–2 years. Among other things, it lengthens the common trunk period with one year, and effectively the overall training period from 6 to 7 years. It also seems to end the role of general surgery as an independent specialty. Whether this will alleviate the problems associated with the current training system is questionable. The Finnish Society of Surgery has taken the initiative to urge for complete reorganization of the surgical services based on a regionalized model.

Since deletion of SA1665 has been shown to increase β-lactam resistance, reduced SA1665 transcription in the presence of β-lactams may also provide some protection against β-lactam exposure.

selleck products Figure 5 Northern and Western blot analyses. A, Transcription of SA1665 over growth in CHE482, with RNA harvested at the OD600 nm values indicated. B, Transcription of SA1665 from CHE482 grown to OD600 nm 0.25 and either left uninduced AZD1152 nmr (-) or induced with either 4 or 120 μg/ml of cefoxitin fo 0′, 10′ and 30′. C, Transcriptional profiles of SA1664, SA1665, SA1666 and SA1667 in CHE482 and ΔCHE482, grown to OD600 nm 0.25 and either uninduced or induced with cefoxitin 4 μg/ml for 0′, 10′ or 30′. Approximate sizes of transcripts, in kb, are indicated on the right of the blots. D, Transcription of mecA and mecR1 in CHE482 and ΔCHE482, grown to OD 0.25 and either left uninduced or induced with cefoxitin (4 μg/ml) and sampled after 0′, 10′ and 30′. Ethidium bromide stained 16S rRNA bands from all Northern gels are shown as a comparative indication of RNA loading. E, Western blots showing amounts of PBP2a in ZH44 and ZH73 ICG-001 in vitro and their respective

SA1665 deletion mutants, before (0′) and after induction with 4 μg/ml of cefoxitin for 10′ and 30′. Northerns also showed that, as expected, the SA1665 transcripts were absent from the deletion mutant (Figure 5C), and additional experiments demonstrated that wild type SA1665 transcription patterns were restored by complementation of ΔCHE482 with pME26 (data not shown). The effects of SA1665 deletion on directly up- and down-stream genes Teicoplanin were also investigated. Northern blots of the neighbouring genes SA1664, SA1666 and SA1667, showed that expression of all three genes was very weak compared to that of SA1665. A weak transcript of about 3 kb was present in hybridizations probed with orfs SA1665-SA1667. This band decreased in size in the SA1665 mutant when probed with SA1666 and SA1667. One of the transcripts hybridising

to the SA1664 probe also decreased in size by ~0.5 kb in the SA1665 mutant, suggesting that SA1665 was present on several transcripts of different lengths, including a high abundance monocistronic transcript and low abundance polycistronic transcripts (Figure 5C). Transcript abundance of both the upstream SA1666-SA1667 operon and the downstream SA1664-specific transcript all appeared to increase slightly in ΔCHE482. The significance of these subtle increases in transcription are unknown, however, polar effects from SA1665 deletion seem unlikely, based on the facts that all genes were still transcribed, their transcription levels all remained extremely low and the transcriptional terminator of SA1665 remained intact in the deletion mutant (Figure 1B). Expression of mecR1 and mecA were analysed from RNA of uninduced and induced cultures of CHE482 and ΔCHE482. Cells were induced at OD600 nm 0.25 (Figure 5D) and 1.

0 ml/min. In brief, 20 μL plasma was mixed uniformly with 100 μL derivative regent (containing phenylisothiocyanate, triethylamine, dehydrated alcohol, deionized water) after thawing, and 20 μL mixed SIS3 in vitro liquid was injected into HPLC pump to measure the plasma concentrations of amino acids. The measurement for all plasma samples were repeated in triplicate [18]. Statistical analyses The data are presented as means ± SEM. SPSS16.0 software was applied for statistical analysis of all data (SPPS Inc., Chicago, IL, USA). Differences between groups were examined for statistical significance using

one-way analysis of variance (ANOVA) and then determined with the Student-Newman-Keuls test. The correlation was determined find more by stepwise multiple linear regression. The criterion for significance was P < 0.05. Results Food intake, excrement

and body weight Groups EX + SD and EX + HP consumed 30 grams of standard diet daily. No significant differences in food intake were observed between groups (SD: 31.0 ± 2.5 g, EX: 33.0 ± 3.1 g, EX + SD: 30.0 ± 1.9 g, EX + HP: 32.0 ± 2.8 g), selleck chemical suggesting protein supplementation did not influence food intake within the 72 hours period. Supplementation of protein hydrolysate or water did not increase the frequency of diarrhea in the EX + SD group and EX + HP group, compared with SD group during the duration of the study (SD: 2.2 ± 0.5 g, EX + SD: 2.5 ± 0.8 g, EX + HP: 2.8 ± 0.6 g). Before the experiment, there was no difference in body weight among the four groups (SD: 255.7 ± 14.4 g, EX: 265.5 ± 8.5 g, EX + SD: 257.3 ± 8.1 g, EX + HP: 259.7 ± 23.7 g). Following exhaustive swimming exercise, body weights of EX group, EX + SD group and EX + HP group were significantly decreased compared with their initial body weights (EX: 257.5 ± 9.2 g, EX + SD: 253.5 ± 6.4 g, EX + HP: 252.7 ± 19.6 g). At 72 hours after feeding, the body weights of EX + SD group and EX + HP group were higher than

immediately following exercise (P < 0.05). Doxorubicin The body weight increase observed in EX + HP group was higher compared with EX + SD group (269.7 ± 29.0 g vs 263.0 ± 7.8 g), but the difference did not reach significance (P > 0.05). Total protein, PC and MDA levels in rat skeletal muscle As illustrated in Figure 1, the total protein amount of skeletal muscle was significantly increased in EX + HP group, compared with EX + SD group (P = 0.02). The level of MDA was significantly lower in EX + HP group compared with EX + SD group (P = 0.035), meanwhile it was elevated in EX + SD group compared with EX group (P = 0.014) (Figure 2). The mean level of PC was increased in EX + SD group compared with SD group (p < 0.001), but it was ameliorated significantly in EX + HP group compared with EX + SD group (p < 0.001) (Figure 3).

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