Low compliance with monitoring of waist measurement and lipid levels and inaccurate

information held on CPMS. The Trust management clozapine plan and policy of clozapine have been altered as a result of the audit. Clozapine check details treatment is associated with a potentially fatal agranulocytosis and thus registration with a clozapine monitoring service, e.g. Clozaril Patient Monitoring Service (CPMS), is required 1. NICE recommends annual monitoring of weight, waist measurement, blood pressure, blood glucose, and lipid levels and also gives guidance on clozapine augmentation 2. Inpatients on clozapine subject to Section 58 of the Mental Health Act must have a T2/T3 form specifying clozapine use and a maximum antipsychotic dose. The audit see more aims to evaluate compliance with clozapine therapy associated requirements. The population

consisted of all patients registered with active clozapine treatment on CPMS (141). Alternative patients registered on CPMS were selected for the audit. A criteria based data collection tool was developed with web-based software and used for collecting and analysing data. Medical notes, medicines administration record charts and T2/T3 forms of selected patients were examined on a retrospective basis from both inpatient and outpatient units. The audit was undertaken in November 2012-February 2013. Ethics approval was not required. A sample size of seventy-six patients, giving a confidence Glycogen branching enzyme level of 80%, was audited. Compliance with NICE recommended annual monitoring for seventy-one patients (five patients started the therapy less than 12months ago) is shown in the table 1. Accuracy of the data held on CPMS is summarised in the table 2. Table 1: Annual physical monitoring compliance with NICE Parameter Compliance Weight 65/71 (92%) Blood pressure 64/71 (90%) Waist measurement 6/71 (8%) Blood glucose 50/71 (70%) Lipid levels 29/71 (41%) Table 2: Accuracy of data held on CPMS Parameter Correct data Medical officer 55/76 (72%) Case holder

12/76 (16%) Team base 55/76 (72%) An additional antipsychotic drug for clozapine treatment augmentation was prescribed in thirteen patients and after the six week recommended trial. However, clozapine therapeutic levels were measured for only ten patients. Full compliance (100%) was observed for specifying treatment with clozapine and maximum antipsychotic dose on the T2/T3 forms. The audit also revealed that four patients were using clozapine for unlicensed indications without the required Drug and Therapeutic committee (DTC) approval. Poor compliance of physical monitoring with regards to waist measurement and lipid levels was observed. Recommendations to modify a currently used physical monitoring form for clozapine by including NICE monitoring advice was made and implemented.

Since the first report of ESBLs in 2002 (Chanawong

et al., 2002), blaCTX-M has been predominant in mainland (Yu et al., 2007; Liu et al., 2009). In this multicentre study, the prevalence of ESBL production in K. pneumoniae has been demonstrated to be about 40%. Of 158 ESBL-producers, the isolates harboring ESBL genes and blaCTX-M-14 were 94.3% and 49.4%, respectively, and were shown to increase 10% and 9% to those in another large-scale study (Yu et al., 2007), respectively. The proportion of blaCTX-M increased 12% compared to the percentage (72.3%) described in a report of southern China three years ago (Liu et al., 2009) and doubled the percentage reported nine years ago (Li et al., 2003). Because the usage of plasmid-based amplification method in this study and the potential Birinapant false-negative products

owing to the unbinding on some novel bla, the detection of β-lactamase genes click here may have been underestimated. Although there are some differences in the source of the isolates in our study as compared to the studies mentioned above, our results clearly suggest the increasing prevalence of blaCTX-M in K. pneumoniae in China. CTX-M-type ESBLs exhibit powerful activity against cefotaxime and ceftriaxone but generally not against ceftazidime, and several variants with enhanced ceftazidimase activity have been reported (Poirel et al., 2002; Bonnet et al., 2003; Rebamipide Rossolini et al., 2008). In this study, it was observed that the isolates harboring CTX-M-15 or CTX-M-27 alone exhibited higher resistance rates to ceftazidime and aztreonam than that in subgroup CTX-M-14 without other ESBLs

(Table 2). Further, a high percentage of isolates harboring blaCTX-M-27 demonstrated the MDR phenotype. To our knowledge, this is the first study about the high prevalence of CTX-M-27 in Enterobacteriaceae in China. This warrants for an active surveillance to monitor these resistant bacteria. The overall resistance rates to the tested β-lactam antimicrobial agents were over 30% except for cefepime, piperacillin/tazobactam, and cefotetan in this study. As shown in Table 2, only 9.3% isolates harboring CTX-M-14 alone showed resistance to cefepime, but 50% isolates harboring CTX-M-15 exhibited resistance (P < 0.01), and a 100% resistance rate when CTX-M-15 coexisted with other ESBLs. Nevertheless, piperacillin/tazobactam show only 10.1% resistance rate in vitro, although the proportion increased to 26.7% when the isolates contained two types of ESBLs(blaCTX-M + blaSHV)(Table 1). Several clinical intervention studies also supported that piperacillin/tazobactam may contribute to preventing the ESBL-producing K. pneumoniae outbreaks (Lee et al., 2007; Tangden et al., 2011). These properties highlight the value of piperacillin/tazobactam as empirical therapy for infections by suspected organisms possessing a single ESBL (especially the blaCTX-M).

Since the first report of ESBLs in 2002 (Chanawong

et al., 2002), blaCTX-M has been predominant in mainland (Yu et al., 2007; Liu et al., 2009). In this multicentre study, the prevalence of ESBL production in K. pneumoniae has been demonstrated to be about 40%. Of 158 ESBL-producers, the isolates harboring ESBL genes and blaCTX-M-14 were 94.3% and 49.4%, respectively, and were shown to increase 10% and 9% to those in another large-scale study (Yu et al., 2007), respectively. The proportion of blaCTX-M increased 12% compared to the percentage (72.3%) described in a report of southern China three years ago (Liu et al., 2009) and doubled the percentage reported nine years ago (Li et al., 2003). Because the usage of plasmid-based amplification method in this study and the potential Anti-diabetic Compound Library purchase false-negative products

owing to the unbinding on some novel bla, the detection of β-lactamase genes Ivacaftor mw may have been underestimated. Although there are some differences in the source of the isolates in our study as compared to the studies mentioned above, our results clearly suggest the increasing prevalence of blaCTX-M in K. pneumoniae in China. CTX-M-type ESBLs exhibit powerful activity against cefotaxime and ceftriaxone but generally not against ceftazidime, and several variants with enhanced ceftazidimase activity have been reported (Poirel et al., 2002; Bonnet et al., 2003; Anacetrapib Rossolini et al., 2008). In this study, it was observed that the isolates harboring CTX-M-15 or CTX-M-27 alone exhibited higher resistance rates to ceftazidime and aztreonam than that in subgroup CTX-M-14 without other ESBLs

(Table 2). Further, a high percentage of isolates harboring blaCTX-M-27 demonstrated the MDR phenotype. To our knowledge, this is the first study about the high prevalence of CTX-M-27 in Enterobacteriaceae in China. This warrants for an active surveillance to monitor these resistant bacteria. The overall resistance rates to the tested β-lactam antimicrobial agents were over 30% except for cefepime, piperacillin/tazobactam, and cefotetan in this study. As shown in Table 2, only 9.3% isolates harboring CTX-M-14 alone showed resistance to cefepime, but 50% isolates harboring CTX-M-15 exhibited resistance (P < 0.01), and a 100% resistance rate when CTX-M-15 coexisted with other ESBLs. Nevertheless, piperacillin/tazobactam show only 10.1% resistance rate in vitro, although the proportion increased to 26.7% when the isolates contained two types of ESBLs(blaCTX-M + blaSHV)(Table 1). Several clinical intervention studies also supported that piperacillin/tazobactam may contribute to preventing the ESBL-producing K. pneumoniae outbreaks (Lee et al., 2007; Tangden et al., 2011). These properties highlight the value of piperacillin/tazobactam as empirical therapy for infections by suspected organisms possessing a single ESBL (especially the blaCTX-M).

The aim of this review is to identify studies investigating the acute effects of weight training on blood glucose levels in type 1 diabetes. A search of Cumulative Index to Nursing and Allied Health Literature,

Cochrane, Medline and SPORTDiscus databases was conducted. A systematic review of these studies was undertaken to address the issue. After fulfilling the inclusion criteria, eight articles were retrieved. The individual studies reported comparatively different results. Study findings from this review are inconclusive regarding the acute glycaemic response to weight training exercise. Analyses of the MAPK inhibitor intervention studies highlight that weight training may increase, minimally affect or decrease post-exercise glycaemia in type buy JQ1 1 diabetes. It is likely that the heterogeneity regarding the weight training methods used among the studies, as well as the pre/post-exercise insulin and carbohydrate intake of the study participants have impacted on the findings. There remains a gap in the evidence base to inform health care professionals of the likely acute glycaemic response to weight training exercise. Problems in managing patient glycaemia may arise due to erroneous insulin and carbohydrate alterations based on unfounded and anecdotal-based guidance. The studies highlighted in this review have reported some of the potential effects that weight training

may have on glycaemia. Copyright © 2012 John Wiley & Sons. “
“Although metabolic and cardiovascular effects of resistance exercise in type 1 diabetes (T1DM) remain poorly explored, research employing type 2 diabetes suggests glycaemic and cardiovascular benefits. However, this intense exercise carries some risks. Here we describe the cardiovascular and metabolic responses of a newly

diagnosed, previously sedentary T1DM individual experiencing syncope during an unaccustomed acute bout of resistance exercise. The cause of this exercise-induced incident was attributed to inappropriate cardiovascular control and lack of habituation to accompanying acid-base disturbances. Careful consideration of exercise intensity and progression in previously sedentary T1DM performing resistance exercise sessions is warranted. Copyright © 2013 John Wiley & Sons. “
“The objective of this Sorafenib concentration study was to introduce a practical insulin protocol for hospital inpatients with hyperglycaemia. The acronym BBB emphasised the insulin supply in three components, basal, bolus (nutrition correction) and booster (blood glucose level [BGL] correction). The insulin dosage was based on patient weight and adjusted to BGL at pre-specified times. Compliance of BGL measurements and insulin injections, and efficacy were evaluated prospectively. Fifty-seven hospital inpatients with significant hyperglycaemia were treated and compared with 45 historical controls (with similar age, HbA1c and diabetes duration) treated with sliding scale insulin (SSI).

The aim of this review is to identify studies investigating the acute effects of weight training on blood glucose levels in type 1 diabetes. A search of Cumulative Index to Nursing and Allied Health Literature,

Cochrane, Medline and SPORTDiscus databases was conducted. A systematic review of these studies was undertaken to address the issue. After fulfilling the inclusion criteria, eight articles were retrieved. The individual studies reported comparatively different results. Study findings from this review are inconclusive regarding the acute glycaemic response to weight training exercise. Analyses of the Ceritinib intervention studies highlight that weight training may increase, minimally affect or decrease post-exercise glycaemia in type Dabrafenib supplier 1 diabetes. It is likely that the heterogeneity regarding the weight training methods used among the studies, as well as the pre/post-exercise insulin and carbohydrate intake of the study participants have impacted on the findings. There remains a gap in the evidence base to inform health care professionals of the likely acute glycaemic response to weight training exercise. Problems in managing patient glycaemia may arise due to erroneous insulin and carbohydrate alterations based on unfounded and anecdotal-based guidance. The studies highlighted in this review have reported some of the potential effects that weight training

may have on glycaemia. Copyright © 2012 John Wiley & Sons. “
“Although metabolic and cardiovascular effects of resistance exercise in type 1 diabetes (T1DM) remain poorly explored, research employing type 2 diabetes suggests glycaemic and cardiovascular benefits. However, this intense exercise carries some risks. Here we describe the cardiovascular and metabolic responses of a newly

diagnosed, previously sedentary T1DM individual experiencing syncope during an unaccustomed acute bout of resistance exercise. The cause of this exercise-induced incident was attributed to inappropriate cardiovascular control and lack of habituation to accompanying acid-base disturbances. Careful consideration of exercise intensity and progression in previously sedentary T1DM performing resistance exercise sessions is warranted. Copyright © 2013 John Wiley & Sons. “
“The objective of this Bacterial neuraminidase study was to introduce a practical insulin protocol for hospital inpatients with hyperglycaemia. The acronym BBB emphasised the insulin supply in three components, basal, bolus (nutrition correction) and booster (blood glucose level [BGL] correction). The insulin dosage was based on patient weight and adjusted to BGL at pre-specified times. Compliance of BGL measurements and insulin injections, and efficacy were evaluated prospectively. Fifty-seven hospital inpatients with significant hyperglycaemia were treated and compared with 45 historical controls (with similar age, HbA1c and diabetes duration) treated with sliding scale insulin (SSI).

marinintestina IK-1. This work was partly supported by the National Institute of Polar Research. T.N. and R.H. contributed equally to this work. “
“Staphylococcus aureus MrgA (encoded by mrgA) belongs to the Dps family of proteins, which play important roles in coping with various

stresses. The staphylococcal mrgA gene is specifically expressed under oxidative stress conditions and is one of the most highly induced genes during phagocytic killing by macrophages. We previously reported that mrgA is essential for oxidative stress resistance, and can cause nucleoid compaction. However, whether nucleoid compaction by itself would contribute to oxidative stress resistance was hard to determine, because Dps family proteins generally have ferroxidase activity to prevent hydroxyl radical formation via the Fenton reaction. Lenvatinib In this study, we resolved the crystal structure of MrgA and conducted mutation analysis of Asp56 and Glu60, which are located at the expected ferroxidase centre. In the strain expressing

Asp56Ala/Glu60Ala MrgA (termed MrgA*), MrgA* retained dodecamer formation and nucleoid compaction ability. By contrast, the PD-166866 clinical trial ferroxidase activity of MrgA* decreased by about half. Viability of the mrgA* strain was as low as the mrgA null mutant in oxidative stress and phagocytic killing assays. These results suggest that nucleoid compaction by itself is insufficient for oxidative stress resistance, and Asp56 and Glu60 constitute essential molecular sites in MrgA

for oxidative stress resistance and survival against phagocytic killing. “
“Patients suffering from major depression have repeatedly been reported to have dysregulations in hypothalamus–pituitary–adrenal (HPA) axis activity along with deficits in cognitive processes related to hippocampal and prefrontal cortex (PFC) malfunction. Here, we utilized three mouse lines selectively bred for high (HR), Fenbendazole intermediate, or low (LR) stress reactivity, determined by the corticosterone response to a psychological stressor, probing the behavioral and functional consequences of increased vs. decreased HPA axis reactivity on the hippocampus and PFC. We assessed performance in hippocampus- and PFC-dependent tasks and determined the volume, basal activity, and neuronal integrity of the hippocampus and PFC using in vivo manganese-enhanced magnetic resonance imaging and proton magnetic resonance spectroscopy. The hippocampal proteomes of HR and LR mice were also compared using two-dimensional gel electrophoresis and mass spectrometry. HR mice were found to have deficits in the performance of hippocampus- and PFC-dependent tests and showed decreased N-acetylaspartate levels in the right dorsal hippocampus and PFC. In addition, the basal activity of the hippocampus, as assessed by manganese-enhanced magnetic resonance imaging, was reduced in HR mice. The three mouse lines, however, did not differ in hippocampal volume.

salmonis

proteins, the amino acid sequences of Ps-Tox and PS-Antox were analysed using the protparam tool of the Expasy Proteomic Server. The molecular weight of the Ps-Antox protein was 8.9 kDa and its theoretical pI is 4.79. The predicted molecular weight of Ps-Tox was 15.9 kDa with a pI of 6.7. In order to characterize this pair of predicted proteins, we cloned the ps-Antox and ps-Tox genes into the pET27b+ expression vector, either individually or together and attempted to express the genes in E. coli BL21 DE3. After the IPTG induction, the expression of the recombinants proteins was checked UK-371804 molecular weight every 1 h for a 3-h period, finding that the greatest amount of the two proteins is obtained 2-h post-IPTG induction. The expression level of Ps-Antox was much lower than that of its partner Ps-Tox when expressed alone (Fig. 2). When the two proteins were expressed simultaneously in a bicistronic operon the expression level of both proteins was similar, not showing a significant

polar effect (Fig. 2). To determine the toxic proprieties of the P. salmonis www.selleckchem.com/products/MS-275.html toxin, we made cultures of the E. coli transformant cells in the presence of IPTG. The growth of the E. coli carrying the pET27b+ vector that contains the ps-Tox gene was minimal in the presence of IPTG during 8 h of growth kinetics (Fig. 3a). In contrast, the growth of E. coli strains that contained the ps-Antox and ps-Tox-Antox in the pET27b+ was normal compared with the host that had the vector without insertion (Fig. 3a). All the transformants strains grew normally in the these absence of IPTG, including the strain with the ps-Tox gene in the pET27b+ vector (Fig. 3b). When the strains were streaked out on LB agar plates supplemented with IPTG, the results were the same as those obtained in LB broth (data not

shown). The model constructed is presented in Fig. 4b and c. In general, the secondary structure is conserved compared with that of the M. tuberculosis VapC-5 toxin. Some amino acids implicated in the toxin function are conserved, in particular, three of the four acidic amino acids present in the PIN domains that are related with an exonuclease activity (Miallau et al., 2008), VapC-5: D26, E57, D115, D135, and Ps-Tox: D6, E44, D100, and E121, as can be seen Fig. 4a (see Table S1). In order to determine whether the newly described toxin behaves in the same way as most described toxins, we tested Ps-Tox for putative RNAse activity. When P. salmonis RNA was treated with a crude extract of E. coli containing the recombinant Ps-Tox protein, a significant degradation was observed compared with that of the untreated sample (Fig. 5, lanes 2 and 6, respectively). The same effect was observed in the corresponding extract containing Ps-Antox and Ps-Tox-Antox proteins (Fig. 5, lanes 1 and 3, respectively). The RNA degradation produced by the protein extract that contains Ps-Antox and Ps-Tox-Antox could also have been produced by E.

CtpA from P. aeruginosa, however, behaves differently. At least under the experimental conditions used here, this does not contradict our abovementioned hypothesis of an extracellular localization STA-9090 of C. trachomatis CtpA, but demonstrates that P. aeruginosa CtpA is in fact a periplasmic protease and that the subcellular localization is an important protein characteristic that must be determined to understand

the physiological role of the protein. The same can be said for CTPs from Gram-positive bacteria as bioinformatic analysis of genomic sequence data suggests that these CTPs are secreted to the extracellular environment. CtpA of P. aeruginosa will remain in the periplasm and is not secreted to the extracellular environment or present in the outer membrane. Several dozen reports have been published about bacterial CTPs after the initial study of Hara et Epacadostat cell line al. (1991). Most refer to CTPs as periplasmic proteases, although the experimental evidence

for the individual protein was not given. As far as we know, we are the first to confirm experimentally the exclusive periplasmic localization of a CTP-3 of P. aeruginosa. The periplasmic localization of CtpA strictly excludes the possibility that the protein is directly involved in the virulence of P. aeruginosa as an extracellular effector molecule. The obvious role of CTPs in the virulence of pathogenic bacteria, as shown experimentally in B. suis, B. bacilliformis and B. mallei (Mitchell & Minnick, 1997; Bandara et al., 2005, 2008; Lad et al., 2007) and P. aeruginosa (R. Hoge et al., unpublished data), must be due to an indirect effect mediated by 4��8C a substrate protein of CTP in the context of a periplasmic function. Equivalent to the evolution and function of CTPs from phototrophic organisms, CTPs from Gram-negative

bacteria may be required to activate periplasmatic proteins by cleavage, just as the photosynthetic D1 protein is activated in plant cells. A good candidate as a substrate protein would be the PBP-3. Their periplasmic localization would support evidence of the Prc substrates in E. coli identified by their subcellular localization, because PBP-3 is anchored in the cytoplasmic membrane with the C-terminal end facing the periplasm (Nguyen-Distèche et al., 1998). As PBP-3 in E. coli is involved in the essential process of cell wall synthesis and the CTP could function as an activator of PBP-3, E. coli PBP-3 is thought to be a key element cell division in which it presumably initiates polymerization of the septum peptidoglycan by catalysing a transpeptidation reaction during cell division (Nguyen-Distèche et al., 1998).

Current responses were recorded using

an Axopatch 200B amplifier (Molecular Devices, Sunnyvale, CA, USA) and the pclamp software (version 9.2; Molecular Devices). Signals were filtered at 1 kHz and digitized at 4 kHz. 4-Hydroxytamoxifen (4OHT; Sigma) was dissolved in ethanol at a concentration of 20 mg/mL and diluted with 9 volumes of corn oil (Sigma). The diluted 4OHT (200 μL per mouse) was intraperitoneally injected into mice at P6. Under deep anesthesia, the mice were fixed by cardiac perfusion with 0.1 m sodium phosphate buffer (PB), pH 7.4, containing 4% paraformaldehyde (4% PFA/PB); the cerebellum was then removed and SCH727965 datasheet soaked in 4% PFA/PB for 4–24 h. After rinsing the specimens with PBS, parasagittal slices (50–100 μm thick) were prepared using a microslicer (DTK-2000; Dosaka, Kyoto, Japan) and subjected to immunohistochemical staining with the following antibodies: guinea pig anti-calbindin (1 mg/mL; Nakagawa et al., 1998), rabbit anti-calbindin (1 : 500; Millipore, Bedford, MA, USA), mouse anti-NF-H (1 : 1000;

Covance, Berkeley, CA, USA), guinea pig anti-glial fibrillary acidic protein (GFAP; 1 mg/mL, provided by Dr Watanabe at Hokkaido University), guinea pig anti-vesicular glutamate transporter VGluT1 (1 μg/mL; Miyazaki et al., 2003), mouse anti-HA (1 : 500; Covance) and goat anti-RORα (1 : 500; Santa Cruz Biotechnology, Santa Cruz, CA, USA). PD0332991 clinical trial Sections were permeabilized with 0.1 or 0.2% Triton X-100 in PBS, blocked with 10% donkey serum in PBS, and incubated overnight with primary antibodies followed by 1–2 h of incubation

with Alexa Fluor- (Invitrogen, Carlsbad, CA, USA) or DyLight- (Jackson Immunoresearch Laboratory, West Grove, PA, USA) conjugated secondary antibodies. For fluorescence Nissl staining, the sections were incubated with NeuroTrace Red (1 : 100; Invitrogen) for 1 h. The stained slices were viewed using a confocal laser-scanning microscope (Fluoview; Olympus, Tokyo, Japan or LSM710; Carl Zeiss, Göttingen, Germany). To determine the cell-type specificity, parasagittal slices of cerebellar vermis (50 or 100 μm thick) were immunostained for calbindin, and the numbers of EGFP-positive cells that were calbindin-immunopositive or -immunonegative in the cerebellum were counted. Statistical significance was defined by the χ2 test with Bonferroni correction. To separate the emission fluorescence of Mito-ECFP, EGFP-β-actin and Carnitine palmitoyltransferase II DsRed2, z-stack images of spectral data were obtained from a cerebellar slice by confocal microscopy (LSM710; Carl Zeiss). The images were processed by a linear unmixing algorithm (Zimmermann et al., 2003) to generate three-fluorescence images. The reference spectral data were obtained from human embryonic kidney 293 cells expressing only one of the three fluorescent proteins (Mito-ECFP, EGFP-β-actin and DsRed2). To study the effect of RORα1DN-HA on Purkinje cell development, parasagittal slices of cerebellar vermis (100 μm thick) were immunostained for calbindin and HA.

aureus controls its biofilm so as to discover novel compounds capable of find more inhibiting or dispersing biofilms without allowing bacteria to develop drug resistance. The diverse mechanisms that have been reported for biofilm control in S. aureus include quorum sensing, protease, DNase, cis-2-decenoic acid, d-amino acids, phenol-soluble polypeptides, several

surface proteins, and pH change (Boles & Horswill, 2011). Particularly, the activation of agr quorum-sensing and protease treatment in S. aureus inhibited its own biofilm formation and dispersed the established biofilms (Vuong et al., 2000; Boles & Horswill, 2008). A serine Esp protease in Staphylococcus epidermidis inhibited S. aureus biofilm formation and nasal colonization (Iwase et al., 2010). However, the target of these agr controlled protease and the specific

target of Esp protease is not known (Boles & Horswill, 2008; Iwase et al., 2010). Recently, we have shown that various Actinomycetes strains produce a large I-BET-762 cost amount of protease that rapidly dispersed S. aureus biofilm (Park et al., 2012). In the present study, more diverse bacteria are used to screen for S. aureus biofilm reduction. We find that two Pseudomonas aeruginosa supernatants dispersed S. aureus biofilm and contained high protease activities. Another study goal is to identify a main antibiofilm component and a possible mechanism of protease-involved biofilm dispersal. Transcriptional analysis and phenotypic assays are conducted to confirm that S. aureus Ribonuclease T1 triggers its biofilm dispersal through the accelerated effect of protease activity. All experiments were conducted at 37 °C, and Luria-Bertani (LB) medium was used for culturing all strains (Table 1). Two S. aureus strains (ATCC 25923 and ATCC 6538) were obtained from the Korean Agricultural Culture Collection and used to reinforce our findings in two different strains. To identify a main antibiofilm protease, thirteen P. aeruginosa PAO1 transposon

mutants (Jacobs et al., 2003) were obtained from the University of Washington Genome Center (Supporting information, Table S1). To obtain culture supernatants, a fresh single colony of bacteria was inoculated and cultured in LB at 250 r.p.m. for 24 h. All bacterial supernatants were filtered with a 0.45 μm filter to completely remove any bacteria before further use. Fresh culture supernatants were used in every experiment. Crystal violet, casamino acid, succinic acid, calcium carbonate, sodium phosphate, ethanol, soluble starch, and potassium phosphate were of analytical grade. DNase I (Cat. 79254) was purchased from Qiagen (Valencia, CA), and RNase A (Cat. 12091021) was purchased from Life Technologies (Grand Island, NY). For the cell growth measurements, the optical density was measured at 600 nm using a spectrophotometer (UV-160, Shimadzu, Japan). Each experiment was performed with at least two independent cultures.