Lipopolysaccharide (LPS)-treated dendritic cells (DCs) from active BD patients showed a higher level of interleukin (IL)-1β, IL-6, IL-23 and tumour necrosis factor (TNF)-α production. FICZ or ITE selleck screening library significantly inhibited the production of IL-1β, IL-6, IL-23 and TNF-α, but induced IL-10 production by DCs derived from

active BD patients and normal controls. FICZ or ITE-treated DCs significantly inhibited the T helper type 17 (Th17) and Th1 cell response. Activation of AhR either by FICZ or ITE inhibits DC differentiation, maturation and function. Further studies are needed to investigate whether manipulation of the AhR pathway may be used to treat BD or other autoimmune diseases. ABT-199 chemical structure “
“After infection or vaccination, antigen-specific T cells proliferate then contract in numbers to a memory set point. T-cell contraction is observed after both acute and prolonged infections although it is unknown if contraction is regulated similarly in both scenarios. Here, we show that contraction of antigen-specific CD8+ and CD4+ T cells is markedly reduced in TNF/perforin-double deficient (DKO) mice responding to attenuated Listeria monocytogenes infection. Reduced contraction

in DKO mice was associated with delayed clearance of infection and sustained T-cell proliferation during the normal contraction interval. Mechanistically, sustained T-cell proliferation mapped to prolonged infection in the absence of TNF; however, reduced contraction required the additional absence of perforin since T cells in mice lacking either TNF or perforin (singly deficient) underwent normal contraction. Thus, while T-cell contraction after acute infection is independent of peforin, a perforin-dependent pathway plays a previously unappreciated role to mediate contraction of antigen-specific CD8+ and CD4+ T cells during

prolonged L. monocytogenes infection. “
“The recent article in Immunology by Park et al.[1] entitled ‘Interleukin-32 Oxymatrine enhances cytotoxic effect of natural killer cells to cancer cells via activation of death receptor 3’ is very interesting; however, I believe that non-specialist readers would benefit from a more expansive and detailed discussion of its context. The authors have omitted much of the recent literature detailing the broader biological functions of Death Receptor 3 (DR3), most of which do not relate to regulating cell death. In addition, clarification is also required with regards to the ligands of DR3 because the older nomenclature can cause confusion and is particularly pertinent to the interpretation of this study. Towards the end of 1996 and beginning of 1997, DR3 (TNFRSF25) was reported simultaneously by a number of groups as a tumour necrosis factor receptor superfamily (TNFRSF) member with an intracellular, apoptosis-inducing death domain and was ascribed a variety of names – Apo3, LARD, TR3, TRAMP and WSL-1.

It has been shown recently in a murine model that local oral DCs bind and process topically applied ovalbumin (OVA), which leads to the induction of IFN-γ- and Selleck Autophagy Compound Library IL-10-producing

T cells [41]. Furthermore, it is tempting to speculate that TLR-4 activation by components originating from commensal bacteria or supplemented to SLIT formulations might serve as adjuvants. In this regard, a recently published study in a mouse model supports the assumption that TLR-2 activation on purified murine oral mucosal DCs promotes IFN-γ- and IL-10-producing T cells [42], resulting in stronger Th1 and tolerogenic immune responses. Altogether, the published data suggest that mucosal DCs are prone to induce proinflammatory as well as tolerogenic immune responses. Nasal mucosal DCs facilitate allergic immune responses in atopic individuals, while oral mucosal DCs such as oLCs induce preferentially a regulatory immune response, which on one hand supports the immunological homeostasis within oral mucosal tissue, and on the other hand propagates the desired allergen-specific tolerance induction during SLIT. The variable subtypes of DCs, as well as functions of DCs located in different microenvironments such as non-inflammatory versus inflammatory skin or mucosal tissue, account for the highly versatile character of DCs, ranging from good to very bad players

of allergic–inflammatory immune responses. The notion that regulatory missions of DCs are modulated directly by the character click here of the microenvironment provides several exciting ways in which DCs might be decisive for the prevention or promotion of allergic–inflammatory reactions and a healthy or diseased immune state, both under physiological conditions or as therapeutic target cells. This work was supported by grants from the Deutsche Forschungsgemeinschaft (SFB704 TPA4, KFO209 TP A1) and a BONFOR grant of the University of Bonn. N.N. is supported by a Heisenberg-Professorship HSP90 of the DFG NO454/5-2. The authors have

received grants and lecture fees from Alk Abello, Stallergenes, Novartis, Bencard Allergy Therapeutics and the German Research Council. “
“National Institute of Arthritis and Musculoskeletal and Skin Diseases, National Institutes of Health, Bethesda, Maryland, USA In helper T cells, IL-13 is traditionally considered a Th2-type cytokine that is coexpressed with IL-4. Using mouse models of immunization and autoimmunity, we demonstrate that IL-13 is frequently uncoupled from IL-4, and that it can be produced by both IFN-γ+ Th1 cells and IL-17+ Th17 cells. We report that these IL-13-producing Th1 and Th17 cells are distinct from classical IL-4+ Th2 cells and that they are relatively common, appearing in the context of both protective and pathogenic T-cell responses.

ELISAs were developed using o-phenyl diamine dihydrochloride (OPD) substrate (Sigma) in sodium citrate buffer, ACP-196 order pH 5, plus H2O2. H2SO4 (12·5%) was used to stop the OPD reaction, and plates were read at

490 nm using Softmax™ Pro software (MDS Analytical Technologies, Sunnyvale, CA). Modulation of the CD3–TCR complex in peripheral blood was analyzed by flow cytometry 2 and 24 hr after each dose when mice were dosed every 24 hr and 2 and 72 hr after each dose when mice were dosed every 72 hr. Following red blood cell lysis, cells were stained using murine antibodies to CD3 (145-2C11), CD4 (RM4-5), CD8 (53-6.7) and TCR-β (H57-597) (BD Biosciences, San Jose, CA). Molecules of equivalent soluble fluorochrome (MESF) values were generated Rapamycin using Quantam™ fluorescein isothiocyanate (FITC) MESF microspheres as per the manufacturer’s instructions (Bangs Laboratories,

Fisher, IN). FoxP3 expression was evaluated using a FoxP3 staining kit (NRRF30 clone; eBioscience, San Diego, CA), as per the manufacturer’s instructions. Fluorescent cells were analyzed by flow cytometry using FACScalibur (BD Biosciences). In Study B, serum was collected before and after treatment and analyzed for the murine C-peptide I content by ELISA, according to the manufacturer’s instructions (ALPCO, Salem, NH). In Study B, pancreata were fixed in formalin, processed and embedded in paraffin. CHIR-99021 mw Sections of 4–5 μm in thickness were stained with haematoxylin and eosin. Islet inflammation was evaluated using light microscopy by a board-certified veterinary pathologist (Charles River Laboratories, Wilmington, MA). Peri-insulitis inflammation was scored as: 0 = normal (no leucocytes);

1 = minimal (< 5 leucocytes in any islet); 2 = mild (6–20 leucocytes in the ‘most severe’ islet); 3 = moderate (21–50 leucocytes in the ‘most severe’ islet); 4 = marked (> 50 leucocytes in the ‘most severe’ islet); or 5 = severe (> 50 leucocytes in > 1 islet). MESF values were analyzed using repeated-measures analysis of variance (anova), with treatment and time as factors. Lymphocyte count data were analyzed by one-way anova. Pairwise treatment group comparisons for these analyses were carried out using the corresponding t-tests. Fisher’s exact test was used for pairwise treatment group comparisons of proportion data. Exploratory comparisons between post-treatment remission and diabetic groups were made using t-tests (quantitative data), Fisher’s exact test (proportion data), or the chi-square test (categorical data). P-values were not adjusted for multiple comparisons.

The percentage and absolute numbers of different cell types were determined by flow cytometric analysis and cell-counting beads (Life Technologies, Grand Island, NY). FACS analysis was performed using a BD Biosciences LSRII Flow cytometer and FlowJo (Tree Star, Ashland, OR) analysis software. In other SB203580 cost experiments,

cells from blood were analysed and quantified by flow cytometry. Expression of CXCR2, CD62 ligand and CD44 on neutrophils in blood was quantified using antibodies purchased from eBioscience. C57BL/6 and MyD88−/− mice were treated with a cocktail of broad-spectrum antibiotics in their drinking water starting from birth to the time they were used in experiments as described before.[22] The antibiotic cocktail consisted of ampicillin 1 g/l, neomycin 1 g/l, metronidazole 1 g/l (Sigma-Aldrich) and vancomycin 0·5 g/l (PhytoTechnology

Laboratories, Shawnee Mission, KS). The artificial aspartame sweetener, Equal (Merisant Company, Chicago, IL) was added to the water 5 g/l to make it palatable for the mice to drink. Pups received the antibiotics indirectly via lactating mothers till they were weaned. Drinking water containing the antibiotics was replaced every week. DNA was isolated from colonic contents of find more mice by the DNeasy Blood and Tissue Kit (Qiagen, Hilden, Germany). The quantitative PCR primers used to amplify the bacterial 16S V2 region were sense, 5′-AGYGGCGIACGGGTGAGTAA-3′; and anti-sense, 5′-CYIACTGCTGCCTCCCGTAG-3′. Quantitative PCR primers used to amplify the housekeeping gene GAPDH were sense 5′-TGATGGGTGTGAACCACGAG-3′; and anti-sense 5′-TCAGTGTAGCCCAAGATGCC-3′. Quantitative PCR was performed using the iQ SYBR Green supermix on the CFX96 Touch Bio-Rad machine (Bio-Rad, Hercules, CA). The PCR cycling

reaction used was 15 min activation step (95°C); 35 cycles of 30 seconds denaturation (95°C), 30 seconds annealing (60°), and 30 seconds extension (72°C). Lipopolysaccharide (LPS) from Escherichia Bay 11-7085 coli, serotype 026:B6, purified by gel-filtration chromatograph (Sigma Aldrich) was administered in the drinking water of mice at a concentration of 33 mg/l from 3 to 5 weeks of age. Tamoxifen (Sigma-Aldrich) solution was prepared in corn oil (Sigma-Aldrich) at 10 mg/ml by incubating at 37°C for 2 hr. To induce deletion of floxed genes in adult mice, tamoxifen (50 mg/kg of body weight) was administered to floxed mice by oral gavage for three alternate days. Mice were used in experiments 7 days after the last administration. For treating pups, lactating mothers were treated intraperitoneally with tamoxifen (200 mg/kg of body weight) from the day of birth for 5 consecutive days. The efficiency of deletion of floxed MyD88 allele was assessed using Taqman PCR using primers and the method described previously.[23] The PCR cycling reaction was performed on the C1000 Thermal Cycler (Bio-Rad).

The following selleckchem mice were used in this study: C57BL/6 mice, CD80/86−/− 18 CD11c-DTR transgenic (B6.FVB-Tg Itgax-DTR/GFP 57Lan/J) mice carrying a transgene encoding a human DTR-GFP fusion protein under the control of the murine CD11c promoter 15; CD11c-Cre mice 31, R26-DTA mice 32 and R26-DTA mice were crossed with CD11c-Cre transgenic mice to generate CD11c-Cre:DTA mice 15. For conditional DC ablation [CD11c-DTR>wt], BM chimeras were inoculated intraperitoneally every second day for 2 wk with 16 ng DTx/g body weight. For BM chimera generation, recipient mice were lethally irradiated with a 950 rad dose and a day later i.v. injected with 5×106 BM cells isolated from donors femora and tibiae.

BM recipients were then allowed to rest for 8 wk before use. All mice were maintained under specific pathogen-free conditions

and handled under protocols approved by the Weizmann Institute Animal Care Committee according to international guidelines. Staining reagents used PF-6463922 chemical structure in this study included the PE-coupled antibodies anti-MHC II, CD25, CD62L, CD8, CD11b, CD115, CD80, IL-17; the biotinylated antibodies: anti CD45.1, CD4, CD3; the APC-coupled antibodies: anti CD11c, CD4, CD44, IFN-γ, CD19 and Gr-1 (Ly6C/G); and PerCP-coupled streptavidin. Foxp3 intracellular staining was performed according to the manufacturer’s protocol (eBioscience 77-5775-40). Unless indicated otherwise, the reagents were obtained from eBioscience or Biolegend. The cells were analyzed on a FACS Calibur Glutamate dehydrogenase cytometer (Becton-Dickinson) using CellQuest software (Becton-Dickinson). Cells obtained from mesenteric LN were incubated at 37C for 4 h in 10% FBS DMEM medium with 50 ng/mL PMA (Sigma-Aldrich) and 1 μg/mL ionomyicin (Sigma-Aldrich). Brefeldin A (5 μg/mL, Sigma-Aldrich) was added after 2 h. Cells were resuspended in fixation/permeabilization solution (Cytofix/Cytoperm kit, BD). Intracellular cytokine staining using anti-IL-17 and anti-IFN-γ was performed according to the manufacturer’s protocol. Serum immunoglobulin isotypes were determined using commercial ELISA

antibodies (SouthernBiotech). C57BL/6 mice were inoculated with B16 tumor cells (3×106) that had been manipulated to overexpress Flt3L 22. All statistics were generated using a Student’s t-test. All error bars in diagrams, and numbers following a ± sign, are standard deviations. The authors thank all lab members of the Jung laboratory for helpful discussions. This work was supported by the Israel Science Foundation (ISF) and the Yeda-Sela Center for Basic Research. Conflict of interest: The authors declare no financial or commercial conflict of interest. See accompanying commentary:http://dx.doi.org/10.1002/eji.201041335 “
“The epithelial cells of the thymus govern the differentiation of hematopoietic precursors into T cells, which are critical for acquired immunity.

It is tempting to argue that upon uptake of apoptotic DC, conversion of viable immature DC to tolerogenic DC with a potential to induce Treg via secretion of TGF-β1 is largely phosphatidylserine dependent. However, in

our study, when viable immature DC were exposed to apoptotic splenocytes, no increase in TGF-β1 secretion was observed, and previous studies have also indicated that exposure of murine DC to apoptotic cells or phosphatidylserine does not induce TGF-β1 secretion 24–26. Therefore, it is likely that the ability to secrete TGF-β1 and to induce Foxp3+ Treg may be dependent CP-673451 price on the uptake of apoptotic DC by viable DC, which has not been described previously and could be independent of phosphatidylserine. It is

feasible that as DC undergo apoptosis, there is exposure of phosphatidylserine, which may play a passive role in the suppression of DC by suppressing the ability of DC to undergo maturation without any induction of Foxp3+ Treg.. We propose that uptake of apoptotic DC, in particular, triggers signaling through a previously unidentified receptor in viable DC that induces TGF-β1 secretion. Our findings identify that the release of TGF-β1 upon uptake of apoptotic DC by viable DC is regulated at translational level via mTOR pathway. Mammalian target of rapamycin (mTOR), a serine/threonine JQ1 purchase protein kinase, is a regulator of translation and its major substrates include p70S60K serine/threonine kinase and 4EBP-1. mTOR phosphorylates 4EBP-1 which results in the release of protein

translation initiation factor eIF4E. eIF4E plays a role in enhancing rates of translation of capped mRNA which also includes TGF-β1. mTOR is likely regulated upstream by PI3/Akt pathway, and Rho A has previously been HSP90 shown to induce PI3 pathway to prevent myoblast death 27. Therefore, it is likely that RhoA induces PI3K which phosphorylates mTOR resulting in release of eIF4E, which further results in increased translation of TGF-β1 mRNA. Some studies have indicated that another mechanism whereby DC can acquire tolerogenic potential is through induction of IDO 28, 29. Our results show no upregulation of IDO upon uptake of apoptotic DC by viable DC, indicating that induction of IDO is likely not the underlying mechanism for tolerance induction (data not shown). The hallmarks of sepsis include impaired immune function along with immunosuppression 30. Concominantly, there is substantial depletion of DC along with increased levels of circulating Treg 31–33. However, the mechanism of how DC apoptosis can contribute to immunosuppression in sepsis is unclear. Our findings suggest that perhaps enhanced DC apoptosis in sepsis may result in their uptake by viable DC, resulting in immunosuppression and Treg induction/expansion. We need to be cautious in interpreting our findings because our data indicates that several fold higher amounts of apoptotic DC are required than live DC for tolerance induction.

However, HDAC inhibitors can impact a wide array of cellular functions through alterations in gene expression or post-translational protein modification. The functional unresponsiveness characteristic of CD4+ T cell anergy was initially demonstrated in CD4+ T cells stimulated in the absence of co-stimulatory signals [8]. Subsequent work established that these anergized CD4+ T cells were sequestered in the G1 phase of

the cell cycle [9]. This finding inspired a search of various pharmacological agents known to block cell cycle progression, with the aim of locating an agent that could induce CD4+ T cell anergy, even in the presence of co-stimulation check details [10]. Known G1 blocker and HDAC inhibitor n-butyrate was shown to be such an agent. n-Butyrate induced anergy in murine CD4+ T cells stimulated with antigen in the presence of co-stimulation, LY294002 purchase but not in un-stimulated CD4+ T cells [11]. This observation suggests that short-term exposure to an HDAC inhibitor such as n-butyrate could control unwanted immune responses through deactivation of activated effector CD4+ T cells while allowing naïve T cells to respond to future challenge. One of the functions attributed to HDAC inhibitors is the capacity to enhance the generation and/or activity of Treg cells [12]. Murine Treg cells express transcription factor FoxP3 and have been shown to suppress activated effector

CD4+ T cells [13]. Treg cells may arise naturally from the thymus as part of immune tolerance or can be induced experimentally as a means of inhibiting unwanted T cell-mediated immune responses [14]. If the only mechanism for HDAC inhibitor–induced anergy requires Treg cell activity, the therapeutic potential of this class of drugs might be limited. Studies suggest a correlation between autoimmune disease and an increased risk for development of cancer in the lungs, liver,

skin and pancreas [15, 16]. Positively skewing an autoimmune patient’s Treg cell profile may be harmful, as it is known that the suppressive properties of Treg cells present an obstacle to immune clearance of tumours [17]. Documenting Treg cell-independent DNA ligase CD4+ T cell anergy induced by HDAC inhibitors would underline the functional significance of this class of drugs for patients in which increased Treg cell activity may not be helpful. The Gilbert lab has previously reported that n-butyrate induced anergy in Th1 CD4+ T cell clones [10, 11, 18, 19]. Those CD4+ T cells were highly differentiated and unlikely to exhibit the plasticity needed to convert into Treg cells. However, a direct role for Treg cells in n-butyrate-induced CD4+ T cell anergy was not examined in those studies. We extended those studies to determine if n-butyrate-induced CD4+ T cell anergy requires the generation of suppressive CD4+FoxP3+ Treg cells. Mice.

It is not clear whether the kidneys remove cardiac troponin from

the circulation. The cardiac troponins are too large to be filtered by the glomerulus and are predominantly released as either free cTnT, cTnT:I:C complex or cTnI:C complex (Table 1). Free cTnI is less often identified.7 However, cardiac troponin has been measured in the urine of patients with reduced kidney function79 and measures of troponin kinetics such as half-life, peak maximum value and area under the curve were significantly increased in patients with creatinine clearance <60 mL/min selleck products compared with >60 mL/min in a study of patients undergoing coronary artery bypass graft surgery.80 These measures were not significantly different in haemodialysis patients compared with people with normal kidney function after myocardial infarction.81 One group identified smaller fragments of cTnT in the serum of patients with ESKD that could accumulate in renal failure and be detected by troponin assays.82 However, other investigators failed Fostamatinib solubility dmso to find such cTnT fragments.83 The fate of BNP-32 in the circulation is much better understood than that of NT-BNP-76. The active

hormone, BNP-32, binds to natriuretic peptide receptor A, which mediates its biological actions, and to natriuretic peptide receptor C, which is responsible for clearance of BNP-32 via receptor-mediated endocytosis and lysosomal degradation.9 Neutral endopeptidases also cause enzymatic degradation by breaking the ring structure of BNP-3284 and the kidneys are an important site for removal of the peptide in this way. Conversely, NT-BNP-76 has no ring structure and these processes have not been demonstrated to be involved in its removal from the circulation. Sinomenine One controversy regarding

NT-BNP-76 is whether renal clearance is more important for this form of BNP than for BNP-32. Although both forms are released by the ventricles in equimolar amounts, the level of NT-BNP-76 in the serum of patients with reduced kidney function is substantially greater than BNP-32.5,85 Furthermore, the ratio of NT-BNP-76 to BNP-32 is higher in patients with lower glomerular filtration rate (GFR),85,86 leading some to speculate a role for renal elimination. However, other investigators have demonstrated no difference in the strength of the association of BNP-32 or NT-BNP-76 with renal function.

, 1999) but may also be suspended in host material as seen in many chronic infections (Burmølle et al., 2010). Microbiologists have up until the last few decades focused and emphasized the planktonic state over the biofilm state. However, the importance of the biofilm mode of growth is becoming increasingly

recognized as improved methods to study sessile bacteria have become available, and hence the subsequent accumulation of evidence for its widespread presence. It has been suggested that bacteria are predominantly growing as sessile communities rather than as single cells (Costerton et al., 1987; Davey & O’Toole, 2000). Sessile growing bacteria are defined as an assemblage of cells embedded ‘in a self-produced polymeric matrix’. This matrix is SB525334 very important for the properties of the biofilm, because it offers structural stability and increased tolerance to antimicrobials and immune cells (Stoodley Selleck Vemurafenib et al., 2002; Anderson & O’Toole, 2008; Mulcahy et al., 2008; Ma et al., 2009). To gain further information on this phenomenon, one has to investigate how a biofilm is established and propagated. The most

common method is the continuous-culture once-through flow system using the model organism Pseudomonas aeruginosa. In this system, media are slowly passed over the biofilm-growing bacteria, which have attached to a cover slip on a flow cell. This in vitro process of P. aeruginosa biofilm formation can be divided into at least five stages: in the first stage, planktonic cells reversibly attach to a vacant surface. Irreversible binding follows this attachment and then multiplication into microcolonies. The microcolonies produce an extracellular polymeric matrix, which in turn envelopes the colonies. After a couple of days, the microcolonies MRIP attain tower- or mushroom-like structures measuring up to 50 μm in the flow cell (Costerton et al., 1995; Davey & O’Toole, 2000;

Stoodley et al., 2002). The extracellular matrix contains a mixture of polysaccharides, proteins, and DNA (Wingender et al., 2001; Whitchurch et al., 2002; Costerton et al., 2003). When the biofilm grows to a size not beneficial for bacterial survival and growth (e.g., owing to nutrient limitations), focal areas of the biofilm are sloughed off. It is hypothesized this enables the otherwise sessile biofilm bacteria to spread and colonize new surfaces and biofilms to spread. Hence, it seems that the biofilm lifecycle by P. aeruginosa is a dynamic process capable of renewing itself (Costerton et al., 1995; Davey & O’Toole, 2000; Stoodley et al., 2002). The biofilm lifecycle and the matrix components have preferably been investigated by means of confocal laser scanning microscopy (CLSM). This method has provided valuable insight into the biofilm development; however, the information on the detailed ultrastructure of the biofilm is difficult to image by light microscopes.

The sample is injected onto a column

of cation exchange resin and derivatized with o-phthalaldehyde. The reaction with the amino acids present in the eluent forms conjugated compounds whose quantity is then established by spectrophotometric analysis. The amount of each reaction product is directly proportional to the quantity of amino acid present. The retention time of peak identifies the amino acid, the area under the peak indicating the quality of amino acid present. The required calibration analysis has been performed by using nor-leucine as internal standard. All data are expressed as mean ± standard error of the mean (SEM) or ± standard deviation (SD). The SE estimate for the fitted rheobase (R) and time constant (τ) values (and relative independent Ceritinib chemical structure statistical analysis) were obtained as previously described. Independent one-way anova analysis for multiple comparison of drug efficacy was performed on the two fitted values [8,29]. Statistical analysis for direct comparison between two means was performed by unpaired Student’s t-test. Multiple statistical

comparison between groups HM781-36B cell line was performed by one-way anova, with Bonferroni’s t-test post hoc correction for allowing a better evaluation of intra- and inter-group variability and avoiding false positive. Animal groups were homogenous for body weight and fore limb strength at the beginning of the study (Table 1). As expected, a typical reduction in fore limb strength was observed after 4 weeks of exercise in the mdx animals [8]. The three groups of drug-treated mdx mice showed an amelioration of the exercise-induced decrease of fore limb strength, detectable on both the absolute strength value and its 4-week

increment (Table 1). However, the effect was remarkable and significant only with the combination PDN + taurine, which exerted a greater effect than either of the two drugs administered alone. A difference in body weight gain was observed between the drug-treated groups, with PDN- and PDN + taurine-treated mice showing the less not increment. To take into account the inter-individual influence of body weight, for each mouse the fore limb strength has been normalized to body weight both at the beginning (time 0) and at the end of 4 weeks of exercise (time 4) and the normalized force increment over the 4 weeks of treatment was calculated (Figure 1). In agreement with previous findings [8], both PDN and taurine significantly contrasted the exercise-induced impairment of normalized force increment. The increment presently observed with PDN was greater than that previously found, likely in relation to the different administration route used (i.p. vs. oral [8];).