Proteins were separated on 24 × 18-cm Tricine/SDS-PAGE (12% acrylamide) [77].

After migration, the gels were fixed, and the proteins were visualized by coomassie brilliant blue R-250. Images of the gels were taken with a high-resolution scanner (Amersham Biosciences). BN-PAGE Proteins were concentrated and directly loaded on native PAGE gradients 6-15% acrylamide for the first dimension and on a 12% Tricine-SDS-PAGE for the second dimension, as described in Peltier et al., 2004 [78]. Proteins were visualized by coomassie blue staining. Protein identification by mass spectrometry Stained protein spots were manually excised, washed, digested with trypsin, and extracted using formic acid. Protein digests were analyzed using either a hybrid triple-quadrupole linear ion trap mass spectrometer (Q-TRAP 4000; Applied Proteasome purification Biosystems), coupled to a nano-chromatography system (Dionex), or an ion trap mass spectrometer (Esquire HCT; Bruker), interfaced with an HPLC (high-performance liquid chromatography) chip system (Agilent). MS/MS data were searched against NCBI (National Center for Biotechnology Information) and Trypanosoma

brucei databases using Mascot software. Raw data were analyzed using Data Analysis software (Bruker) to generate a peak list for searching a Trypanosoma database extracted from the Sanger Institute. The Mascot (v2.2) search engine was used with the following parameters: one missed cleavage allowed for trypsin, Amino acid carboxymethylation of cyst as fixed modification, methionine oxidation as variable Erismodegib research buy modification, and a 0.6-Da tolerance range for mass accuracy in MS/MS. At least one matching sequence tags of high quality was needed for positive identification of proteins. Potential false positive identifications have been addressed as described in Elias et al., 2005 [79] using identical search parameters against a database in which the sequences have been reversed. We set a false discovery rate (FDR) of 1%. When the Mascot peptide score was below (and even above) the Mascot peptide score indicated for a FDR of 1%, a systematic manual validation was done with stringent parameters (at least 6 y or b ions, at least

4 consecutive ions, and peptidic sequence formed of more than 7 amino acids). The proteins were classified according to MapMan http://​mapman.​gabipd.​org. Raw data will be made available upon request for research purposes. Additional data on identified proteins are supplied in additional file 8 (Table S8). Preparation of vesicles by ultracentrifugation and sucrose gradient Secretion buffer and infected rat serum after parasite depletion were filtered (0.2 μm). Membranes were isolated from secretion buffer and serum of Trypanosoma-infected rats by a 140,000 g ultracentrifugation for 30 min at 4°C. Pellets were resuspended in 20 mM Tris/Hcl buffer pH 7.8 and layered on top of a step sucrose gradient (20-30-40-60% sucrose [Sigma-Aldrich]).

aeruginosa isolates collected from CF patients using a method adopted from Jacob 1954 [14]. Bacterial cells of dense LB cultures (48 h old) of PA01 and PA14 were spun down in a centrifuge. Supernatant was collected and filtered (0.20 μm) and serially Ribociclib diluted in minimal salts medium [14]. For the assay asking if proteinaceous compounds are responsible for killing, the sterile supernatant was heated for 15 s at 100°C. 0.5 ml of a dense culture of a natural isolate was added to 3 ml of molten semi solid LB (bacto-tryptone 10 g, yeast extract 5 g, NaCl 10 g, agar 7 g, 1000 ml dH2O) and poured out over the surface of a Petri dish containing

minimal salts agar (as described above with 10 g of agar added) as an overlay. A dilution series of either non-heat treated or heat treated sterile supernatant was spotted on top of the layer of natural isolate, up to 11 spots of 15 μl were spotted on a single Petri dish with overlay. Cultures were incubated for 48 h at 37°C. The inverse of the highest dilution of sterile supernatant giving rise to inhibition was defined as the inhibition score, which is effectively a measure of the minimal inhibitory concentration (MIC). SAHA HDAC molecular weight The inhibition scores were log transformed

prior to analysis. No inhibition was observed when spotting sterile PA01or PA14 supernatant on top of an overlay with the same strain. To exclude the possibility that bacteriophage are responsible for the observed inhibition, we performed a one-step growth assay as follows. The zones of inhibition formed on overlays of clinical isolates were transferred to an exponential liquid culture of growing cells of the same clinical isolate. After 24 h, cell free extract was prepared and spotted

onto a layer of the clinical isolate. A resulting clear zone of inhibition would be indicative of the presence of bacteriophage because a 24 h liquid culture of clinical isolate should contain even more bacteriophage than the initial culture since bacteriophage are able to reproduce with the appropriate host cells present. We found no evidence for the presence of bacteriophage. Acknowledgements We thank anonymous reviewers and Andy Gardner for comments Tacrolimus (FK506) on this work and Tracy Giesbrecht, Talía Malagón and Danna Gifford for assistance. The Ontario Provincial Government, the Canadian Cystic Fibrosis Foundation and the National Research Council of Canada provided funding. Electronic supplementary material Additional file 1: Table S1. Inhibition of clinical isolates by toxins in cell free extract collected from laboratory strains PA01 and PA14 as a function of metabolic similarity (correlation coefficient) between toxin producer and clinical isolate based on BIOLOG profiles. A unimodal non-linear relationship peaking at intermediate metabolic similarity give best fit to the data for producer PA14 (solid lines), better than a linear fit; for PA01 no such relationship was found.

smegmatis [24], and a knockout plasmid construct was therefore prepared to isolate an M. tuberculosis impA mutant. As the gene lies within the his operon (Figure 2), this plasmid carried an unmarked deletion that would not have polar effects. The mutant was generated using a two-step method [26], and grew well on solid medium. www.selleckchem.com/products/acalabrutinib.html Unlike the M. smegmatis impA mutant which had altered colony morphology, there were no obvious differences in colony morphology between the wild-type and mutant strains. We carried out a similar experiment to determine whether suhB plays a role in inositol metabolism. Again, a deletion construct was prepared, and an unmarked mutant isolated, with no obvious differences

in colony morphology. Inactivation of CysQ We constructed a plasmid to delete the cysQ gene. Initially, we were unable to obtain a mutant; of 97 double crossovers (DCOs) screened in the presence of inositol,

all were wild-type. We therefore made a merodiploid strain by integrating a second copy of cysQ into the single crossover (SCO) strain, and repeating the selection for DCOs on sucrose. Using this method, 24 out of 30 colonies were found to be mutants. The ability to isolate a mutant only in the presence of a functional copy of the gene indicates that this gene was essential under the conditions tested. DNA Damage inhibitor It could be inferred that cysQ synthesizes all the inositol in the cell, or all the inositol for a specific essential molecule. However, this hypothesis is improbable, as, if true, we would predict thatmutants would be inositol auxotrophs, yet no mutants were isolated even in the presence of high levels of inositol. One possibility is that inositol does not penetrate

the cell wall, which is known to be highly impermeable. find more However, as we had successfully isolated a mutant lacking inositol-1-phosphate synthase (an inositol auxotroph), only when the media was supplemented with extremely high levels of exogenous inositol (50-77 mM) [23], it seems that inositol does enter the cell in sufficient quantities but permeability to this molecule is poor. This suggests that even a slight increase in the requirement for inositol might make mutant isolation impossible, since we had reached the limits of inositol solubility. We reasoned that an increase in the availability of inositol by introduction of a porin might allow a mutant to be isolated. We therefore electroporated an integrating plasmid (pMN013) carrying the M. smegmatis porin gene mspA [44, 45] (for which M. tuberculosis has no orthologue) into the SCO strains, and repeated the sucrose selection. Using this method, we successfully isolated a cysQ mutant in the presence of 77 mM inositol. We screened 16 DCO colonies and two were mutants. We then plated the mutant on inositol-free medium, and were surprised to observe normal growth, indicating that once the mutant has been isolated, it does not require inositol.

After watertight abdomen closure, a closed Trametinib circuit was established by an electric pump (Abbott-Gemstar, Crestline Medical, Pleasant Grove, UT, USA) at a flow rate of 15 ml/min. Total volume of the circuit was 500 ml of saline solution which was pre-heated to 37°C. Starting time was defined as the moment the temperature reached 41.5°C and 30 mg/l cisplatin was added. The temperature was kept constant at 42°C for 1 hour in the peritoneal

cavity by immersing an intermediate reservoir and about 1 meter of the circuit tubing in a thermostat-regulated bath at an average temperature of 48°C. The third grouphad a 2 hours treatment with 30 mg/l of cisplatin and 2 mg/l of intraperitoneal adrenaline: after 1 hour the abdomen was open to empty the peritoneal cavity and a second identical bath was then performed for 1 additional hour. A previous experiment showed that 1 hour of BIBW2992 purchase treatment with 2 mg/ml adrenaline at 37°C did not increase the platinum content in peritoneal nodules and, thus, such a group was not planned in this study

(unpublished data). The fourth groupunderwent the same treatment as the third group, but without adrenaline. All animals from the 4 groups were kept anesthetized, lying on the back, for the entire duration of the treatment, using repeated IM ketamine and xylazine injections as necessary. At the end of treatment, the rats were sacrificed; the abdominal cavity was opened and abundantly

washed with water. Epiploic tumor nodules (200 mg), the left diaphragm, a piece of the muscle lining the abdominal cavity measuring 5 × 5 × 1 mm thick, parietal thoracic muscle (200 mg) Benzatropine in order to reflect the extra-abdominal tissues, half of the left kidney, and about 200 mg of the anterior edge of the liver were sampled and kept at -80°C until the platinum assay. The comparison of groups 1 and 2 should assess the effect of hyperthermia; that of groups 3 and 4 should assess the effect of adrenaline; and that of groups 1 and 4 should assess the effect of the duration of IPC. A 2-hour HIPEC was impossible due to intolerance of the animals. Atomic absorption spectrometry The total concentration of platinum was measured by atomic absorption spectrometry (AAS). Cultured cells were washed twice after cisplatin incubation, then trypsinised and counted. Cell pellets were frozen at – 80°C until AAS assay. After weighing, the frozen rat tissues were digested in a microwave digester (MLS-1200 Mega, Milestone, Sorisole, Italy). Platinum concentration was measured after dilution in distilled water, using a Zeeman atomic absorption spectrometer (Spectra-A; Varian, Les Ulis, France). Platinum is 65.01% of the molecular mass of cisplatin; to convert platinum concentrations into cisplatin concentrations, the first must be multiplied by 1.54.

Ultrasound scans were obtained for all of the patients. Computed tomography scans

was available for 13 patients. Ultrasound scans revealed intra-abdominal fluid in all cases, Intraperitoneal multiple cysts in 11 cases (sensitivity = 78.6%) (Figure 1) and heterogeneous cavity or cystic structures in the liver in 12 cases (sensitivity = 85.7%). Both CT showed multiple cystic lesions in the liver and peritoneum with intra-abdominal free fluid (Figures 2, 3, 4). Extensively dilated biliary ducts due to intrabiliary rupture were seen in one case. The ruptured cysts were located in the right lobe of the liver in seven patients, in Decitabine research buy the left lobe in six patients and in both lobes in one patients. Cysts were single in 8 cases (78%) and multiple in 6 cases (22%). The cysts were infected in four patients (28,6). In both cases, cystic infection was determined incidentally BVD-523 during the operation. Table 1 Patient

and cyst characteristics   Number of patients (%) Age   mean 39,5 ± 18,5 median 30 (20-70) Sex   Male 8(57,2) Female 6(42,8) Previous hydatid disease surgery   Yes 0 no 14(100) No. of cysts   1 7(50,0) 2 5(35,7) 3 1(7,1) 4 1(7,1) Cyst diameter (cm)   1-5 0 6-10 5(35,7) >10 9(64,3) Position   Superficial 11(78,6) Deep 3(21,4) Bile content   Positive 6(42,8) Negative 8(57,2) Cyst infection   Positive 4(28,6) Negative 10(71,4) Figure 1 US images showing ruptured hydatid cysts of the liver. Figure 2 Axial contrast enhanced computed tomography images demonstrate ruptured hydatid lesion within right liver lobe. Exoribonuclease Figure 3 Coronal contrast enhanced computed tomography images demonstrate ruptured hydatid lesion within right liver lobe with perihepatic free fluid. Figure 4 Axial contrast enhanced computed tomography images demonstrate ruptured hydatid lesion with free serous pelvic fluid. Besides the ruptured cyst, intact hepatic hydatid cysts were present in six patients and were definitively treated during the surgery. All patients underwent surgery within the first 48 hours after presentation (mean 7 hours). One to five liters of hydatid fluid with floating daughter cysts and purulent material was present in the

abdomen (Figure 5). Partial pericystectomy and drainage was the most frequent surgical procedure. In two patient, there was direct communication between the cyst and the gallbladder, and cholecystectomy was performed. Procedures to fill the cystic cavities were applied after removal of the intraperitoneal fluid. Unroofing the cyst, capitonnage and external drainage in all patients, omentoplasty in two patients, were the methods used to manage the cysts. Four patients had two or more of these procedures. No patients died in the early postoperative period. A total of seven complications developed in six patients. biliary fistula developed in two patients. Other complications were prolonged ileus, pulmonary infection, and wound infection, one each.

PubMed 12. Bennett JM, Catovsky D, Daniel MT, Flandrin G, Galton DA, Gralnick HR, Sultan C: Proposals for the classification of the myelodysplastic syndromes. Br J Haematol 1982, 51:189–199.PubMed 13. Vardiman JW, Harris NL, Brunning RD: The World Health Organization (WHO) classification of the myeloid neoplasms. Blood 2002, 100:2292–2302.PubMedCrossRef 14. Lo Coco Selleck Talazoparib F, Foa R: Diagnostic and prognostic advances in the immunophenotypic and genetic characterization of acute leukaemia. Eur J Haematol 1995, 55:1–9.PubMedCrossRef 15. Slovak ML, Kopecky

KJ, Cassileth PA, Harrington DH, Theil KS, Mohamed A, Paietta E, Willman CL, Head DR, Rowe JM, Forman SJ, Appelbaum FR: Karyotypic analysis predicts outcome of preremission and postremission therapy in adult acute myeloid leukemia: a Southwest Oncology Group/Eastern Cooperative

Oncology Group Study. Blood 2000, 96:4075–4083.PubMed 16. Qian J, Wang YL, Lin J, Yao DM, Xu WR, Wu CY: Aberrant methylation of the death-associated protein kinase 1 (DAPK1) CpG island in chronic myeloid leukemia. Eur J Haematol 2009, 82:119–123.PubMedCrossRef 17. Greenberg P, Cox C, LeBeau MM, Fenaux P, Morel P, Sanz G, Sanz M, Vallespi T, Hamblin T, Oscier D, Ohyashiki Tamoxifen solubility dmso K, Toyama K, Aul C, Mufti G, Bennett J: International scoring system for evaluating prognosis in myelodysplastic syndromes. Blood 1997, 89:2079–2088.PubMed 18. Karlsson R, Pedersen ED, Wang Z, Brakebusch C: Rho GTPase function in tumorigenesis. Biochim Biophys Acta 2009, 1796:91–98.PubMed 19. Benitah SA, Valerón PF, van Aelst L,

Marshall CJ, Lacal JC: Rho GTPases in human cancer: an unresolved link to upstream and downstream transcriptional regulation. Biochim Biophys Acta 2004, 1705:121–132.PubMed 20. Aznar S, Fernández-Valerón Axenfeld syndrome P, Espina C, Lacal JC: Rho GTPases: potential candidates for anticancer therapy. Cancer Lett 2004, 206:181–191.PubMedCrossRef 21. Vidal A, Millard SS, Miller JP, Koff A: Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status. J Biol Chem 2002, 277:16433–16440.PubMedCrossRef 22. Seasholtz TM, Zhang T, Morissette MR, Howes AL, Yang AH, Brown JH: Increased expression and activity of RhoA are associated with increased DNA synthesis and reduced p27(Kip1) expression in the vasculature of hypertensive rats. Circ Res 2001, 89:488–495.PubMedCrossRef 23. Olson MF, Paterson HF, Marshall CJ: Signals from Ras and Rho GTPases interact to regulate expression of p21 Waf1/Cip1 . Nature 1998, 394:295–299.PubMedCrossRef 24. Liberto M, Cobrinik D, Minden A: Rho regulates p21(CIP1), cyclin D1, and checkpoint control in mammary epithelial cells. Oncogene 2002, 21:1590–1599.PubMedCrossRef 25. Vega FM, Ridley AJ: Rho GTPases in cancer cell biology. FEBS Lett 2008, 582:2093–2101.PubMedCrossRef 26. Melo JV, Barnes DJ: Chronic myeloid leukaemia as a model of disease evolution in human cancer. Nat Rev Cancer 2007, 7:441–453.PubMedCrossRef 27.

parapsilosis ATCC 22019 and C. glabrata ATCC 39316, were from the [ATCC], Cryptococcus neoformans IFM 5844 and IFM 5855 were from IFM Quality Services

Pty Ltd [IFM], and Aspergillus fumigatus SzMC 2486, A. flavus SzMC 2536 and A. niger SzMC 2761 were from the Szeged Microbiological Collection [SzMC]. Furthermore, clinical strains of C. albicans (n = 14), C. glabrata (n = 5), C. tropicalis (n = 4), C. parapsilosis (n = 5), C. krusei (n = 4), C. quillermondii (n = 4), C. lusitaniae (n AZD9291 order = 3), C. norvegensis (n = 1), C. inconspicua (n = 2), C. dubliniensis (n = 2) and Cryptococcus neoformans (n = 2) from the Institute of Clinical Microbiology at the University of Szeged were also tested. Bacterial DNA purification The bacterial strains were grown on Columbia agar base under aerobic conditions, except that Bacteroides fragilis was grown under anaerobic conditions. The bacterial DNA was extracted with the QIAamp® DNA Blood Mini Kit (QuiaGene Inc, Chatsworth, Calif., USA), following the manufacturer’s instructions in “Protocols for Bacteria”. One millilitre of log-phase culture suspension, at a concentration of 107 CFU/mL, was used for the preparation. For determination of the sensitivity of the reaction, 100 μL of the serially diluted

S. aureus reference strain was used for DNA extraction. The number of bacterial cells was determined by plating aliquots of serially learn more diluted samples onto Columbia agar base. For lysis of the rigid multilayered G + bacterial cell wall, we used a pre-incubation step with 20 mg/mL lysozyme (in 20 mM Tris · HCl, pH 8.0, 2 mM EDTA, 1.2% TritonX100). The spin protocol for “DNA Purification from Tissues” was followed, after Avelestat (AZD9668) incubation at 30°C for 30 min. The final concentration of DNA was 2.0-13.8 ng/μL, with a ratio A260/A280 = 1.6-1.8 after purification. Fungal DNA purification All the fungi were grown on Sabouraud medium. The fungal DNA was extracted from 1 mL of a log-phase culture suspension containing 9.6 × 107 of fungal cells. For determination of the sensitivity

of the reaction, 100 μL of the serially diluted C. albicans reference strain was used for DNA extraction. The number of fungal cells was determined by plating aliquots of serially diluted samples onto Sabouraud-glucose medium. We followed the QIAamp® DNA Mini Kit Protocol for Yeasts. In this case, additional reagents were required for elimination of the complex fungal cell-wall structure: sorbitol buffer (1 M sorbitol, 100 mM EDTA, 14 mM β-mercaptoethanol) [34] was used, and the samples were incubated with lyticase for 30 min at 30°C. Efficient and complete lysis was achieved in 1.5 hour in a shaking water-bath. This purification yielded 2.0–25 μg of DNA in 100 μL of water (2.0–13.8 ng/μL), with A260/A280 = 1.6–1.8. DNA preparation from infected blood Samples of 180 μL healthy donor bloods in EDTA vacutainer tubes were infected with 20 μL of log-phase culture suspension at a concentration of 108 CFU/mL bacterial and/or fungal suspensions.

005, 0.025, 0.05, 0.1, 5, 20 or 100 mM. To test for specificity of induction, additional cultures were incubated in the presence of 0, 0.5, 5 and 50 μM learn more PbNO3 in mXBM; 0, 0.5, 5 and 50 mM Na2HAsO4·7 H2O in 0.2X NB; and 0, 0.5, 5, 50 mM hydrogen peroxide (H2O2) in 0.2X NB. Cells were incubated for 2.5 hours at 30°C with agitation. Induction experiments with Cr(VI)-sensitive strain D11 transformed with pKH22, pKH23 and pKH24 were carried out in the same manner with the following exceptions:

kanamycin was added to a concentration of 30 μg ml-1 and chromate was added to one culture at a concentration of 0.025 mM. Generation of chromate-sensitive FB24 derivative The lead- and chromate-sensitive mutant, D11, was generated from the resistant wild-type strain FB24 by growing cells in LB without chromate. SCH727965 chemical structure Cultures were transferred daily by diluting cells 1:1000 into fresh media. Transfers were maintained for approximately 90 generations

at 30°C with shaking at 200 rpm and then screened for cells sensitive to 75 μM lead on mXBM agar plates. Lead-sensitive colonies were then tested for Cr(VI) sensitivity on 0.1X nutrient agar (NA) plates supplemented with 0.5, 1, 2 and 5 mM K2CrO4. Loss of plasmid DNA in strain D11 was assessed by Southern hybridization and rep-PCR. Loss of the CRD genes was confirmed by PCR using gene-specific primers. Total genomic DNA was extracted from cultures grown overnight in NB with appropriate selection. Cells were harvested by centrifugation, suspended in TE buffer, and treated with

lysozyme (1 mg ml-1) for one hour followed by treatment with proteinase K (10 mg ml-1). Cells were lysed using a FastPrep instrument (Qbiogene, Carlsbad, CA) at a setting of 4 for Vildagliptin 30 s with 0.64 cm ceramic beads. Genomic DNA was purified by phenol: chloroform: isoamyl alcohol extraction and precipitated with isopropanol [50]. DNA was digested with restriction enzymes (SacI and XcmI) and separated on a 0.7% agarose gel and transferred to Hybond-N+ membrane (Amersham Pharmacia, Pisscataway, NJ) using a Trans-blot semi dry transfer cell (Bio-Rad, Hercules, CA) following the manufacturer’s recommendations for voltage and transfer time. A digoxigenin-labeled probe targeting the 10.6-kb CRD on Arthrobacter sp. strain FB24 pFB24-104 [GenBank: NC_008539] was generated by PCR with primers C42/F and C42/R (Table 4) using the TripleMaster PCR system (Eppendorf North America, Inc., Westbury, NY) according to the manufacturer’s reaction mixture and cycling specifications for long-range PCR. Hybridization and chromogenic detection was carried out under high stringency conditions as described in the DIG Application Manual for Filter Hybridization (Roche Applied Science, Indianapolis, IN). Table 4 PCR and qRT-PCR primers used in this study.

On the

other hand, there are studies that have demonstrated a coexistence of the two entities. One study [12] found that OA did not protect against generalized primary OP. Glowacki et al. found occult osteoporosis and hypovitaminosis D in women with advanced OA [13]. In the Chingford study [14], a similar increase in bone resorption was found in patients with progressive knee OA as in patients with OP. They measured the level of urinary N-terminal and C-terminal, type I collagen telopeptides, both validated markers of bone resorption. A lower bone mineral density has been observed in patients with trochanteric fractures than with cervical fractures [15], and OA may give a trend toward a reduced risk of femoral neck fractures compared to trochanteric femoral fractures [4, 5]. OP is a silent disease until fracture occurs, while OA AZD8055 manufacturer gives a gradual onset Romidepsin datasheet of symptoms. A possible way to study the relation between osteoporosis and osteoarthritis is to assess the presence of osteoarthritis in patients with an osteoporosis-related fracture, such as a hip fracture, and compare patients with a similar trauma, but who did not sustain a fracture. A study with hip contusion patients forming a control group has, to our

knowledge, not been performed previously. We, therefore, wanted to assess differences in the rate of hip OA between hip fracture and hip contusion patients. We also wanted to evaluate cervical and trochanteric femoral fractures in association with OA. Materials and methods We performed a retrospective, case–control study on 461 patients, 349 hip fracture patients (cases) and 112 hip contusion patients (controls). Hip fracture patients admitted from November 2003 to October 2004 were registered prospectively in the hospital’s fracture registry. Four hundred one hip fracture patients were identified. The exclusion criteria were patients aged <50 (n = 31), patients with a fracture in bone with a malignant disease (n = 6), patients with incomplete or missing radiographs (n = 14) and high-energy trauma (n = 1). This left 349 fracture

patients for further analysis. The fractured Methamphetamine hip was classified on the postoperative radiograph. Femoral neck fracture patients operated with arthroplasty (n = 89) were thus not included on the injured side. Preoperative radiographs were not used because they generally were of poor quality, but mainly because an intracapsular hematoma and the displacement of the femoral head in femoral neck fractures could influence the classifications, especially the minimal joint space (MJS). For ten patients, we could not retrieve the anteroposterior (AP) radiographs of the pelvis postoperatively. This left 250 patients with available postoperative radiographs of the fractured hip. Ninety-six of these were femoral neck fractures and 154 were trochanteric fractures. Separate analyses between the fracture types were performed. All 349 patients had interpretable radiographs of the non-injured side.

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