Solutions with concentrations of 10-3 and 10-4 M for PAH and PSP were prepared; in all cases, the mixtures had a 0.15 M NaCl to set the ionic strength. The pH

of both solutions was adjusted to 6.37 with NaOH or HCl [23]. The nanofilms were developed by either dipping the substrate into the 10-3/10-4 M solutions or by spraying the different solutions on the substrate. Therefore, up to four different growing conditions were studied (10-3 and 10-4 M of LbL dipping and 10-3 and 10-4 M of spray-assisted LbL). The anchoring layer of PEI led a positive superficial density charge onto EPZ-6438 purchase the fiber so that each bilayer shows the structure PSP/PAH. Films with 20, 40, 60, 80, and 100 bilayers were prepared in each growing configuration

in order to study the effects of the construction parameters. In the case of the dipping process, each construction cycle was performed by immersing the slide into the PSP solution for 2 min and then rising it in ultrapure water for 1 min; thereafter, it was dipped into the PAH mixture for 2 min and rinsed again for 1 min in ultrapure water. This process was repeated as many times as required for the film. The steps were similar for the spray technique: the polymeric solutions and ultrapure water were sprayed for 10 s onto the slides. Both methods were automated by using a robotic arm (in the case of the dipping construction) and a spraying robot (both of them acquired from Nadetech https://www.selleckchem.com/products/Nolvadex.html Innovations S.L., Sarriguren, Spain). Characterization

The films prepared were characterized in order to study the growing process depending on the construction conditions. One of the key parameters, roughness, was measured by an atomic force microscope (AFM) very (Veeco Innova, model 840-012-711; Veeco Instruments, Inc., Plainview, NJ, USA) in tapping mode; it was also used to register the thickness of the films by scratching the surface with a needle and scanning the cantilever perpendicularly to the scratch. For each sample, the AFM measurements were performed seven times in different zones to get the mean value and the standard deviation. AFM images were obtained by scanning 5 μm × 5 μm areas with 512 lines at a 0.1-Hz frequency. UV/Visible transmission spectra were recorded by a spectrometry transmission configuration, placing the glass slide under study in a holder between a white light source (HL2000; OceanOptics, Dunedin, FL, USA) and a spectrometer (USB2000XR1, OceanOptics). Finally, the contact angle was registered using a contact angle meter (KSV Instruments goniometer; Espoo, Finland) for each sample. Results and discussion As it was cited before, four sets of samples were prepared: 10-3 and 10-4 M of LbL dipping as well as 10-3 and 10-4 M of spray-assisted LbL. In each set, five slides were coated with different number of bilayers (20, 40, 60, 80, and 100).

albicans

flocculation by 30 μM FeCl 3 in YNB Microscopic analysis of the reference strain (DAY286) after exposure to 30 μM or 1.2 μM FeCl 3 in YNB. Cells were incubated at 30°C for 2 h. (TIFF 219 KB) Additional file 2: Deletion of HOG1 led to de-repression of MCFOs. Whole gel of the SDS-PAGE analysis shown in Figure. 4A. Δhog1 JMR114; Δpbs2 JJH31. (TIFF 91 KB) Additional file 3: SDS-PAGE analysis of proteins extracted from the Δ hog1 mutant cultivated in YPD medium and RIM. Whole gel of the SDS-PAGE described in Figure  4 C. (TIFF 108 KB) Additional check details file 4: Effect of cycloheximide pre-incubation on iron induced flocculation. (A) Relative sedimentation rates of DAY286 cells treated with cycloheximide (CHX)

C. albicans DAY286 was pre-treated either with 500 μg ml-1 CHX or MeOH in RPMI at 30°C for 15 min. Iron or water were subsequently added and cells were incubated at 30°C for 2 h. Sedimentation rates were determined as described in the experimental part. Means and standard deviations of three independent samples are shown (n = 3). ** denotes P ≤ 0.01 (student’s t-test). (B) Microscopic analysis of CHX or MeOH pre-treated Angiogenesis inhibitor cells (see A). (TIFF 482 KB) Additional file 5: ROS determination in the Δ hog1 (JMR114) mutant. Experiments for ROS accumulation in Δhog1 cells were performed twice (n = 2). Means and standard deviations are shown of one representative experiment where all samples were derived from the same pre-culture. *** denotes P < 0.001 (student’s t-test). (TIFF 13 KB) Additional file 6: Deletion of HOG1 had no influence on C. albicans growth in media with high iron concentrations. The WT (SC5314), the reference strain (DAY286), and the Δhog1 (JMR114) and Δpbs2 (JJH31) mutants were diluted in YPD each to ca. 0.5 · 106 cells ml-1 and further diluted in 1:10 steps. 5 μl of each cell suspension were dropped on RPMI agar plates containing

Fenbendazole 0 (RPMI), 1 or 30 μM FeCl3. Plates were incubated for 2 d at 30°C before pictures were taken. All plates were prepared in triplicates and one representative for each plate is shown. (TIFF 88 KB) References 1. Gow NA, van de Veerdonk FL, Brown AJ, Netea MG: Candida albicans morphogenesis and host defence: discriminating invasion from colonization. Nat Rev Microbiol 2012,10(2):112–122. 2. Pfaller MA, Diekema DJ: Epidemiology of invasive candidiasis: a persistent public health problem. Clin Microbiol Rev 2007,20(1):133–163.PubMedCrossRef 3. Sutak R, Lesuisse E, Tachezy J, Richardson DR: Crusade for iron: iron uptake in unicellular eukaryotes and its significance for virulence. Trends Microbiol 2008,16(6):261–268.PubMedCrossRef 4. Weinberg ED: Iron availability and infection. Biochim Biophys Acta 2009,1790(7):600–605.PubMedCrossRef 5. Nairz M, Schroll A, Sonnweber T, Weiss G: The struggle for iron – a metal at the host-pathogen interface. Cell Microbiol 2010,12(12):1691–1702.PubMedCrossRef 6.

02 to 24 ± 3.12 × 104/ml (Figure 2). At 12 h of exposure, the highest viability of cells was recorded: 6 ± 10.03 × 104/ml, which was consistently the same in all concentrations of exposure. However, at 24 h of exposure, the highest

viability (18 ± 2.14 × 104/ml) was recorded at the doses of 0.5 and 1.0 mg/l and the total cell count decreased from 16 ± 2.01 × 104/ml to 14 ± 1.02 × 104/ml at exposure of 2 to 5 mg/l ZnO NPs. This reflects that at high concentration the viability of coelomocytes decreases significantly. Similarly, at 36 h of exposure of up to 1 mg/l, the viability of coelomocytes recorded was 20 ± 2.01 × 104/ml, selleck chemicals and this was gradually decreased (14 ± 2.01 × 104/ml) by increasing the concentration of nanoparticles. At 48 h, the number of coelomocytes was similar to that of control (24 ± 2.12 × 104/ml) at 0.5 mg/l but gradually decreased with the increase in the concentration of nanoparticles. Results indicate that the viability of coelomocytes deceases with the increase in the concentration of NPs (100 nm). Figure 2 Viability of coelomocytes after exposure to ZnO NPs (100 nm) at different intervals. After exposure to 50-nm ZnO at 12 h, the viability recorded was 6 ± 1.0× 104/ml which was dependent on neither the size nor the concentration of NPs. However, at 24 h, the

uptake of NPs triggers cell replication and increases the number of coelomocytes from 10 ± 2.04 × 104/ml to 18 ± 3.12 × 104/ml (Figure 3). However, there was a little trend in the decrease in the number of coelomocytes: 14 ± 1.12 × 104/ml. At 48 h, the highest cell count was recorded at exposure of 0.5 mg/l. There was a gradual Cell Cycle inhibitor decrease in coelomocytes (18 ± 2.08 × 104/ml to 12 ± 1.06 × 104/ml). However, the total viability

ranges were between 6 ± 1.02 × 104/ml and 20 ± 3.12 × 104/ml. Results indicate that exposure up to 1 mg/l increases the replication of coelomocytes (Figure 4). Yang et al. [33] also recorded the uptake of NPs which depends on their size and concentration. Figure 3 Viability of coelomocytes after exposure to ZnO NPs (50 nm) at different intervals. Figure 4 Total viability of coelomocytes after exposure to ZnO NPs: (A) 100 nm and (B) 50 nm. Earthworms in general are tolerant to many chemical contaminants including heavy metals and organic pollutants in MRIP soil and can bioaccumulate them in their tissue [34]. They absorb the dissolved chemicals through their moist body wall due to the interstitial water and also ‘ingest’ by mouth while the soil passes through the gut. They either ‘biotransform’ or ‘biodegrade’ chemical contaminants, rendering them harmless in their bodies. Satchell [35] suggested that earthworms can uptake chemicals from soil pore water through passive ‘absorption’ of the dissolved fraction through their body wall. Coelomic uptake can also occur as soil is ingested and passed through the coelomic cavity.

The TMAs were constructed using a tissue array instrument (Beecher Instruments, Manual Tissue Arrayed, USA). A tissue core from Tanespimycin the donor block was removed using a thin-walled needle with an inner diameter of approximately 2.0 mm. Two core samples from each tumor

were precisely placed into a recipient block at specifically assigned locations. The array block was sectioned and leveled on the microscope slide, baked in an oven, and finally tested with routine H&E staining, immunohistochemistry (IHC), and in situ hybridization (ISH). IHC The expression levels of Hsp90-beta and annexin A1 were determined using an S-P combination of IHC techniques (UltraSensitive S-P Rabbit, Product Code: SP9000, Zhongshan Jinqiao biotech company, Beijing, China). IHC was strictly implemented according to the UltraSensitive S-P Rabbit kit. The first antibody concentration consisted of a rabbit anti-human Hsp90-beta polyclonal antibody (1:100 dilution; Product Code: BA0930, Bostere Biotech Company, Wuhan, China) and the rabbit anti-human annexin A1 (1:100 dilution; Product Code: 55018-1-AP, ProteinTech Group, Inc., USA). The kit provided positive slices that served as the positive control sample, and an identical volume of PBS as a replacement to the primary antibody incubated

in identical conditions was used as the negative control sample. Immunostaining was blindly evaluated by two independent experienced pathologists (Wang JS and Li J) according to a scoring method previously described selleck kinase inhibitor [11]. At least ten randomly selected high-power fields and >1,000 cells were counted for each section. Each specimen was scored according to the intensity of staining (intensity) and the area of staining (extent). Resveratrol The intensity was graded according to the following scale: 0, no staining; 1+, mild staining; 2+, moderate staining; 3+, intense staining. The

extent was evaluated as follows: 0, no staining of cells in any microscopic fields; 1+, <30% of tissue stained positive; 2+, between 30% and 60% stained positive; 3+, >60% stained positive. A combined staining score (intensity + extension) of ≤2, between 3 and 4, and between 5 and 6 were considered as low, moderate, and high expression levels, respectively ISH The mRNA expression levels of Hsp90-beta and annexin A1 were determined by ISH. Initially, the mRNA sequences of Hsp90-beta and annexin A1 were identified in the GeneBank (MedLine, USA). The oligonucleotide probe sequences of Hsp90-beta and annexin A1 were designed using the oligonucleotide probe designing software (Vector NTI 9.0). The probe sequence of Hsp90-beta was 5′-TACCA GTGCT GCTGT AACTG AAGAA ATGCC-3′, and that of annexin A1 was 5′-TACAC CAAGT ACAGT AAGCA TGACA TGAAC AAAGT-3′. Finally, the probes were synthesized in a DNA synthesizing instrument (Bostere biotech company, Wuhan, China).

Bold-faced underlined text shows number of isolates of each host in the specific BAPS cluster. Admixture was mainly found in clusters 1 and 4 for a total of nine STs (12.2%) including a total of 18 isolates (7.2%). Mainly novel STs in the ST-21 complex (two STs), ST-48 complex (one ST), ST-658 complex (one ST), ST-1962 and ST-1970 were found to be admixed. However, also ST-618 (ST-61 CC), ST-945 (ST-1287 CC) and ST-58 (unassigned) were significantly admixed. Bovine isolates were found to be associated

with admixture (p = 0.05). BAPS clusters 4 and 5 were associated with the bovine isolates (Table 2), BAPS cluster 1 was associated with Selleck GSK3235025 the poultry isolates and BAPS clusters 2 and 3 were not associated with any host. Bovine isolates were found in selleck screening library bovine-associated clusters in 71.7% of cases. Of the poultry isolates 72.7% were found in the poultry-associated cluster. Human isolates

were found in the bovine-associated BAPS cluster 4 in 44.3% of the cases and in 45.4% of the cases found in the poultry-associated BAPS cluster 1. The NJ tree shown in Figure 1 illustrates the molecular variation within and between the clusters estimated by BAPS from a phylogenetic perspective. eBURST analysis yielded seven groups containing two (smallest group) to 12 (biggest group) STs and 34 singletons. Table 3 shows the degree of similarity between the eBURST groups and BAPS populations. The biggest BAPS clusters (1 and 4) were made up of several eBURST groups, while BAPS cluster 2 did not have an equivalent eBURST group. Figure 1 Neighbour-joining tree illustrating BAPS clusters Dapagliflozin from a phylogenetic perspective. BAPS cluster 1: Red; BAPS cluster 2: Green; BAPS cluster 3: Blue; BAPS cluster 4: Yellow; BAPS cluster 5: Purple. Table 3 Number

of STs of Campylobacter jejuni assigned to both a BAPS population and an eBURST group BAPS populations eBURST groups   1 2 3 4 5 6 7 1 1 10     3     2               3             2 4 11   1 4   3   5     5         Discussion Our study revealed a high diversity of MLSTs among 102 bovine C. jejuni isolates obtained from three major Finnish slaughterhouses, representing 81 farms, in 2003. A total of 50 STs (nine CCs) were observed, nearly half of which were novel, emerging mostly from new combinations of known alleles and in two cases from new alleles carrying a one-nucleotide difference from alleles commonly found in cattle (pgm allele 2, tkt allele 1 and uncA allele 17).

Numerous studies have described

many virulence factors that are essential to suppress host immune responses [2, 31]. The direct contributions of these Sotrastaurin nmr virulence factors to bacterial dissemination, however, are still unclear. The study of dissemination per se is a field that is lagging behind in plague research. BLI is a tool that allows for the visualization of a pathogen in a host during infection and a very promising alternative to better understand Y. pestis dissemination. A recent report described the use of BLI in a subcutaneous (SC) model of bubonic plague [25]. In this report, the pGEN-luxCDABE plasmid was described to have no effect on the virulence of Y. pestis and to be suitable for BLI as luminosity correlated with bacterial counts in vivo; our results confirmed and expanded upon these findings. Our goal was to determine whether www.selleckchem.com/products/PF-2341066.html BLI could be used to follow dissemination and colonization of Y. pestis

in mice after using different routes of inoculation that closely mimic bubonic and pneumonic plague. Moreover, we tested whether BLI could be used to detect mutants with defects in colonization or dissemination. After inoculation with a strain of Y. pestis that contains pGEN-luxCDABE, we showed that animals can be imaged through the course of infection in such a way that bacterial spread could be followed over time for three different models of infection. Our results

from the SC inoculation model support the previous notion that, during bubonic plague, Y. pestis travels from the site of inoculation to the proximal lymph node prior to dissemination to deeper tissues Immune system [16]. We observed that bacteria were maintained at the site of inoculation during the course of infection, as previously reported for ear intradermal (ID) infections [15]. For both, the SC and ID models, the bacterial population at the site of inoculation appeared not only to be maintained, but also to expand. However, while we quantified signal from the site of infection in the SC-inoculated animals, we cannot conclude such signal comes from the skin alone. In our SC model, the patch of inoculated skin is located in an anatomical position on top of the superficial cervical LNs and thus, both, skin and LNs, are imaged as a single source of radiance. We could determine that signal was coming partly from the site of inoculation after removing the patch of skin and imaging it individually. This complication is minimized in the ID model, where the site of inoculation (ear pinna) is distant from the draining LN (superficial parotid LN). While an increase overtime in signal intensity from the ear was observed, we were not able to quantify the signal, as it was difficult to place the ears of all mice at the same position inside of the animal isolation chamber.

bovis BCG Moreau provides valuable information regarding specific proteins, many of which have been implicated in protective immune responses, and helps defining candidates for future vaccination strategies. Methods Bacterial strains and growth conditions Mycobacterium bovis BCG Pasteur 1173P2 was obtained from the Pasteur Institute

(Paris, France) culture collection, and stocks were maintained at -80°C. Mycobacterium bovis BCG Moreau was provided by Fundação Ataulpho de Paiva (FAP). Both strains were cultured as surface pellicles, for 2 weeks at 37°C, in 100 ml of Sauton vaccine production medium, provided by FAP. Sample BAY 73-4506 mouse preparation Culture filtrate proteins (CFPs) were obtained after separation of culture supernatants from the bacterial pellicles and subsequent centrifugation at 2,500 × g for 10 min at 4°C. The resulting supernatant was filtered through a 0.22 μm low protein binding membrane (Millipore Express; Millipore, Bedford, MA, USA) in order to remove any remaining bacteria. CFPs (on average 5.5 mg total protein) were precipitated with 17% (v/v) TCA and washed with cold acetone. Finally, proteins were dissolved in 1.5 ml of IEF buffer (8 M urea, 2% CHAPS, 4 mM tributylphosphine [TBP], 0.4% ampholytes pH 3-10) for 1 h at room temperature. Lumacaftor price Protein concentration

was determined using the RC-DC Kit (Bio-Rad). Proteins were stored at -80°C until analysis. Two dimensional gel electrophoresis (2DE) IPG strips and all 2DE reagents were purchased from Bio-Rad (Hercules, CA, USA). Isoelectric focusing was performed at 20°C on 17 cm

IPG strips, using 500 μg of CFPs diluted in a final volume of 300 μl in rehydration buffer (8 M urea, 2% CHAPS, 4 mM TBP, 0.4% ampholytes pH 3-10). Samples were applied to IPG strips (pH intervals of 3-6, 4-7 and 5-8) by in-gel rehydration and incubated for 1 h at room temperature. Isoelectric focusing was performed on a Protean® IEF cell (Bio-Rad) with maximum current of 50 μA/strip. Focusing parameters used for IPG strips in the pH range 4-7 and 5-8 were: active rehydration (50 V) for 11 h; step 1- linear gradient from 1 to 250 V over 20 min; step 2 – linear gradient from 250 to 10,000 V over 2 h; step 3- constant 10,000 V until 80,000 Vh was achieved. For IPG strips in Calpain the pH range 3-6, step 3 was constant 10,000 V until 60,000 Vh was achieved. After isoelectric focusing, proteins were reduced in 130 mM DTT and alkylated in 270 mM iodoacetamide, both in equilibration buffer (6 M urea, 2% SDS, 375 mM Tris-HCl pH 8.8, 20% glycerol). Second dimension separation was done in 17 cm, 12% or 15% SDS-PAGE gels, 1.0 mm thick, using a vertical system (Bio-Rad) in standard Laemli buffer [84] at 40 mA/gel, 10°C, until the tracking dye left the gel. Protein visualization and image analysis Gels were stained with colloidal Coomassie Brilliant Blue G-250 essentially as described [85], and documented using a GS-800™ auto-calibrating imaging densitometer (Bio-Rad).

Disks were observed for colour change up to 60 min. β-lactamase producer strain ATCC 29213 (#1) and β-lactamase negative strain ATCC 25923 (#2), were used as positive and negative controls respectively. Antibiotic susceptibility testing – disk diffusion and E-test The standard procedure recommended by CLSI was followed [41, 42]. Briefly, inoculum was prepared by the direct colony suspension method preferred for S.

aureus. Isolated colonies from non-selective overnight BHI agar plates were used to make a saline suspension, and turbidity was adjusted equivalent to a 0.5 McFarland turbidity standard. Thereafter, the standardized inoculum was spread uniformly on a Mueller Hinton II agar plate, allowed to dry, cefazolin disk applied to the centre of the plate, and plates incubated at 35°C for 20–24 h. The zones of inhibition MG-132 solubility dmso were selleck chemical measured and compared

against CLSI Zone Diameter Interpretive Charts, to categorize isolates as susceptible, intermediate or resistant. (The CLSI 2012 charts were used, which were most current at the time of the experiments [41]). S. aureus ATCC 25923 (#2) was included in each experiment as the CLSI recommended quality control strain for disk diffusion [41]. For the zone edge test comparison criteria, ATCC 29213 (#1) and ATCC 25923 (#2) were used as the CLSI recommended positive and negative controls, showing ‘sharp’ and ‘fuzzy’ inhibition zone edges respectively. For the E-test, cefoxitin or cefepime E-test strip was applied to the inoculated plate, and following incubation at 35°C for 24 h, the MIC value was read. The CLSI interpretive criteria, most current at the time of experiments, were used to categorize isolates as susceptible, intermediate or resistant [41]. S. aureus ATCC 29213 (#1) was included in each experiment as the recommended quality control for MIC determination [41]. Experiments were similarly performed

with ‘induced’ growth cultures, wherein bacteria grown in presence of penicillin disks overnight were used as Sunitinib nmr the starting inoculum to prepare the saline suspension. The standard procedure described above was followed. Results β-LEAF assays determine β-lactamase production and assess cefazolin activity We used a panel of S. aureus comprising two ATCC strains and 25 clinical isolates (Table 1) as a model system. Isolate numbers (eg. #1, #4, etc.), rather than full names, are used to refer to isolates as per Table 1 throughout this study. ATCC strains with established β-lactamase status, β-lactamase producing strain 29213 (#1) and β-lactamase negative strain 25923 (#2) were used as positive and negative controls respectively. Cefazolin, a first generation cephalosporin, was used as the test antibiotic in these experiments. Each isolate was assayed under two conditions, with β-LEAF alone and with β-LEAF and saturating concentration of cefazolin (2500-fold higher concentration of cefazolin than β-LEAF) respectively.

Imaging of Fluorescence Emission from Plant Tissues is presented by Zuzana Benediktyová and Ladislav Nedbal. Exploring Photosynthesis by Electron Tomography is reviewed by Martin F. Hohmann-Marriott and Robert W. Robertson; it summarizes its application to resolve ultrastructures of photosynthetic click here organisms within a few nanometers. Single Particle Electron Microscopy is presented by Egbert J. Boekema, Mihaela Folea, and Roman Kouřil. Simon Scheuring and James N. Stugis provide rationale for imaging, at high resolution, of a native photosynthetic membrane by Atomic Force Microscopy (AFM) to study supramolecular

assembly of the photosynthetic complexes; Scheuring and Stugis show that AFM bridges the resolution gap between atomic structures selleck kinase inhibitor and cellular ultrastructures. MRI is a non-destructive and non-invasive technique that can be used to study the dynamics of plant water relations and water transport. Henk van As, Tom Scheenen, and Frank J. Vergeldt provide an account of MRI techniques that can be used to study plant performance in relation to its photosynthetic activity. Structural methods can be divided into two: (1) for determining

geometric structures and (2) for revealing electronic structures. For understanding how electrons are transferred within an electron transfer chain, or how chemical bonds, which are made up by electrons, are split and rearranged, information on both geometric and electronic structures are equally important for understanding the underlying design principles of unique photosynthetic catalysts. Mei Li and Wen-rui Chang, as well as James P. Allen, Chenda Seng, and Chadwick Larson describe, in two separate contributions, the basics of Protein Crystallography and X-ray Diffraction. Depending on the resolution, this approach can give very detailed information on the geometric structure of the proteins, their cofactors,

and sometimes of bound substrates or products; “snapshots” are taken on deep frozen crystalline samples and provide the structural basis for understanding how proteins function. Junko Yano and Vittal Yachandra describe how X-ray Spectroscopy can be employed to obtain high-resolution data of metal–metal STK38 and metal–ligand distances in active sites of proteins without the need for crystallization of the protein. This technique and the related X-ray Fluorescence method described by Uwe Bergmann and Pieter Glatzel provide important information on the electronic structures of (metal) cofactors. While these X-ray spectroscopy experiments are currently mostly performed with samples frozen in different intermediate states of the catalytic cycle, kinetic X-ray spectroscopy experiments at room temperature can also be performed; these experiments have started to give important information on dynamic changes at (metal) cofactor sites.

A further issue is the capacity for primary care to offer preconception counselling. As discussed by Ten Kate (2012), a study of preconception counselling in primary care found that 42 % of couples required further action by the GP and 4 % referral learn more to a clinical geneticist based upon identified risks. In the Netherlands, preconception care has become more integrated into primary care partly through the establishment of midwifery-led clinics (Riedijk et al. 2012). If the costs of next-generation sequencing fall as predicted

(Ropers 2012), offering preconception counselling will only become more complex but there are insufficient specialist genetic services available to provide this counselling. New models of providing preconception care in the community need to be developed and evaluated if we are to offer couples the opportunity to make informed decisions about the growing array of genetic tests that will be available soon. References Bennett R, Mulvihill (2012) The importance of family medical history in preconception consultation. J Community Genet 3. doi:10.​1007/​s12687-012-0107-z

De Wert GMWR, Dondorp WJ, Knoppers BM (2012) Preconception care and genetic risk: ethical issues. J Community Genet 3. doi:10.​1007/​s12687-011-0074-9 Hamamy H (2012) Consanguineous marriages. Preconception consultation in primary health EPZ6438 care settings. J Bay 11-7085 Community Genet 3. doi:10.​1007/​s12687-011-0072-y

Metcalfe S (2012) Carrier screening in preconception consultation in primary care. J Community Genet 3. doi:10.​1007/​s12687-011-0071-z Mulvihill JJ (2012) Preconception exposure to mutagens: medical and other exposures to radiation and chemicals. J Community Genet 3. doi:10.​1007/​s12687-012-0104-2 Read A, Donnai D (2012) What can be offered to couples at (possible) increased genetic risk? J Community Genet 3. doi:10.​1007/​s12687-012-0105-1 Riedijk S, Oudesluijs G, Tibben A (2012) Psychosocial aspects of preconception consultation in primary care: lessons from our experience in clinical genetics. J Community Genet 3. doi:10.​1007/​s12687-012-0095-z Ropers HH (2012) On the future of genetic risk assessment. J Community Genet 3. doi:10.​1007/​s12687-012-0092-2 Ten Kate LP (2012) Genetic risk. J Community Genet 3. doi:10.​1007/​s12687-011-0066-9″
“Introduction Preconception care aims to provide prospective parents information and support with regard to preconception measures that are conducive to a healthy pregnancy-outcome for mother and child (Health Council of the Netherlands 2007; Atrash et al. 2008). Experience with preconception care as a systematic approach to promoting reproductive health is still limited, as is ethical thinking about conditions and implications. Preconception care then is a practice in the making, still looking for its own identity (Delvoye et al. 2009).