Among various miRNA, miR-155 has been associated with the regulation of different immune-related processes, such as haematopoiesis,14 B-cell and T-cell differentiation,15 cancer16 and innate immunity.12 The miR-155 is processed from an exon of a non-coding RNA transcribed from the B-cell Integration Cluster located on chromosome 21, showing strong sequence homology AP24534 manufacturer among humans, mice and hens, and is highly expressed in cells of lymphoid and myeloid origin.17 Recently, miR-155 has been identified

and characterized as a component of macrophage and monocyte response to different types of inflammatory mediators, such as bacterial lipopolysaccharide (LPS), interferon-β (IFN-β), tumour necrosis factor-α (TNF-α) and polyriboinosinic-polyribocytidylic acid [poly(I:C)].12,18,19 Many of the miR-155 target transcripts identified so far are pro-apoptotic and anti-inflammatory proteins, such as the Fas-associated death domain protein, IκB kinase ε, inositol 5-phosphatase 1 and the suppressor of cytokine signalling-1 (SOCS-1). SOCS-1 belongs to a family www.selleckchem.com/products/pd-0332991-palbociclib-isethionate.html of proteins known to regulate the response

of immune cells to cytokines and other inflammatory stimuli, such as LPS, through direct inhibition of the Janus tyrosine kinase (JAK) and consequent inhibition of signal transducer and activator of transcription factors (STAT), as a ‘classical’ negative feedback loop. In addition, the C-terminal SOCS box domain interacts with components of the ubiquitin ligase system and mediates proteasomal degradation of associated proteins, including key elements of other pro-inflammatory pathways, such as the nuclear

factor-κB and Jun N-terminal kinase pathways. Experimental evidence suggests that miR-155 plays a pro-inflammatory role and may be implicated in chronic inflammatory processes, such as those Tryptophan synthase contributing to cancer and to certain neurodegenerative diseases. Given the similarities between microglia and other cells of the immune system, such as macrophages and dendritic cells, where miR-155 has been found to be up-regulated upon activation,20 in this work we investigated the contribution of miRNA-155 to microglia activation and microglia-mediated immune responses. To our knowledge, this is the first study providing evidence that miR-155 has a strong pro-inflammatory role during microglia activation and is required for SOCS-1 post-transcriptional regulation and progression of the immune response in these cells. Moreover, our results suggest that miR-155 inhibition induces neuronal protection from microglia-induced damage, and miR-155 may therefore constitute an interesting and promising target for the control of neuronal inflammation.

11–15 Cytokine release in subjects administered otelixizumab selleck products is significantly reduced compared with cytokine release in subjects administered OKT3, an Fc-intact monoclonal anti-CD3.13,14 In a Phase 2 trial conducted by the Belgian Diabetes Registry (BDR), subjects with new-onset type 1 diabetes who received a single

6-day course of otelixizumab (total dose 48–64 mg) had significantly greater endogenous insulin production than subjects who received placebo, and this effect was durable for at least 48 months.14,16 Preliminary clinical activity in new-onset type 1 diabetes has also been demonstrated with teplizumab, another Fc-modified monoclonal anti-CD3.17 Upon ABT 199 the administration of monoclonal anti-CD3, antibody rapidly binds the CD3 molecule and is internalized, resulting in modulation of the CD3–T-cell receptor (TCR) complex. Loss of CD3–TCR complex expression is reversible, as it recycles back to the surface after clearance of the antibody. Binding and subsequent modulation of the CD3–TCR complex by monoclonal anti-CD3 is

considered to be pharmacodynamically important and is routinely assessed in clinical studies evaluating monoclonal anti-CD3 therapies. This pharmacodynamic (PD) effect potentially impacts the mechanism of action of monoclonal anti-CD3 in at least two ways: (i) temporarily blocking antigen binding; and (ii) delivering a partial agonist signal, which may induce anergy of autoreactive T Oxymatrine cells while allowing for the expansion of Treg cells (reviewed in2,18). In the Phase 2 BDR study of otelixizumab, profound and sustained modulation of the CD3–TCR complex occurred

on the first day of dosing and persisted through the 6-day dosing period.14 In the mouse, there are limited data evaluating dose responses with monoclonal anti-mouse CD3 F(ab′)2 or examining modulation of the CD3–TCR complex during treatment and its potential correlation with efficacy. We performed dose-ranging studies in diabetic NOD mice to determine the minimum effective dose of monoclonal anti-CD3 F(ab′)2. CD3–TCR complex-modulation patterns elicited during antibody administration were assessed to determine whether nearly complete and sustained modulation is required for efficacy of monoclonal anti-CD3 therapy. We demonstrated that doses resulting in partial and transient modulation of the CD3–TCR complex are sufficient to induce remission in diabetic NOD mice, such that doses more than 30-fold less than the originally published 250 μg regimen resulted in similar rates of remission.

2b). C4d staining patterns remained the same. Anti-C5 antibody therapy was not available. DS had been doing very poorly on dialysis pre-transplant and was very keen to pursue all selleck products avenues of treatment. In this setting of severe, treatment refractory rejection a splenectomy was performed

and she was continued on plasma exchange. After some initial improvement, her creatinine continued to rise and a progress biopsy at 5 weeks was remarkable for cortical necrosis and interstitial haemorrhage (Fig. 2c). V3 was still present, as was severe tubulointerstitial inflammation (i3, t3). Mild tubular atrophy was thought to be present but it was difficult to assess the amount of interstitial fibrosis. No transplant glomerulopathy was evident. Very focal, weak C4d positivity was noted in peritubular capillaries; arteriolar wall staining was again noted. Six weeks post transplant she developed P. mirablis line sepsis and repeat biopsy

showed ongoing rejection and more scarring than previously. Her creatinine had risen to 497 μmol/L and emergency dialysis was required for pulmonary oedema. In the setting of uncontrolled rejection on maximal treatment it was considered futile to continue and graft nephrectomy was performed on day 50 post transplant (Fig. 2d). Luminex at 4 weeks showed a new donor specific antibody (DSA) to DR 52 (MFI 1094) however when repeated in 2013 showed antibodies to each of the see more 5 mismatched antigens in the graft with MFI ranging between 8000–15 000. DNA was extracted and sent for analysis at the Immunology Laboratory, Hunter Area Pathology Service, Newcastle, Australia and analysed using a Fluidigm microchamber chip for the first round of nested PCR and sequencing using Massively Parrallel Sequencing (‘nextgen’) on Illumina Miseq. Variants in CD46/MCP, CFH and CFI were assessed using phenotype prediction models (SIFT, Polyphen2, Align, MutationTaster), publically available genome data (1000Genome Project), mutation registries and past publications. Likely pathogenic single nucleotide polymorphisms

were identified in CD46/MCP (104G>A, C35Y)) and CFH (3590T>C, V1197A). Further variants of uncertain though potential pathogenic significance were also found in both CD46/MCP (565T>G, T189D) and CFH Enzalutamide purchase (3226C>G, Q1076E; 3572C>T, S1191L). Further confirmatory testing is awaited. In summary, a DBD renal transplant for ESRD secondary to aHUS was performed. After good early graft function intractable ABMR developed that was unresponsive to aggressive therapy with high dose methyl prednisone, anti-thymocyte globulin and plasma exchange and resulted in rapid graft loss and transplant nephrectomy. Of note, at no stage were any haematological features of thrombotic microangiopathy demonstrable, with LDH and haptoglobin in the normal range and no significant thrombocytopenia or schistocytes present.

1) and has been demonstrated as a positive regulator for T-cell development and cell activation. SLP-76-deficient mice show a T-cell developmental block at the double-negative stage, whereas the SLP-76-deficient T-cell line shows impaired phosphorylation of phospholipase C-γ1 and defective Ras pathway activation.29–31 Importantly, SLP-76 has been implicated in the regulation of integrin adhesion in both Selleck SB203580 ‘inside-out’ signalling and ‘outside-in’ signalling in multiple cell types. SLP-76-deficient T cells could not adhere to integrin β1 ligand fibronectin after TCR stimulation via the ‘inside-out’ signalling. Further, in response to ligand-induced ‘outside-in’ signalling,

SLP-76-deficient platelets fail to spread on integrin β3 ligand fibrinogen-coated plates,32,33 and SLP-76-deficient neutrophils fail to spread and produce reactive oxygen intermediates after integrin ligand simulation.34 Interestingly, the upstream effectors LAT and Gads do not seem to play a role because

the Gads-binding domain of SLP-76 seems to be dispensable for platelet spreading on fibrinogen, and LAT-deficient platelets aggregate and spread normally in response to integrin stimulation in the ‘outside-in’ signalling.35 As a central click here scaffolding protein, SLP-76 is associated with a guanine-nucleotide exchange factor (GEF) Vav1 after being phosphorylated by ZAP-70 and SYK.36–38 Mannose-binding protein-associated serine protease Similar to the role of SLP-76, Vav1 mediates integrin β1 and β2 activation in T cells, neutrophils and platelets via both ‘inside-out’ and ‘outside-in’ pathways. Vav1-deficient cells are impaired in cell adhesion, spreading and production of reactive oxygen intermediates in response to integrin ligand stimulation in the ‘outside-in’ signalling.39–42 Also, Vav1 mediates TCR-induced integrin clustering and T–APC conjugate formation via ‘inside-out’ signalling.41 As a GEF, Vav1 activates the GTPase Rac1, which regulates adhesion by directly controlling the balance between actin-mediated protrusion and myosin II-mediated contraction

through interacting with the WASP/WAVE complex and activating the ARP2/3 complex (Fig. 1).43–45 Other GEFs including DOCK180 (dedicator of cytokinesis 180), DOCK8 also regulate integrin adhesion, which activate the GTPase Rac1 or Cdc42.46 Upon activation, SLP-76 also interacts with adhesion and degranulation promoting adaptor protein (ADAP) via its phosphorylated tyrosines.47 The SLP-76–ADAP interaction regulates integrin-initiated ‘outside-in’ signalling.48 Disruption in the interaction between SLP-76 and ADAP blocks T-cell spreading and migration in the ligand ICAM-1-coated surface.49,50 Similar to ‘outside-in’ signalling in other cells, the upstream LAT–Gads complex is not required for the SLP-76–ADAP module-induced ‘outside-in’ signalling in T cells.

In contrast, the viscosity of the spent click here culture medium obtained from ATCC33650 was similar to that of the control TSBY medium (Fig. 1a). SEM observations on the cell surfaces of these strains revealed that YS-11 had meshwork-like structures surrounding the cells (Fig. 1b), but

ATCC33650 lacked this phenotype (Fig. 1c). Chemical analyses showed that the isolated materials primarily consisted of neutral sugars, small amounts of uronic acid, and amino sugars, with mannose constituting 78.4% of the polysaccharides (Table 3). Lipopolysaccharide activity in the purified viscous materials was 0.33±0.08 EU mg−1. We constructed a mutant that lacked the ability to produce exopolysaccharide in the culture supernatant and to form meshwork-like structures around cell surfaces by random insertion of EZ-Tn5 Tnp to chromosomal DNA of YS-11. Among 486 colonies grown

on TSAY-Km, only one strain (strain 455) showed low viscosity in its culture medium as a control level (Fig. 2) and cell surfaces without meshwork-like structures (Fig. 3a). Southern hybridization indicated that strain 455 had an insertion of EZ-Tn5 Tnp (data not shown). Sequencing analysis by DNA walking showed that the transposon in strain 455 was inserted into an ORF that was highly homologus to wzt. This gene encodes the ATP-binding protein of the ABC transporter system in the O-antigen biosynthesis gene cluster of Y. enterocolitica serotype O:9 (Lubeck et al., 2003; Skurnik, 2003) (Fig. 4). The upper region of wzt ORF contains Erlotinib supplier homologues of Erwinia chrysanthemi manB (Touze et al., 2004), gmd, per, wzm of Aeromonas hydrophila (Seshadri et al., 2006) or Y. enterocolitica serotype O:9 (Lubeck et al., 2003; Skurnik, 2003), and wbcT of Y. enterocolitica serotype O:9 (Lubeck et al., 2003; Skurnik, 2003). The flanking regions of the transposon insertion are depicted in Fig. 4. To further investigate how wztYS-11 was involved in viscous material production,

we constructed a plasmid pWZT carrying the wztYS-11 ORF in which wzt was fused with the lacZα-peptide gene on the pSTV28 to complement the mutant strain lacking this phenotype. Plasmid pWZT was introduced into strain 455. The resultant recombinant, designated as strain L-gulonolactone oxidase 455-LM, was capable of producing extracellular materials of higher viscosity (Fig. 2) and cell surface-associated meshwork-like materials as revealed by SEM (Fig. 3b) than those of strain 455. IPTG induction augmented both the viscosity of the extracellular viscous material and the abundance of meshwork-like structures around cells (Figs 2 and 3c). Control strains, strains 455-pSTV28 and E. coli DH5α-pWZT, exhibited any changes of the above-described phenotypes (data not shown). The ability to induce abscess formation in mice by E.

resulted in seven clusters (data not shown). The nine blood isolates were distributed among six clusters. No correlation was observed between the clusters and the presence of any OXA-like gene type, biofilm forming ability or meropenem resistance. Though carbapenemase resistance among Acinetobacters spp. in India has been reported (9, 10), the genes involved and their association with ISAba1 have not been elucidated.

In this study, multiplex PCR was used to characterize the species and examine the prevalence of OXA-type genes. The blaOXA-51-like gene is intrinsic to A. baumannii and is chromosomal (22). The G+C content of OXA-51 closely matches that of the A. baumannii genome (39–40%) and has been used for the identification of this species. OXA-23 Topoisomerase inhibitor is encoded either chromosomally or in plasmids and has been found to have a global distribution, accounting for carbapenemase resistance in most clinical isolates of A. baumannii MI-503 (1). The results of Mendes et al. (23) and our study corroborate the above findings (Table 2). blaOXA-24-like gene, which has been reported for isolates from Europe, the USA (1) and Thailand, Indonesia and Taiwan in the Asia Pacific region (23) has not previously been recorded in Indian isolates. However, our results

for samples from India reveal the presence of this gene in both A. baumannii (22.9%) and other Acinetobacter spp. (64.3%), suggesting the possible acquisition of this gene from other sources. blaOXA-58-like genes have been reported from Europe, North and South America, and West Asia (1, 7).The low prevalence in India evident in our study is in agreement with the report of Mendes et al. (23). Resistance to meropenem according to MIC assay was 39.6% in A. baumannii and 14.2% in other Acinetobacter spp. (Table 2) which is higher than the reported resistance (25%) for Asia (1) and could be a reflection of the increasing use of meropenem in the clinical setting. The insertion sequence ISAba1 observed in 33.3% of the isolates presents sequence similarity to that reported previously

(18). The presence of ISAba1 upstream of blaOXA-23 gene is in accordance with earlier reports (1, 18) wherein the insertion sequence was generally associated with blaOXA-23 gene. Further, the presence of ISAba1 in A. baumannii only in our isolates (Fig. 2) confirms the earlier Ribonuclease T1 finding that this insertion sequence is unique to this species (1). The presence of ISAba1 in the promoter region has been thought to cause over-expression of genes (17). However, in our study, we identified some isolates that were resistant to meropenem, but did not have ISAba1 upstream of OXA genes, suggesting there may be other mechanisms of over-expression of these genes in such strains. Recent findings have suggested that over-expression of the naturally occurring blaOXA-51 gene is mediated by the novel insertion sequence ISAba9 (24) and the blaOXA-23 gene to ISAba4 (25), providing evidence for other mechanisms of resistance.

Virus-derived siRNAs (vsiRNAs) are generated in the host during infection by RNA viruses in both Drosophila Selumetinib mw and mosquitoes. The biogenesis of these vsiRNAs has been the focus of much research to discover the identity of the viral RNA precursor targeted, and to provide insight into how the RNAi pathway mechanistically responds to infection against distinct classes of viruses [1]. Figure 1A diagrams the potential RNA precursors of vsiRNAs generated during RNA virus infection, bearing in mind that these precursors must be in the form of dsRNA.

Small RNA sequencing of virus-infected cells or animals has revealed that the dsRNA replication intermediate of RNA viruses is a common target of the antiviral machinery [4, 7-9] (and Sabin and Cherry, unpublished observations). In addition, as RNA viruses have limited coding capacity, they often encode highly structured cis elements (structured viral RNA) with double-stranded character that direct transcription, replication, and packaging. Therefore, it is perhaps not surprising that the antiviral Cilomilast RNAi machinery is capable of targeting those regions with double-stranded character within the highly structured viral transcripts. Viruses such as Flock House virus, Drosophila C virus, and West Nile virus, appear

to expose such structures during infection; the majority from of the small RNAs generated during their replication derive from only the genomic RNA strand [10-12] (and Sabin and Cherry, unpublished observations). This suggests that double-stranded structures within single-stranded RNAs can be processed into siRNAs during infection. Genetic studies have indicated that robust antiviral RNAi requires not only vsiRNA biogenesis by Dicer-2, but also the action of the core siRNA RISC effector, Ago2; however, only a fraction of vsiRNAs are specifically bound to Ago2 in infected cells [13, 14] with a large proportion of vsiRNAs being stable, but not bound to Ago2. Whether the

“free” vsiRNAs are loaded onto another RISC, such as Ago1 RISC, which normally binds miRNAs, or whether the vsiRNAs are stabilized elsewhere remains unknown. Furthermore, while some reporters that bear viral RNA target sequences can be silenced by vsiRNAs produced during infection, this is not always the case [8, 13, 15]. Altogether, these findings raise questions regarding which vsiRNAs reflect the active pool for viral silencing, and whether viral sequences are indeed generally targeted by Ago2-RISC. Additional studies of the effector step of antiviral RNAi are necessary to resolve these issues. Since viruses co-evolve with their hosts, one hallmark of an important antiviral pathway is the development of robust countermeasures against the host-encoded antiviral immune factors by viruses.

At 6 months, the primary patency rate was 29% (12 patients) for angioplasty alone, and 75% (30 patients) for angioplasty with stenting. However, the proportion of patients

with cured or improved hypertension was not different between the two groups. Leertouwer et al.9 performed a meta-analysis of renal arterial stent placement in comparison with renal angioplasty in patients with renal arterial stenosis, including studies published up to August 1998. The cure rate for hypertension see more was higher after stent placement than after renal angioplasty (60–70%) but the probability of improvement in renal function following intervention was lower after stenting compared with conventional angioplasty (20% vs 10% and 30% vs 38%, respectively; P < 0.001). This ZD1839 ic50 may be because the stent studies included more patients with impaired renal function instead of hypertension, which may affect the clinical outcome in terms of renal function. In addition, many of these studies used an isolated serum creatinine concentration as a measure of renal impairment, which is an imprecise measure of renal disease progression. The complication rate of the stent procedure was 8–25%. Rocha-Singh et al.10 looked at stenting after failed PTRA in the ASPIRE-2 study. This population with uncontrolled hypertension and multiple comorbidities

had an 80% procedural success, a 9-month restenosis rate of 17.4% and a 19 mmHg reduction in systolic BP at 24 months. Serum creatinine was unchanged and the complication rate was 19.7% at 2 years. Zahringer et al.11 in the ‘Great Trial’ compared a sirolimus-eluting stent with a bare metal stent and demonstrated a 20/10 mmHg BP reduction, a small trend to improved creatinine, and a 26% complication rate. There have been five RCTs comparing Erastin clinical trial balloon angioplasty with medical therapy in hypertensive patients with high-grade RAS (greater than 50% reduction in luminal diameter) now totalling >1000 patients. Three meta-analyses have been undertaken that look at the first three trials before the ASTRAL study and one

systematic review which graded the quality of uncontrolled studies. The few additional uncontrolled studies since are mainly using distal protection. Two of the meta-analyses demonstrate no clear difference in BP, and the third demonstrates a weighted mean difference of a 7 mmHg reduction in systolic BP, and a 3 mmHg reduction in diastolic BP, with no difference in renal function. However, the likelihood of a patent artery from angioplasty at 12 months was 52% compared with 19% with medical therapy. This difference is considered significant in the literature but the small trial that this difference is based on has both a marked occlusive rate and only a 50% patency rate in both populations, making it difficult to conclude robustly that this is a real phenomenon.

1%) compared with control mice (32±1.4%). These learn more data suggest that the enhanced incidence of diabetes in mice reconstituted with CD4− iNKT cells is due to the increased frequency of diabetogenic BDC2.5 T cells. Indeed, the frequency of pathogenic

BDC2.5 T cells is probably a key parameter controlling the development of diabetes, since non-diabetic mice reconstituted with CD4+ iNKT cells contained only 0.9±0.2% and 12±6.4% of BDC2.5 T cells in their PLNs and pancreas, respectively. Our results highlight the pathogenic role of CD4− iNKT cells. To demonstrate the key role of IL-17, produced by iNKT17 cells, we treated mice with an anti-IL-17 antibody. Importantly, this treatment abolished the deleterious role of CD4− iNKT cells whereas it does not alter the incidence of diabetes induced by BDC2.5 T cells alone (Fig. 4B). Altogether, our results show that CD4− iNKT cells containing iNKT17 cells exacerbate the development of diabetes in an IL-17-dependent manner. It has been well established that activation of iNKT cells by repeated αGalCer injections prevents the development of diabetes in NOD mice 8, 10, 15. Autoimmunity prevention correlated with the ability of αGalCer to induce Selleck BYL719 iNKT cell anergy and to strongly

suppress their IFN-γ production while IL-4 production was less inhibited 33. Interestingly, we have observed that αGalCer treatment suppressed not only IFN-γ by iNKT cells but also their IL-17 production whereas it does not inhibit IL-10 production (Fig. 5). This inhibition of IL-17 production could be critical in the protective role of αGalCer treatment. Our study reveals that NOD mice exhibit a high frequency of iNKT17 cells, which produce IL-17 in the pancreas and can exacerbate diabetes development upon cell transfer. Inositol oxygenase This study suggests that IL-17 can participate in the pathology of type 1 diabetes. The role of IL-17 in autoimmune diabetes was first suggested by the low IL-17 production observed in NOD mice protected against the disease after treatment with a modified self-peptide 25. More recent

studies showed that IL-17 neutralization with specific antibodies prevents the development of diabetes in NOD mice 27. Different immune cell populations can secrete IL-17 34. The role of Th17 cells in diabetes remains unclear. Indeed the induction of the disease in NOD SCID mice after transfer of in vitro polarized Th17 anti-islet T cells was abolished by anti-IL-17 treatment in one study but not in two others 25, 26. It has been reported that IL-17-producing γδT cells do not exacerbate diabetes upon co-transfer into NOD/SCID mice 35. iNKT17 cells represent a new subset of IL-17-producing cells 19 and we observed an increased frequency of this cell population in NOD mice as compared with non-autoimmune C57BL/6 mice. iNKT17 cells from NOD and C57BL/6 mice exhibit a similar phenotype, mainly CD4− and NK1.1−.

High molecular weight chaperone complexes, hsp110- or grp170-tyrosinase-related protein 2 peptide (TRP2175–192), were superior to conventional chaperones as a vaccine platform to deliver tumour-derived antigens.[74] In addition, the immunization with chaperones combined to two different melanoma antigens (gp100, TRP2) significantly improved anti-tumour efficacy compared with either of the single antigen vaccines,[74] demonstrating that hsp combination vaccines can offer increased efficacy. In a Phase II clinical

trial, vaccination with autologous tumour-derived gp96–peptide complex vaccine (hsp complex-96) together with granulocyte–macrophage colony-stimulating factor and interferon-α was associated with mild local and systemic toxicity.[75] Vaccination was proven to instigate both tumour-specific T-cell-mediated and natural killer cell responses in some Epacadostat cost patients. However, neither immunological nor clinical responses were improved compared with those recorded in a previous study investigating hsp complex-96 monotherapy. A recent study has provided the first evidence

in man of patient-specific immune responses against autologous tumour-derived peptides bound to gp96.[76] Over-expression of hsp70 increases significantly the immunogenicity of cancer cell extracts; with the mechanism of cell death influencing both hsp70 expression levels and the immunogenicity of cell extracts.[77] In addition C-X-C chemokine receptor type 7 (CXCR-7) to hsp complex from hsp70 (hsp70C), synthetic peptide-mimics of hsp70C can modulate positively MK0683 the immune response against tumours[78] and therefore provide an additional approach for therapeutic intervention. Heat shock protein 70 derived from tumours of characterized antigenic makeup could be used as a generic subunit tumour vaccine.[73] Vaccines derived from tumours or cell lines that have undergone heating to increase the abundance of hsp

may provide an innovative approach. For example, vaccination with heated autologous prostate cancer cells elicits protection against tumour challenge in 60% of vaccinated rats, compared with 0% protection in control rats receiving vaccines from non-shocked cells, together with an increase in the T helper type 1 (interferon-γ) response.[79] Heat shock protein 70 extracted from DC fused to patient-derived ovarian cancer or breast cancer cells (hsp70.PC-F) were tested as tumour vaccines.[80] The hsp70.PC-F induced T-cells expressing higher levels of interferon-γ and with increased killing capacity for tumour cells, compared with those induced by hsp derived from tumour cells, although these were characterized by a higher content of tumour antigens and the detection of hsp such as hsp90 and hsp110.