These differences did not reach statistical significance probably because of small number of patients in these groups. Short duration of levamisole therapy as compared with previous studies might be another contributing factor to the negative seroconversion in two patients in the levamisole group. In earlier studies, the seroconversion rate in haemodialysis patients 1 year after tetanus vaccination has been reported to range from 38% to 65%.[3,

4] However, in our study, only 33% and 25% of the patients in the placebo group developed protective levels of anti-tetanus IgG antibodies 1 and 6 months post-vaccination. Our patients were on low-flux haemodialyser. Low-flux haemodialysers cannot remove large this website molecules like β2-microglobuin[16] Accumulation of these molecules have been reported to be associated systemic toxicity and worsened outcomes like all-cause mortality and death check details from infectious causes.[16, 17] Therefore, being dialysed with low-flux dialyser may be one of the contributing factors to the observed lower rate of seroconversion in our placebo group. In agreement with previous studies,[6, 8-10] our results show that levamisole supplementation could

result in mild and reversible adverse effects like leukopenia and gastrointestinal symptoms in haemodialysis patients. However, levamisole supplementation generally appears to be safe and without major side effects. In conclusion, our study shows that levamisole supplementation could effectively enhance the response rate to tetanus vaccination in haemodialysis patients without having any major side effects. Further studies with larger sample sizes and longer durations of follow-up are needed to better evaluate the enhancing effects of levamisole on tetanus vaccination and also on other vaccines in haemodialysis patients. This trial is registered with Clinicaltrial.gov, number NCT00705692. This trial was funded by a grant from Shiraz University of Medical

Sciences. The authors have no conflict of interest Thalidomide to declare. “
“Aims:  Prohibitin (PHB), a ubiquitous protein, is involved in a variety of molecular functions. Renal interstitial fibrosis (RIF) is a hallmark of common progressive chronic diseases that lead to renal failure. This study was performed to investigate whether PHB was associated with Caspase-3 expression/cell apoptosis in RIF rats. Methods:  Twenty-four male Wistar rats were randomly divided into two groups: sham operation group (SHO) and model group subjected to unilateral ureteral obstruction (GU), n = 12, respectively. The model was established by left ureteral ligation. Renal tissues were collected at 14 days and 28 days after surgery.

Published protocols for expanding CD4+ regulatory T cells ex vivo rely on repetitive stimulation

via the TCR in combination with cytokine exposure.26–28 Within the CD8+ regulatory T-cell subset, adaptive CD8+ regulatory T cells are by far the most dominant group. These cells can be induced by stimulation through the T-cell receptor under certain conditions resulting in a variety of different phenotypes. Recently, it was demonstrated that MLN0128 CD8+ CD25+ Foxp3+ regulatory T cells can be generated by the treatment with anti-CD3 antibody.29,30 In addition, another population of human CD8+ CD25+ Foxp3+ regulatory T cells has been described by Siegmund et al.31 Here, TGF-β and CD3/CD28 antibodies were required to expand these cells. For the CD4+ T-cell subset it was shown that TGF-β-induced conversion of CD4+ T cells into the Foxp3+ phenotype by gut-associated DCs is augmented by the key metabolite of Vitamin A, RA, in vitro.32,33 Ideally, if unwanted uncontrolled immunosuppression is to be avoided, regulatory T cells should be manipulated to express homing molecules that direct them to the tissue of interest. Most interesting in this

context is the observation that the RA is synthesized in abundance by gut and gut-associated DCs21,32,33 and induces the specific gut-homing molecules CCR9 and α4β7 integrin on T cells.21 Therefore RA seems to play a predominant role in the homeostasis and homing of lymphoid populations IWR-1 molecular weight of the gut-associated lymphoid Vasopressin Receptor tissue (GALT). The important role of RA in controlling Foxp3 expression in combination with TGF-β suggests that the

GALT has evolved a specific system for maintaining a balanced symbiosis between the gut flora and the immune system.18,32–34 Intriguingly, in the current study we could demonstrate that the potential of TGF-β and RA to convert naive CD4+ T cells into Foxp3+ T cells is also true for both murine and human CD8+ T cells. Our work has shown that treating naive CD8+ T cells with TGF-β and RA induces murine and human CD8+ Foxp3+ T cells with suppressive activity. Although these CD8+ Foxp3+ T cells possess proliferative capability they exhibit a phenotype that is strikingly similar to that of naturally occurring CD4+ Foxp3+ regulatory T cells and TGF-β/RA-induced CD4+ regulatory T cells. Most notably, they specifically express higher levels of CD25, Gpr83 and CTLA-4 than do CD8+ Foxp3− T cells activated in vitro. In vitro and in vivo experimental systems investigating polyclonal populations of CD8+ regulatory T cells have assumed the existence of separate subsets of CD8+ regulatory T cells on the basis of several apparently distinct mechanisms of immune regulation.

Suboptimal clinical outcomes are likely to correlate with poor graft survival and function. As suggested by the analysis of post-mortem transplanted brain tissue, various disease-related factors acting in concert may have provided an inhospitable milieu for the grafted tissue, namely (1) an excitotoxic effect exacerbated by the host cortical projections neurones onto the grafted tissue and (2) an impaired uptake of the glutamate excess by astrocytes; (3) poor graft–host interaction; (4) a significant microglial response cuffing check details the grafts; (5) the lack of neurotrophic support; and finally (6) the paucity of blood vessels within the graft (Figure 1). Taken together,

the latter evidence suggests that the negative impact of the pathological environment on graft

survival exceeds any benefit that might be gained from the graft against the disease. Huntington’s disease brains are characterized by abnormal levels of glutamate, especially in the striatum [57] and the impairment of glutamate PD-0332991 cost reuptake mechanisms may play a significant role in striatal neuronal degeneration [58,59]. Synaptic contacts are known to form between glutamatergic axon varicosities and grafted cells, as confirmed both by immunohistochemistry and electron microscopy. Within the graft, these contacts are more abundant onto striatal projection neurones which normally receive cortical glutamatergic innervation [43] (Figure 1). We also observed that the grafts are strikingly more affected by pathological processes than the host striatum, notwithstanding the fact that the grafts are younger and genetically unrelated to the HD patient and that they have been exposed to the disease for only a decade. Instead of a positive influence of grafts on the cortex, the pathology affecting the cortex

appears to induce neuronal degeneration within the grafts [43]. Despite recent evidence supporting the latter hypothesis in animal studies [60], the functional significance of this interaction remains unknown. It is also possible that glutamate is not the sole agent of striatal excitotoxicity [61,62]. For instance, dopamine released by nigral dopaminergic projections might act concomitantly with glutamate to GABA Receptor generate oxidative stress and modulate glutamate release itself [63]. In fact, decortication or 6-hydrohydopamine lesioning of the substantia nigra in R6/2 mice, a model of HD, leads to behavioural improvements and significant increases in longevity. Animals also exhibit lower striatal glutamate concentrations, suggesting overall that the cortical and nigral pathways may act synergistically to induce excitotoxicity [60]. Astrocytes are key players in glutamate uptake and clearance, which takes place mainly via the gap junction [64].

Implementation was via 3 pathways: (1) self-completion by New patients; (2) nurse initiated for Review patients (scored and triaged by nurses); (3) dietitian initiated and scored for New and Review patients. Methods: (1) A nine month audit of SSQ distribution, scores, and the impact on dietetic review. (2) A survey

of nurse perceptions (n = 4) and confidence using SSQ, and workload implications. Results: 108 SSQs were distributed (20 self-completed; 45 nurse initiated; 43 dietitian initiated; mean eGFR 37.26 ± 12.87 (14–89); 52.8% male); 94 were returned (87% response rate). Sodium assessment preceded the dietetic consultation in 60% of cases, SCH772984 concentration releasing dietitian time to focus on counselling. 23% of patients scored <65 (low sodium diet) vs. 77% scored ≥65 (high sodium diet and need for dietitian intervention). Of the 43 dietitian initiated, a review appointment was not needed in 63% of cases. All nurses agreed they felt confident using/scoring the SSQ, and felt satisfied with their increased role. Nurses felt the MOC expanded their knowledge base, facilitated patient discussion on salt/fluid/blood

pressure, and extended their scope of practice, with minimal implications to workload. Conclusions: The new MOC, HCS assay incorporating the SSQ, improved efficiency of dietetic resources, positively impacted on patient care, and expanded nursing scope of practice which was perceived positively. 199 MEDICATION ADHERENCE, MEDICATION BELIEFS, Glycogen branching enzyme ILLNESS PERCEPTION, & HEALTH LITERACY IN FACILITY HAEMODIALYSIS

(HD) VS. HOME DIALYSIS PATIENTS S CURD1, D KUMAR1, S LEE1, K PIREVA1, O TAULE’ALO1, P TIAVALE1, A KAM2, J SUH3, T ASPDEN1, J KENNEDY1, M MARSHALL3 1School of Pharmacy, University of Auckland; 2Pharmacy, Counties Manukau Health, Auckland; 3Department of Renal Medicine, Counties Manukau Health, Auckland, New Zealand Aim: Characterise and contrast patient attitudes to medication and illness between those on facility HD vs. those on home dialysis. Background: Intervention strategies to improve the clinical trajectory of CKD must address self-management by targeting causal factors for poor adherence. Methods: Survey of a stratified (Māori vs. Pacific vs. Other) random sample of prevalent facility HD and home dialysis patients from a single centre to assess: (i) medication adherence (Morisky Medication Adherence Scale, MMAS-8, 8 adherent, 1 non-adherent); (ii) medication knowledge (Okuyan-McPherson Knowledge of Medication Scale, 8 excellent knowledge, 1 poor knowledge), illness perception (Brief Illness Perception Questionnaire, BIPQ, multi-domained including “affects substantially”, “lasts a long time”, control over illness, symptom burden, emotional burden), and 3 single item literacy screeners (≥3 indicates marginal literacy and <3 indicates adequate literacy).

Expression of cytokines including IL-6 and tumour necrosis factor-α (TNF-α)21 was increased. Interestingly, transcripts for IL-10, IL-13, interferon-γ (IFN-γ) and IL-12p35 were increased but no production at the protein level was detected.10,21 Furthermore, LPS stimulation did not induce a change in IL-4 gene expression.20 However, T cells that had been exposed to antigen-pulsed MoDCs produced protein

for both IL-4 and IFN-γ.6 In contrast to MoDCs, however, very little information is available on maturation and activation of isolated BDCs following stimulation with LPS. Following their activation and maturation, DCs are known to drive AZD2014 molecular weight T-cell proliferation and to modulate the immune response towards a Th1, Th2, Th17 or T regulatory type of response.1,2 As a result of the limitations of studying T-cell

proliferation in outbred species, most studies in pigs have used mixed lymphocyte reactions6,10,12 and few have used autologous cells.16,21,22 In the present study, both MoDCs and BDCs were isolated from vaccinated pigs and co-cultured with autologous T cells to assess the induction of antigen-specific T-cell activation. We found that both MoDCs and BDCs were equally able to induce T-cell proliferation. However, Ku 0059436 when stimulated with LPS, BDCs that were directly isolated from blood showed a greater increase in cytokine and chemokine expression, when compared with MoDCs. This study therefore provides further evidence that directly isolated BDCs represent an important cell population for studying DC biology in pigs. Further studies, however, are required to identify Acetophenone the specific role of pDCs within the BDC population. Eight-week-old Dutch Landrace pigs purchased from Saskatoon Prairie Swine Centre, University of Saskatchewan were used in this study. The goal of this study was to directly compare MoDCs with isolated BDCs both phenotypically and functionally. Phenotypically, DC morphology was examined by Giemsa staining

and the expression of cell surface markers was examined by flow cytometry. Functionally, endocytic ability was examined by flow cytometry, changes in transcript expression and the production of cytokines in response to stimulation with LPS were investigated using quantitative real-time polymerase chain reaction (qRT-PCR) and enzyme-linked immunsorbent assay (ELISA), respectively, and lastly for their ability to stimulate autologous T-cell proliferation, thymidine uptake assays were performed. Studies were performed as per the ethical guidelines of the University of Saskatchewan and the Canadian Council for Animal Care. Blood was collected by heart puncture using ethylenediaminetetraacetic acid (EDTA) -coated syringes and blood mononuclear cells were isolated using a 60% Ficoll-Paque™ Plus gradient (GE Healthcare, Uppsala, Sweden). Monocytes were isolated using magnetic beads [magnetic antibody cell sorting (MACS); Miltenyi Biotec, Auburn, CA] and human anti-CD14 (TÜK4) microbeads (Miltenyi Biotec).

An overall sensitivity of 10 pg DNA was determined. Negative results and no template controls were confirmed by a positive band for the internal amplification control QS. The specificity was tested with increasing amount of human DNA. No cross-reactivity was observed up to 90 ng of human DNA. Although the kit is exclusively intended for human in vitro diagnosis, DNA preparations from selected

pets and farm animals (Table 1) were tested at 2 ng. Faint cross-reactivity was only observed with PS-341 clinical trial DNA from cat although the size of the unspecific amplification products did not match the reference ladders. The robustness of the PCR was confirmed by varying the thermocycler (‘Material and

methods’) and the annealing temperatures of the PCR by ±2 °C. Mixtures of 10 pg RGFP966 fungal DNA and 300 ng human DNA were assembled and subjected to PCR 1 and 2. These experiments revealed clear pathogen-specific amplification products and no cross-reactivity with human DNA at the detection limit. In total, 253 patients treated at the Department of Dermatology (University Hospital Carl Gustav Carus, TU Dresden, Germany) and 10 healthy subjects were analysed from September 2011 to April 2012. The clinical diagnosis revealed 122 onychomycoses, 76 tinea peduum, 16 tinea manuum, 3 tinea inguinales, 21 tinea corporum et facies and 15 mucosal candidoses. According to these clinical manifestations, 122 nail clippings, 105 skin scrapings and 26 smears from mucosa and weeping skin lesions were collected and subjected to microscopy, microbial culture and multiplex PCR. The nail clippings from all healthy subjects were negative for the three diagnostic methods. These results were not included in the further calculations. Of the 253 patients, 87 (34.4%) were tested positive in microscopy, 80 (31.6%) in culture, 128 (50.6%) in culture or microscopy or both and 127 (50.2%) in PCR respectively. The compliance

find more between the technologies is shown in Table 3. 44.8% of microscopically positive samples showed positive results in culture whereas in 90.8% of these samples positive results were revealed by multiplex PCR. Positive cultures could be confirmed in 80.0% by multiplex PCR and in 48.8% by direct microscopic examination. The detected pathogens are listed in Table 4. Candida yeast were further differentiated by culture and metabolic tests into 28 C. parapsilosis, 12 C. albicans, 6 C. guilliermondii, 2 C. glabrata and 2 C. krusei. Mixed fungal infections were seen in 10 cultures. These included all Cryptococcus spp. and Trichosporum spp. isolates in combination with T. rubrum or Candida spp. respectively. A combined infection of T. rubrum and C. parapsilosis was observed in three cases. The performance of multiplex PCR 1 and 2 with clinical samples are exemplified in Fig. 2.

To address this question, we examined the role of CR3−/− and CR4−/− in experimental cerebral malaria (ECM). We found that both CR3−/− and CR4−/− mice were fully susceptible to ECM and developed disease comparable to wild-type mice. Our results indicate that CR3 and CR4 are not critical to the pathogenesis of ECM despite their role in elimination of complement-opsonized pathogens. These findings support recent studies indicating the importance of the terminal complement pathway and the membrane

attack complex in ECM pathogenesis. Of the complement C3 receptors, 3-deazaneplanocin A ic50 only the complement receptor 1 (CR1, CD35) has an established role in the pathophysiology of malaria. CR1 serves as a host erythrocyte receptor for Plasmodium falciparum through its binding to PfRh4 (1–3), and polymorphic variants of CR1 associate with susceptibility to, and/or resistance to, severe malaria and cerebral malaria Cetuximab concentration (CM) (reviewed in (4)). By contrast, the remaining complement C3 receptors, CR2, CR3 and CR4, have poorly defined roles in the development and progression of malaria infection and CM. Based on in vitro studies, C3dg, the ligand for CR2, is generated in

large amounts and deposited on red blood cells in an alternative pathway-specific mechanism in murine malaria infections (5). The relevance of this observation to human CM remains unclear, especially in the light of studies demonstrating that coupling of C3d to malaria antigens in murine vaccine studies does not provide enhanced immunogenicity (6–8). The remaining two receptors, CR3

and CR4, are well known for their role in the phagocytosis of iC3b-opsonized pathogens (reviewed in (9–11)). However, the contribution of CR3 and CR4 to parasite killing and/or clearance via phagocytosis in both human and murine uncomplicated malaria and in CM is not known. Complement receptor 3 (a.k.a., αMβ2, CD11b/CD18) and CR4 (a.k.a., αXβ2, CD11c/CD18) are members ioxilan of the β2-integrin family of adhesion molecules that play important roles in tissue-specific homing of leucocytes during inflammation, leucocyte activation in the immune response, and phagocytosis (12–14). Both receptors bind multiple ligands and are widely expressed on all leucocytes (15), including neutrophils and macrophages that aid in clearance of malaria parasites and dendritic cells, which process antigen after ingesting parasite-infected red blood cells. The extent to which CR3 and CR4 contribute to these essential immune functions during malaria has received little attention. Instead, CR3 and CR4 are primarily used as cell surface markers to distinguish between myeloid subsets or followed for changes in expression during the course of malaria infection (16–20). Treatment with anti-CR3 antibody reportedly had no effect on the course of experimental cerebral malaria (ECM) (21,22). However, technical limitations of blocking antibody experiments require cautious interpretation as many variables affect experimental outcome (e.g.

Short-lived plasmablasts express intermediate level of Blimp-1, whereas long-lived plasma cells express high amounts of Blimp-1 [19, 20]. Blimp-1 is universally required for the formation of competent plasma cells. Blimp-1-deficient mice fail to generate antibody-secreting cells [18, 20, 21], and ectopic

expression of Blimp-1 is sufficient to induce antibody-secreting cell differentiation [22]. Blimp-1 can efficiently shut down the B cell gene expression programme and promote the exit from the cell cycle by repressing mature B cell–associated transcription factor genes such as Pax5, CIITA, SpiB, c-Myc and genes important Sorafenib manufacturer for GC formation including Bcl6 and activation-induced cytidine deaminase (AID) [15, 23–25]. However, Blimp-1 is not only needed to drive the plasmacytic properties but is also required for the maintenance of long-lived plasma cells [26]. These findings led to the conclusion that Blimp-1 is a master regulator of the initiation of plasma cell differentiation. This concept,

however, is challenged by a parallel mouse model, where Blimp-1 gene is engineered to harbour a green fluorescent protein reporter gene [20]. This model was used to discover a subset of cells called preplasmablast that have downregulated the expression of a central B cell transcription factor Pax5 but not yet induced the expression of Blimp-1 [27]. This finding fits with other models, BAY 80-6946 mw where deletion of Pax5 Edoxaban gene in DT40 B cell line induced spontaneous plasma cell differentiation [8, 9] and inactivation of Pax5 in mature mouse B cells induces Blimp-1 expression [28]. Collectively

these findings suggest that Blimp-1 drives the differentiation of plasma cells, but the initiation of plasma cell differentiation precedes the induction of Blimp-1 and is caused by downregulation of B cell properties. IRF4 has a two-phase expression pattern during the B cell development. While it is expressed in immature B cells in the bone marrow, it is lost in proliferating GC centroblasts [29, 30]. However, its expression starts to gradually increase again in some centrocytes and plasmablasts and reaches its highest level in plasma cells [30, 31]. In addition to Blimp-1, IRF4 is generally required for plasma cell differentiation. IRF4-deficient mice lack plasma cells, their serum Ig levels are low and their B cells cannot form plasma cells in vitro [16, 32, 33]. IRF4 seems to act upstream of Blimp-1, as IRF4 can bind to Blimp-1 gene and B cells cannot express Blimp-1 in the absence of IRF4 [33]. Xbp1 is also necessary for effective plasma cell formation [17], but it cannot initiate the process in the absence of Blimp-1 [18]. Xbp1 is required for secretion of antibody in plasma cells [34]. Within the B cells, the expression of Xbp1 is suppressed by Pax5 [35] and its overexpression in B cells expands the protein secretory apparatus [34]. Xbp1 acts downstream of IRF4 and Blimp-1 [18, 32].

To exclude unspecific effects of the chitin particles, we included glass beads of comparable size or just PBS as controls.

Chitin did neither induce nor inhibit Th2 polarization under neutral or polarizing conditions, respectively (Fig. 1C). This result led us to conclude that reduced Th2-cell expansion in vivo is not due to a direct inhibitory effect of chitin on T cells. The reduced frequency of TCR-tg cells in lung and LN of OVA/chitin-treated mice (Fig. 1A and B) could be due to inefficient homing, impaired proliferation or reduced survival of transferred T cells. To address the possibility that chitin inhibits T-cell proliferation, we labeled total splenocytes from BALB/c mice with CFSE and stimulated them in vitro with anti-TCR/anti-CD28 in the presence or absence of chitin. Proliferation of CD4+ T cells was inhibited by 30–40% selleck in the presence of chitin (Fig. 2A and B). Next, we sought to determine whether the inhibitory function of chitin was mediated by binding of chitin to the mannose receptor which has previously been shown to

serve as chitin receptor 11. T cells were cultured in the presence of chitin and soluble mannan in order to block binding of chitin to the mannose receptor as described earlier 11. However, the inhibitory activity of chitin was not reduced in the presence of INCB018424 in vitro mannan and mannan alone did not inhibit T-cell proliferation (Fig. 2A and B). To further determine whether inhibition of T-cell proliferation can be induced by direct interaction of chitin with T cells, we stimulated purified and CFSE-labeled CD4+ T cells on anti-TCR/anti-CD28-coated plates in the presence or absence of chitin or glass. Chitin or glass had no influence on the efficiency of T-cell proliferation, suggesting that the inhibitory effect of chitin is mediated by an accessory cell

type (Fig. 2C). The accessory cell type that mediates chitin-induced inhibition of T-cell proliferation might be a macrophage population. Indeed, cocultures of macrophages and T cells revealed Atezolizumab order that chitin caused a strong inhibitory effect (Fig. 3A and B). We have previously shown that chitin upregulates expression of Arg1, an enzyme which is induced in macrophages by Stat6-mediated signaling from the IL-4 receptors and therefore served as marker to indicate differentiation into AAM 9, 23, 24. However, it has recently been shown that Arg1 can also be induced by TLR-mediated signaling in a Stat6-independent fashion 25. Therefore, other markers like the chitinase-like protein Ym1 or “found in inflammatory zone 1” (Fizz1)/“resistin-like molecule α” appear to be more specific for AAM 26.

MonoMac6 (1 × 106/ml) cells were incubated alone or with antibody to FcγRIIB (0·1 µg/ml) or irrelevant goat polyclonal IgG (0·1 µg/ml) in RPMI-1640 at 10% of FCS for 30 min at 4°C, or alone or with JNK inhibitor SP 600125 (0·5 µM) or p38 inhibitor SB 203580 (1 µM) in RPMI-1640 at 10% of FCS for 30 min at 37°C. After this the cells were stimulated with GXM (100 µg/ml) for 2 h. Cells were washed and incubated successively with lymphocytes (PBL) treated previously with PHA, as described Selleckchem CX-5461 above, at an effector : target ratio (E : T) = 10/1. The percentage of lymphocytes (PBL) undergoing

apoptosis was quantified after 24 h of incubation by staining with propidium iodide (PI) (50 µg/ml) (Sigma-Aldrich). The PI analysis was performed because, unlike annexin V, which detects the early stages of apoptosis [24], it measures total apoptosis rate [25]. Briefly, cells were centrifuged, resuspended in hypotonic PI solution and kept for 1 h at room temperature. Apoptosis was evaluated as described previously [26]. Data are reported as the mean ± standard error of the mean (s.e.m.) from three to seven replicate experiments. Data were evaluated by one-way analysis of variance (anova). Post-hoc comparisons were made with Bonferroni’s test. A value of P < 0·05 was considered significant. We have demonstrated previously that GXM elicits a potent increase in cell surface FasL expression in macrophages,

and this effect was achieved by increasing the FasL synthesis [12]. Selleckchem RAD001 GXM is recognized by several surface receptors including TLR-4, CD14 and CD18, as well as FcγRIIB [15]. Indeed, FcγRIIB is responsible for 70% of macrophage uptake. As a consequence, the possible role of FcγRIIB in GXM-mediated FasL up-regulation was assessed. In a first series of experiments,

MonoMac6 cells were treated for 30 min at SPTLC1 4°C with antibody to FcγRIIB and then incubated with 100 µg/ml of GXM for 2 h at 37°C. This was the concentration found in the serum and cerebrospinal fluid of a group of cryptococcosis patients [27]. FasL expression was measured by cytofluorimetric analysis. The results (Fig. 1) show that, as expected, GXM induced up-regulation of FasL. A significant (P < 0·05) reduction in FasL expression, evidenced as the percentage of FasL-positive cells, was produced by blocking FcγRIIB (Fig. 1a). Furthermore, a significant (P < 0·05) reduction in FasL protein expression levels was also observed in Western blotting experiments (Fig. 1b). It has been reported that p38 MAPK and JNK may be involved in the regulation of FasL expression [28–30]. Therefore, MonoMac6 cells were incubated for 30 min at 37°C both in the presence and absence of SP 600125, a specific inhibitor of JNK catalytic activity [31], or SB 203580, a specific inhibitor of p38 catalytic activity [32], then GXM was added to the cells for 2 h.