Despite his uneventful clinical course, protocol biopsy at 2 years post transplant showed de novo CNI tubulotoxicity despite low tacrolimus exposure. Everolimus was added in order to discontinue TACER. However, prominent proteinuria impeded continuation of everolimus since biopsy showed diffuse glomerular endocapillary proliferation without C4d deposition. No Hormones antagonist donor-specific antibody was detected. Pulse

steroids were given and proteinuria returned to normal with histological reversal. Mammalian target of rapamycin inhibitors (mTORi) have been employed to reduce exposure to calcineurin inhibitors (CNI) and their toxicity in order to improve long-term graft outcome of kidney transplant recipients. The CNI-sparing regimen with everolimus (EVR) has been shown to have non-inferior graft function to the standard regimen,[1] and CNI-avoidance by switching cyclosporine

to EVR has also been shown to improve glomerular filtration rate (GFR) although a higher incidence of acute rejection was observed.[2, 3] EVR use has been associated with proteinuria,[1] and its impact with a dose-dependent manner has recently been shown as well.[4] A kidney transplant recipient who showed de novo proteinuria with evidence of glomerular injury in graft biopsy after EVR induction is presented. A 68-year-old man underwent living-unrelated kidney transplantation from his spousal donor. He had been on maintenance haemodialysis for 4 years due to end-stage renal disease click here after heminephrectomy for urothelial cancer with diabetic nephropathy. His donor was ABO-matched and both flow T- and B-cell cross-match were negative. A flow-bead analysis showed no anti-human leukocyte antigen antibody. He was under anti-platelet therapy after percutaneous stenting of coronary artery stenosis. Induction immunosuppression was a steroid-sparing regimen, consisting of extended-release tacrolimus (TACER), mycophenolate mofetil (MMF), basiliximab and 3 days of bolus steroid. His early course was uneventful. Graft function had been stable and no significant proteinuria was observed up to 2 years

post transplant. Protocol biopsies at 3 weeks, 3 months, 6 months and 1 year posttransplant showed no significant findings except for carry-over arteriosclerotic lesions. At 2 years posttransplant, estimated glomerular filtration rate (eGFR) was 31 mL/min, 24 hour collected urine protein was 90 mg/day, TACER trough Resminostat level was 2.9 ng/mL and the 24 hour area-under-the-concentration-curve (AUC0–24) was 95 ng·h/mL and mycophenolic acid-AUC0–12 was 48.7 μg·h/mL (with MMF 250 mg BID). A protocol biopsy at 2 years post transplant showed de novo CNI tubulotoxicity despite low tacrolimus exposure. We therefore decided to add EVR in order to discontinue TACER. Firstly, EVR was begun at a dose of 0.5 mg/day, resulting in low exposure and was increased to 1.5 mg/day with EVR trough levels of 3.0–4.5 ng/mL. Three months after adding EVR, urine protein increased. Then we further increased the dose of EVR to 2.

The complexes formed were visualized after a chemiluminescence reaction (ECL; GE Healthcare, Little Chalfont, UK). The intensity of the respective band was semi-quantified by Image J (version 1·42; http://rsb.info.nih.gov/ij). Eight patients fulfilling the 1982 American College of Rheumatology (ACR) revised criteria for the classification of SLE [26], nine patients fulfilling the 1987 ACR revised classification criteria for RA [27] and 14 healthy volunteers were recruited. selleck products The expression level of let-7i in T cells from these patients was measured by the methods

described above. Fresh isolated human T cells or Jurkat cells (1 × 106/ml) purchased from the American Type Culture Collection (Manassas, VA, USA) were electroporated with 1 μg of scrambled oligonucleotides, miRNA mimics (Ambion) or miRNA inhibitors (Ambion)

using the Gene Pulser MXcell electroporation system (Bio-Rad Laboratories, Hercules, CA, USA), with the conditions developed by Jordan et al. [28]. The expression of miRNA in miRNA-mimic or miRNA inhibitor transfected Jurkat cells was analysed after culturing for 24 h at 37°C in a humidified atmosphere containing 5% CO2. Because the endogenous TLR-4 protein expression in Jurkat cells is minimal, ionomycin (250 ng/ml; Sigma-Aldrich) and 10 ng/ml phorbol 12-myristate 13-acetate (PMA; Sigma-Aldrich) were added to activated Jurkat cells for another 24 h. These cells were then lysed by Western blotting for analysing Galeterone the expression of TLR-4. The expression levels of TLR-4 and IFN-γ mRNA were quantified selleck kinase inhibitor by real-time PCR using a one-step RT–PCR kit (TaKaRa, Shiga, Japan) on an ABI Prism 7500 Fast real-time PCR system (Applied Biosystems). The primers used for TLR-4 were 5′-CGAGGCTTTTCTGAGTCGTC-3′ (forward) and 5′-TGAGCAGTCGTGCTGGT- ATC-3′ (reverse). The primers used for IFN-γ were forward 5′-CTTTAAAGATGACCA- GACCATCCA-3′ and reverse 5′-ATCTCGTTTCTTTTTGTTGCTATTGA-3′. Conditions for the quantitative PCR were 42°C for 5 min and 95°C for

10 s for RT, followed by 40 cycles of 95°C for 5 s and 60°C for 34 s. Expression of 18S ribosomal RNA was used as endogenous control for data normalization. The normalized mRNA level was defined by the equation: 39 – Ct after normalization by the expression of 18S ribosomal RNA. T cells isolated from healthy volunteer or AS patients (1 × 106/well) were cultured in the following three conditions: (i) in culture medium only, (ii) in an anti-human CD3 antibody (1 μg; BioLegend, San Diego, CA, USA) precoated plate + 1 μg anti-human CD28 antibody (BioLegend) and (iii) in an anti-human CD3 antibody precoated plate + 1 μg anti-human CD28 antibody + 100 ng/ml lipopolysaccharide (LPS; Sigma-Aldrich) for 24 h at 37°C in a humidified atmosphere containing 5% CO2.

These two isoforms Panobinostat cost are related closely in structure, but functionally distinct. In the present study we used a specific blocking antibody to FcγRIIB. Moreover, in the present study a different dose of GXM (100 µg/ml versus 50 µg/ml),

different types of cells (MonoMac6 cell line versus monocyte-derived macrophages) and different incubation times (2 h versus 2 days) were used. Our previous observations indicated that active SHIP, in cells treated with GXM, was responsible for reduction of NFκB transcriptional activation and negative regulation of inflammatory cytokines. This effect was mediated via GXM/FcγRIIB interaction [17]. The role of SHIP in FasL up-regulation and in GXM-induced apoptosis remains obscure, but we can assume that in our system SHIP activation induced by FcγRIIB engagement plays a direct role in apoptosis induction. Consistent with this hypothesis, early studies Kinase Inhibitor Library ic50 have shown a pro-apoptotic role of SHIP1 in several cell types, including B cells, myeloid and erythroid cells [44–46]. Moreover, Liu et al. have

reported that myeloid cells from SHIP−/− mice are less susceptible to programmed cell death induced by various apoptotic stimuli via Akt activation [45]. In addition, a substantial amount of literature provides evidence that SHIP1 is required to inhibit Akt activation [45,47–49]. This inhibition is critical for the activation of JNK [50]. Akt negatively regulates apoptosis signal-regulating kinase 1 (ASK1), which activates JNK and p38 transcriptional events [51], therefore inhibition of Akt could lead to ASK activation with consequent phosphorylation of downstream signalling molecules such as JNK and p38. In this study we demonstrated that GXM induces up-regulation of FasL expression by JNK or p38 signalling, which activate c-Jun independently of each other. In particular, 3-oxoacyl-(acyl-carrier-protein) reductase JNK activation seems to be a consequence of GXM interaction with FcγRIIB, whereas p38 activation is also triggered by the binding of GXM with different

pattern recognition receptors (PRRs). However, the capacity of GXM to engage multiple PRRs, such as TLR-4 and FcgRIIB, which simultaneously transmit activating and inhibitory signals, might justify the high level of complexity of these signalling networks. Indeed, more studies are necessary to unravel the complexity of the GXM-induced signalling pathways. A schematic representation of the proposed pathway is shown in Fig. 8. Collectively, our results highlight a fast track to FasL up-regulation via FcγRIIB, and provide evidence for a mechanism involved in the activation of JNK, p38 and c-Jun. Moreover, the present study amplifies the spectrum of FcγRIIB-mediated effects, indicating that this receptor plays a critical role in transducing multiple signallings which contribute to inducing suppressive effects on innate and adaptive immunity.

tb both induced T cells specific for the known epitope residing in TB10.4-P8 27, whereas P3 and P7 were

the main epitopes recognized following TB10.4 vaccination, in agreement with an earlier study (Fig. 1 and 215). Interestingly, although TB10.4 as a subunit vaccine does not induce T cells specific for the major CD4 epitope induced by infection (P8), TB10.4 has been shown to protect CB6F1 mice against an infection with virulent M.tb. This indicates that an M.tb infection does lead to some intracellular processing and presentation of P3 and/or P7 despite the low numbers of infection-driven P3- and P7-specific T cells. It also indicates that vaccines may not have to induce responses against dominant infection-driven T-cell epitopes in order to be protective. This may be important for future vaccine design as discussed below in the concluding remarks of the Discussion PCI-32765 section. It has been demonstrated that post-translational modifications and native folding of Ag can alter immunogenicity

of a protein and even mask or unmask certain epitopes Fostamatinib purchase in an Ag compared with the recombinant version of the same antigen 29, 30. However, we found that immunization with native TB10.4 did not alter the epitope pattern compared to immunization with recombinant TB10.4 produced in E. coli (Fig. 3). In addition, TB10.4 is believed to be co-transcribed and secreted from both BCG and M.tb in a complex with Rv0287 19, 20. Complex formation of the related Ag CFP10-ESAT-6 has been shown to alter the structure, stability and function of these Ag 31, and to reduce their immunogenicity 32, 33. However, we showed that immunizing

with the native complex TB10.4-Rv0287 induced recognition of the same epitopes recognized after immunization with monomer TB10.4 and induced a similar level of IFN-γ production (Fig. 4). Furthermore, it was shown that boosting BCG with TB10.4 led to recognition of the dominant epitopes induced by both BCG and TB10.4, suggesting Sinomenine that the different epitope patterns after TB10.4 and BCG immunization were not due to mutually exclusive dominance between epitopes. BCG and M.tb encode two TB10.4-homologues, TB10.3 and TB12.9 34. Possibly, BCG or M.tb could induce T cells specific for P8 in TB10.3/TB12.9, and not TB10.4. However, only TB10.4 was predicted by RANKPEP (http://bio.dfci.harvard.edu/RANKPEP) 35 to have an MHC-II (I-Ad)-restricted epitope within P8 for the b and d haplotype-restricted CB6F1 mice, suggesting that the P8-specific CD4+ T cells observed in our study recognized P8 from TB10.4. Both BCG and TB10.4/CAF01 vaccines were taken up by DC and macrophages, but TB10.4/CAF01 was targeted by DC to a higher degree than BCG in line with results from Korsholm et al. 7 (Fig. 4). On the other hand, BCG was taken up efficiently by granulocytic Ly6-G expressing neutrophils, in agreement with a recent study by Abadie et al. 5.

Classical pathway activation is important for tissue renovation, thus acting anti-inflammatory, while amplification of complement activation through the alternative pathway releases numerous potent proinflammatory mediators [38, 39] such as the anaphylatoxins C3a and C5a, which bind to anaphylatoxin receptors

Palbociclib clinical trial and are highly proinflammatory [39]. Accordingly, C5a has been associated with atherosclerotic plaque ruptures [40]. The terminal pathway leading to formation of the fluid-phase terminal C5b-9 complex (TCC) and membrane attack complex (MAC) induced progression of atherosclerosis in a mouse model [41]. Extracorporeal treatment is known to affect the complement system in the interface between biomaterial and blood [42, 43]. Fadul et al. [44] studied the effect of LDL apheresis from plasma in hoFH and detected a significant increase in C3a and

TCC after the plasma separation column and a decrease in the same readouts after LDL apheresis, suggesting adsorption to the apheresis column. Oda et al. [45] identified that complement factor D, the limiting factor of the alternative pathway, was removed in LDL apheresis in patients with see more renal failure and peripheral artery disease. Our group performed a study in heFH patients undergoing treatment with different LDL apheresis columns [46]. Blood samples were drawn before (baseline) and after apheresis. We noted a diverse pattern with increase in C3a, C3bBbP and TCC after apheresis relative to baseline, while there was a decrease in C5a. When considering complement activation or adsorption of complement components in LDL apheresis, it should be kept in mind that widely used anticoagulants such as heparin and calcium binding agents affect the complement system while lepirudin

does not [47]. Thus, we then set up an ex vivo whole blood model with lepirudin for LDL apheresis mapping positions (i.e. before and after columns) and time frame during apheresis [48]. In this study, there was evidence that in plasma separation based mafosfamide systems complement was activated through the classical pathway (C1rs-C1inh complexes and C4d), and the plasma separation columns induced formation of C3a and C5a. The anaphylatoxins, however, were adsorbed by the apheresis columns, demonstrating strikingly different properties of the columns. These data are in accordance with Kobyashi et al. [49], who also demonstrated adsorption of C3a and C5a in an ex vivo model. Dihazi et al. [50] performed proteomic analyses on different LDL apheresis columns to investigate what types of proteins where adsorbed in different LDL apheresis columns. They detected ficolin adsorption, suggesting lectin pathway activation, for one of the three tested columns, while all the tested columns removed C3, C4 and complement factor H.

1); that is, HS type 1 (25 of 41 cases, 61%) is equivalent to “classical”

Ammon’s horn sclerosis[9] in which neuronal loss and gliosis is the most severe in CA1, followed by CA3, CA4, with relative sparing of CA2 and often associated with loss of dentate granule cells and/or dispersion. HS type 2 represents neuronal loss and gliosis almost confined to CA1 (CA1 sclerosis), and only one case (2%) was identified in our study. HS type 3 (7 cases, 17%) is characterized by a reverse distribution of the sclerotic lesion to HS type 1, in which neuronal loss and gliosis is the most severe in CA4 followed by CA3, with relative sparing of CA2 and CA1, that is equivalent to EFS.[10] In addition to these three HS types, we also identified eight cases (19%) without mTOR inhibitor apparent neuronal loss and gliosis (no HS). The selleckchem subiculum was relatively well preserved in all cases. Our study also confirmed HS type 1 to be the most frequent pathology in mTLE. Strictly speaking, precise borders between each hippocampal

subfields/sectors (CA1∼4) and CA1/prosubiculum border are not determinable without Golgi staining in specimens from healthy individuals,[8] and each border is still unclear even in specimens from patients with mTLE showing segmental neuronal loss. However, since recognition of the Phospholipase D1 distribution and severity of neuronal loss (lesion patterns) by visual inspection of KB-stained and/or NeuN-immunostained sections

(Fig. 2) seems easy and practical for many pathologists to assess histological changes and make diagnoses, a clinicopathological correlation study based on such a qualitative and simplified histological classification will also be waranted. The term “hippocampal sclerosis” has been used for the neuropathological substrate not only for mTLE but also for dementia in the elderly clinically characterized by severe amnesia and slowly progressive dementia without clinical seizure activity, and which is difficult to distinguish clinically from Alzheimer’s disease.[22, 23] In this review article, the authors use the term “dementia with hippocampal sclerosis (d-HS)” after the term “mTLE-HS” for “mesial temporal lobe epilepsy with hippocampal sclerosis”. Histological feature of d-HS may be observed in a given autopsy brain without significant other pathology (2–4%), but it is frequently found in combination with other dementing illnesses, including vascular and neurodegenerative disorders (12–20% of cases).[24] Among 382 autopsy cases with dementia from the State of Florida Brain Bank, d-HS constituted 13%, and 66% of d-HS cases had concomitant Alzheimer’s disease.

64 Amongst these cytokines, IL-6, IL-21 and IL-23 all signal through STAT3, and not surprisingly, STAT3 is essential for Th17 development. Indeed, disrupted STAT3 expression in T cells blocks Th17 differentiation,65 and confers resistance to experimental autoimmune selleck chemicals encephalomyelitis (EAE) and colitis.66,67 STAT3 controls the expression

of several key Th17 genes such as il17a, il17f, rora, il6r and il2167–69 but also promotes RORγt while repressing Foxp3 expression,65 so STAT3 is key at all stages of Th17 commitment (Fig. 4). Interestingly, the activation of STAT5 by IL-2 is required for optimal differentiation of Th1, Th2 and Foxp3+ Treg cells, but inhibits the development of Th17 cells.70 Indeed, STAT5 binds several sites on the il17 promoter and directly antagonizes STAT3 transcriptional activity,71 showing that STAT3 and STAT5 exert polar opposite effects on IL-17 expression in the context of Th17 differentiation (Fig. 4). This suggests that STAT5 is an essential regulator of CD4+ T-cell plasticity because IL-2 promotes Th1 and Th2 responses, whereas the absence of IL-2 favours the emergence of Th17 cells, as summarized in Table 1. The SOCS3 protein is a well known inhibitor of STAT3 activation in various cell types, and in particular inhibits IL-6 and IL-23 signalling in CD4+ T cells60–62 (Fig. 4). As might have been expected, SOCS3 deletion in T cells favours IL-17

secretion in vitro62 and in vivo,72 whereas enforced expression of SOCS3 PI3K activation inhibits polarization towards Th17 and delays the onset

of EAE.61 Moreover, mutation of the SOCS3 binding site on gp130 results in increased IL-17 secretion60 and spontaneous arthritis.73 Finally, it has been proposed that TGF-β inhibits SOCS3 expression, and subsequently prolongs STAT3 activation, which perhaps explains how TGF-β enhances Th17 differentiation.74 Therefore, SOCS3 clearly inhibits the development of Th17 cells, but SOCS1 and SOCS2 appear to have the opposite effect. Indeed, disruption of SOCS1 expression in T cells strongly inhibits Th17 differentiation and diminishes disease in EAE models.61 This is associated with increased IFN-γ-mediated STAT1 activation, enhanced SOCS3 levels, attenuated STAT3 phosphorylation and reduced TGF-β transcriptional activity. These observations indicate that SOCS1 Oxymatrine promotes Th17 differentiation possibly by modulating TGF-β signalling, but also indirectly by preventing Th1 lineage polarization and by regulating SOCS3 levels. Interestingly, SOCS2-deficient CD4+ T cells also have impaired IL-17 secretion, consistent with reduced STAT3 activation and elevated SOCS3 levels.59 Therefore the positive effect of SOCS1 and SOCS2 on Th17 differentiation might well be simply the consequence of increased SOCS3 levels, which confirms that the regulation of STAT3 activation by SOCS3 is an essential mechanism to limit Th17 development.

p-values below 0.05 were considered significant. The authors want to thank all the subjects who volunteered to participate in this study. The work of Zuyen Gonzáles, selleckchem Esperanza Hechevarría, and Belkys Gómez collecting the blood samples is greatly acknowledged. The authors also want to thank Dr. Thomas

Rothstein and Dr. Daniel Griffin for critical reading of the manuscript. This work was supported by the Center of Molecular Immunology. The authors declare no financial or commercial conflict of interest. As a service to our authors and readers, this journal provides supporting information supplied by the authors. Such materials are peer reviewed and may be re-organized for online delivery, but are not copy-edited or typeset.

Technical support issues arising from supporting information (other than missing files) should be addressed to the authors. Figure S1. Level of anti-NeuGcGM3 antibodies in male and female healthy humans is similar. Figure S2. Total amount of IgM and IgG in healthy donors’ sera does not change with age. Figure S3. Presence of NeuGcGM3 on L1210 Buparlisib chemical structure cells. Figure S4. Healthy humans’ sera induced complement mediated cell death to NeuGcGM3 expressing tumor cells. Figure S5. Induced complement independent cell death positively correlates with both the levels of anti-NeuGcGM3 antibodies and tumor cell binding. Figure S6. Incubation of L1210 cells with cytotoxic healthy humans’ sera did not induce caspase 3 activation. Figure S7. Anti-NeuGcGM3 Abs obtained from NSCLC patients demonstrate specific binding. “
“Bacterial

meningitis is, despite progress in research and the development of new treatment strategies, still a cause of severe neuronal sequelae. The brain is protected from penetrating pathogens by both the blood–brain barrier 5FU and the innate immune system. The invading pathogens are recognized by pattern recognition receptors including the G-protein coupled formyl peptide receptors (FPRs), which are expressed by immune cells of the central nervous system. The expression of FPRs is up-regulated during bacterial meningitis, but the consequence on the progression of inflammation and impact on mortality are far from clear. Therefore, we used mFPR1 and mFPR2-deficient mice to investigate the effects on inflammation, bacterial growth and mortality in a mouse model of pneumococcal meningitis. Our results revealed increased bacterial burden, increased neutrophil infiltration and higher mortality in mFPR1/2-deficient mice in comparison to wild-type mice. The mFPR1- or mFPR2-deficient mice also showed significantly increased glial cell density, whereas the immune responses including the expression of anti-inflammatory cytokines and antimicrobial peptides were decreased in bacterial meningitis.

PARK JI HYEON, PARK KYUNG SUN, JANG HYE RYOUN, LEE JUNG EUN, HUH WOOSEONG, KIM YOON-GOO, OH HA YOUNG, KIM DAE JOONG Division of Nephrology, Department of Internal Medicine, Samsung Medical center, Sungkyunkwan University School of Medicine, Seoul, Republic of Korea Introduction: Living-unrelated donors (LURD) have been widely INK 128 price used for kidney transplantation (KT). We compared clinical outcomes of

KT from LURD and from concurrent living-related donors (LRD), and identified risk factors associated with acute rejection, graft and patient survival in living KT. Methods: We retrospectively reviewed 779 patients who underwent living donor KT (264 from LURD, 515 from LRD) at Samsung Medical Center from January 2000 to December 2012. Results: Median follow-up was 67 months. Mean age (43.2 vs. selleck screening library 38.4 years, P < 0.001), mean number of total HLA mismatches (4.1 vs. 2.5, P < 0.001) and HLA-DR mismatches (1.2 vs. 0.8, P < 0.001) were higher, and mean estimated glomerular filtration rate (eGFR) was lower (87.6 vs. 90.9 ml/min, P = 0.007) in LURD. Acute rejection-free survival (64.9% vs. 72.7% at 5 years, P = 0.018) and graft survival (92.9% vs. 96.5% at 5 years, P = 0.025) were lower for LURD than LRD whereas patient survival rate was comparable (97.9% vs. 98.7% at 5 years, P = 0.957). Cox-regression analysis showed that HLA-DR mismatches (OR 1.77, 95% CI 1.20–2.62, P = 0.004

for 1 mismatches; OR 2.63, 95% CI 1.64–4.20, P. Conclusion: Our data suggest that HLA-DR mismatches and donor eGFR are independent risk

factors for clinical outcomes of living KT. In living KT, these factors should be considered to prevent acute rejection and improve graft survival. ADACHI HIROKI, MUKAI KIYOTAKA, OKUSHI YUKI, OKINO KAZUAKI, SHOJIMA KIYO, MATSUI YUKI, FUJIMOTO KEIJI, ATSUMI HIROKATSU, OKUYAMA HIROSHI, YAMAYA HIDEKI, YOKOYAMA HITOSHI Division of Nephrology, Kanazawa Medical University buy Etoposide School of Medicine Introduction: Although the risk for morbidity and mortality is studied in subjects with renal transplantation, there are very limited data to access the reno-protective effects of lipid and adiponectin. Methods: We studied 105 adult subjects (age 19- to 72-year old; 66 males, 21 cadaveric donors) between January 2004 and December 2012, with at least three years of allograft survival in our hospital. We examined clinical backgrounds, donor types (living or cadaver), treated drugs, blood pressure (BP, mmHg), body mass index (BMI), blood chemistry including cholesterol (total, LDL-C, HDL-C), glucose, glycated hemoglobin (HbA1c), and total, high- and low-molecular adiponectin (ADPN) levels. Results: The initial 4 years alteration of eGFR was at −2.2(−14.3∼7.0) ml/min/1.73 m2/year in 105 subjects. In single analyses, both LDL-C/HDL-C ratio below 2.0 and statin treatment also decreased the reduction rate of eGFR at −1.4 and −1.0 ml/min/1.73 m2/year (p = 0.01, p = 0.02), respectively, but not by total ADPN levels.

Results: Higher baseline RRF was inversely associated with slope of

RRFD (β = −0.72; p < 0.001), phosphate levels (β = −0.18;p = 0.02), and Ca×P levels ((β = −0.18; p = 0.02) by simple linear regression tests. After adjusting for gender, GSI-IX nmr age, serum albumin level, baseline RRF and diabetes mellitus by multivariate lineal analyses, serum phosphate levels (β = −3.57; p < 0.001) rather than calcium levels (β = −0.09; p = 0.12) showed an inverse correlation to the slope of RRFD. Conclusion: After adjusting for baseline RRF, higher serum phosphate level was associated with rapid RRF decline in CAPD patients. CHAO MEI-CHEN, WU MEI-YING, PAI SHING-QUEI, KUO LI-CHUEH, LEE CHIEN-TE, CHEN JIN-BOR Division JNK inhibitor of Nephrology, Kaohsiung Chang Gung Memorial Hospital and Chang Gung University College of Medicine, Kaohsiung Introduction: Infection is one of factors to influence the outcome in long-term peritoneal dialysis (PD) patients. A good quality of exit site care is a key component to avoid infectious events in PD patients. Present study was to investigate

the efficacy of film dressing on the exit site and its influence on quality of life (QoL) in PD patients. Methods: The study design was prospective, open-label, parallel-control. The observation was one year. Eighty patients were enrolled in one PD center, the mean age 48.3 ± 12.6 year-old. The number of patients was forty in each group. The subjects in study group used film dressing on the exit site and changed dressing every two weeks in outpatient clinic. The subjects in control group

cared exit site according to regular guideline by PD nurses. The analyzed variables included infectious events and questionnaires pertaining QoL. Results: The infectious rate in exit site was 0.25 Selleckchem Y-27632 times / 100 patient month in study group vs 0.88 times/ 100 patient month in control group. Five patients had early withdrawn from the study group because of allergic reaction to dressing. In QoL analysis, there were higher score in satisfaction, stress reduction and psychological relaxation in study group than control group. Conclusion: An invention of film dressing on exit site had reached a favorable outcome in infectious control and QoL in PD patients. SEI YUMI1, MIZUNO MASASHI1, SUZUKI YASUHIRO1, IMAI MASASKI2, HIGASHIDE KEIKO1, SAKATA FUMIKO1, IGUCHI DAIKI1, OKADA NORIKO2, MATSUO SEIICHI1, ITO YASUHIKO1 1Nagoya Univeristy Graduate School of Medicine; 2Nagoya City Univeristy Graduate School of Medicine Introduction: Peritoneal dialysis (PD) therapy is one of the most important renal replacement therapies. Impairment of peritoneal function can limit the long-term efficacy of PD therapy. Peritoneal impairment is caused by several factors that occur during PD therapy, including exposure to peritoneal dialysate, catheter trauma and peritonitis.