The difference of plasma sRAGE between patients with normal CP-673451 ic50 (>90 ml/min per 1.73 m2) and lower eGFR was not statistical significant (887.7 ± 82.5 pg/ml versus 949.5±155.1 pg/ml, P = 0.733). The positive rates for ANA, anti-dsDNA, AnuA, anti-Sm were 92.2% (95/103), 53.9% (55/102), 55.7% (54/97), 37.1% (30/89), respectively, in patients with SLE. There was no significant difference between sRAGE levels in patients

with negative ANA and those with different levels of ANA (Fig. 4A). In addition, there was no significant difference between the sRAGE levels in autoantibody-positive patients and those in autoantibody-negative patients (Fig. 4B,C,D). In patients

with SLE, plasma sRAGE levels was negatively correlated with the leucocyte count (n = 95, r = −0.326, P = 0.001, Fig. 5A), absolute values of lymphocytes (n = 95, r = −0.357, P = 0.000, Fig. 5B), neutrophils (n = 95, r = −0.272, P = 0.008, Fig. 5C) and monocytes (n = 95, r = −0.286, P = 0.005, Fig. 5D) in peripheral blood. In this study, we found that plasma sRAGE level in patients with SLE was lower than that in HC, while there was no significant difference of sRAGE level between active and inactive patients. Decreased sRAGE levels in patients with SLE may be explained by the consumption of this soluble receptor. Renard et al. [36] postulated that sRAGE-ligand complexes were eliminated from the blood via spleen and/or liver. JQ1 concentration It has been demonstrated that the level of HMGB1, one important RAGE ligand, is increased in the HSP90 circulation of SLE [19, 20], leading to the binding and consumption of sRAGE during the inflammatory process. It is also possible that sRAGE levels in patients with SLE may be regulated by alternative splicing and proteinases and this possibility needs to be clarified in the

future research. sRAGE might not only function as a decoy to exert their inhibitory effects on RAGE, but also act in a more direct way, e.g. binding to cell surface RAGE to block the formation of homodimers [28]. Therefore, decreased levels of sRAGE, which may contribute to enhanced RAGE-mediated pro-inflammatory signalling [27], support the essential role of RAGE in SLE pathology. Our results were different from the recent report showing that blood sRAGE levels in patients with SLE were higher than those in HC and compared with quiescent SLE, blood sRAGE levels are significantly increased during active disease [34]. One explanation for this discrepancy is that use of medication might influence the results. The discrepancy may also be caused by the low number of cases included in that study (only 10 cases of patients with SLE).

The expression of IL-6 in the supernatant is also increased as seen in the cell lysate (data not shown). Collectively, these in vitro results confirm our findings derived

from cav1 KO mice indicating that the typical phenotypes for K. pneumoniae infection in these mice may result from a dysregulated proinflammatory response associated with altered Akt-STAT5 regulation (Fig. 7). We show severely impaired immunity in cav1 KO mice after infection by K. pneumoniae. cav1 KO mice exhibited a lethal phenotype including elevated bacterial burdens, severe lung injury, and increased septicemia see more compared with WT mice. The levels of TNF-α, IL-1β, and IL-6 were significantly increased in BAL fluid. IL-27p28 was increased both in the lung and Saracatinib solubility dmso kidney, while MIP2 was increased only in the kidney. Our studies indicate that this cytokine profile was regulated by the GSK3β−β-catenin−Akt pathway, which may impact STAT5 activity. In addition, the phagocytic ability of AMs was found to be impaired in infected animals. To our knowledge, these data are the first to reveal that Cav1 is a critical regulator for bacterial immunity against K. pneumoniae. As Cav1

KO mice may gradually develop respiratory complications including fibrosis in late age (12 months), the mice used for infection were younger than 4 months of age. Recent studies using cav1 KO mice have linked Cav1 to innate immunity against P. aeruginosa in lung epithelial cells [[9-11]]. P. aeruginosa utilizes lipid raft-mediated endocytosis as a means of invasion [[6, 20-22]]. Since Cav1 is a structural protein of lipid rafts, Cav1 deficiency is thought to compromise immune function against P.

aeruginosa [[1, 9, 10]]. To better characterize the role of Cav1 in bacterial infections, we studied the immune response of cav1 KO mice against another bacterium, K. pneumoniae. As this bacterium has not been documented to invade host cells via Dipeptidyl peptidase lipid rafts, this model may complement previous studies on Cav1′s immunity. cav1 KO mice exhibited a severe outcome following K. pneumoniae infection compared with WT mice: elevated bacterial numbers, exacerbated lung injury, and severe septicemia. These results are consistent with previous findings [[9]], wherein P. aeruginosa-induced pneumonia developed into a systemic bacterial infection in cav1 KO mice. Along the same lines, Lisanti et al. reported that cav1 KO mice displayed decreased survival rates when intravenously challenged with S. Typhimurium [[8]]. Therefore, our current data support the growing consensus that Cav1 fulfills a crucial function in resistance to invasive pathogens. TNF-α and IL-1β are two potent proinflammatory cytokines. Our results show that their contributions to the proinflammatory response to K. pneumonia intensified under Cav1 deficiency. Both of these cytokines also share a wide range of biological activities, including neutrophil penetration [[23]].

1) with moderate FDA approved Drug Library datasheet interstitial inflammatory cell infiltrate and moderate tubulitis. There was also evidence of moderate peritubular capillaritis. Electron microscopy and fluorescence failed to show evidence of viral inclusions

and stains for BKV, CMV or HSV were negative. Immunofluorescence was negative for C4d. Because of concerns about rejection in the face of possible ongoing viral nephropathy and possible nephrotoxicity from cidofovir, intravenous immunoglobulin (IVIG) was administered at 1 mg/kg weekly and the cidofovir stopped. Over the following 3 days, her fever settled immediately and her creatinine, after peaking at 339 μmol/L, begun to fall sharply. By day 5 her creatinine had fallen to 175 μmol/L, she remained afebrile and her systemic malaise had improved. Her creatinine timeline and therapy as shown in Fig. 2. Discharged home for convalescence, the patient continued to receive a further 3 weekly doses of IVIG (1 mg/kg) JQ1 in vitro and her creatinine continued to fall such that 3 weeks post biopsy the creatinine was 127 μmol/L. Adenovirus PCR remains positive in the urine and respiratory secretions however have been undetectable in the serum and plasma since the last day of cidofovir. Repeat transplant

biopsy at day 98 did not show ongoing vascular rejection or viral inclusions but there was a mild ongoing cellular Palmatine infiltrate. These cases illustrate the potential severity of adenovirus infection in kidney transplant recipients, and highlight the need for consideration of adenovirus infection as a cause of fever of unknown origin in such patients. They also illustrate that disseminated adenovirus infection can present early as well as late from the time of transplantation. Both cases also illustrate the potential renal toxicity of cidofovir. Adenoviral disease is well characterized in haematopoietic stem cell transplant (HSCT) recipients, with incidence ranging from 3% to 47%.[1] Reported clinical syndromes include pneumonia, colitis, hepatitis, haemorrhagic

cystitis, tubulointerstitial nephritis and encephalitis. Disease is often disseminated, and the mortality rate for symptomatic patients approaches 26%.[2] However adenovirus is a rare pathogen in solid organ transplant recipients. In kidney transplant recipients, the most common manifestation is hemorrhagic cystitis which both of our patients presented with. A recent literature review[3] revealed 37 reported cases, 36 of which occurred within 1 year of transplantation. Thirty-four patients received high-dose steroids for treatment of symptoms of acute rejection. Four patients received antiviral medications. Disease was mild and self-limiting in all and no patient required dialysis. There was universal return of creatinine to near baseline.

Domain I, the N-terminal ∼120 residues, is highly basic and is probably involved in the recruitment of the viral RNA during particle formation. Domain II, situated between a.a.∼120 and ∼175, has been predicted to form one or two alpha-helices that are presumed to be involved in the association of Core with membrane proteins and lipids. This domain is not present in the capsid proteins of most of the other members of the Flaviviridae family. It has recently been shown that the cysteine residue at a.a.128 is responsible for the disulfide-bonded dimer of Core and for particle formation (19). Domain III, located at

the C-terminal ∼20 residues, is highly hydrophobic and has been predicted to form an alpha helix. This domain serves as a signal sequence ABT-888 manufacturer Peptide 17 for E1 as described above. The ubiquitin-proteasome pathway, a major route by which selective protein degradation occurs in eukaryotic cells, is involved

in post-translational modification of Core (20–25). Ubiquitin ligase E6AP has been identified as a core-binding protein that enhances its ubiquitylation and degradation. It has been suggested that E6AP-dependent degradation of Core is common to a variety of HCV isolates and plays a critical role in the HCV life cycle (23). Recently, we also demonstrated that proteasomal degradation of Core is mediated by two distinct mechanisms. One leads to polyubiquitylation in which lysine residues in the N-terminal region are preferential ubiquitylation sites. The other is ubiquitin-independent, Fossariinae but depends on interaction with proteasome activator PA28gamma (24). Although is so far unclear as to whether destabilization of Core via two distinct mechanisms is physiologically significant, it is reasonable to consider that tight control over cellular levels of Core may contribute to restricting its potential for functional activity. E1 and E2 proteins are essential

components of the virion envelope and are necessary for viral entry. These glycosylated proteins extend from a.a. 192–383 (E1) and from a.a. 384–746 (E2) of the polyprotein, and have molecular weights of 33–35 and 70–72 kDa, respectively (26). Intracellular envelope proteins mainly exhibit high-mannose type glycans, consistent with their accumulation in the ER (27), whereas infectious-virion-associated envelope proteins display a mixture of high-mannose and complex types of glycans. It has been shown that E1 and E2 are heavily glycosylated, suggesting that HCV glycoproteins are processed by Golgi-resident glycosidases and glycosyltransferases (28). Complex N-linked glycans have also been detected on the surface of HCV particles isolated from patient sera (29). Based on prediction of membrane topology, it is hairpin structures that pass through the membrane twice, thereby allowing processing by a signal peptide in the ER lumen (30).

Larger SIEA diameters correlated with a find more decrease in diameter of ipsilateral DIEA perforators. Conclusion: The SIEA is present more frequently than previously demonstrated, but is typically too small for use in free tissue transfer. The variable degree of SIEA branching suggests that its territory of supply is also variable, and that preoperative imaging may be useful in planning SIEA flaps. © 2010 Wiley-Liss, Inc. Microsurgery 30:386–391, 2010. “
“Combined neurotization of both axillary and suprascapular nerves in shoulder reanimation

has been widely accepted in brachial plexus injuries, and the functional outcome is much superior to single nerve transfer. This study describes the surgical anatomy for axillary nerve relative to the available donor nerves and emphasize the salient technical aspects of anterior deltopectoral approach in brachial plexus injuries. Fifteen patients with brachial plexus injury who had axillary nerve neurotizations were evaluated. Five patients had complete avulsion, 9 patients had Selleckchem PD0325901 C5, six patients had brachial plexus

injury pattern, and one patient had combined axillary and suprascapular nerve injury. The long head of triceps branch was the donor in C5,6 injuries; nerve to brachialis in combined nerve injury and intercostals for C5-T1 avulsion injuries. All these donors were identified through the anterior approach, and the nerve transfer was done. The recovery of deltoid was found excellent (M5) in C5,6 brachial plexus injuries with an average of 134.4° abduction at follow up

of average 34.6 months. The shoulder recovery was good with 130° abduction in a case of combined axillary and suprascapular nerve injury. The deltoid recovery was good (M3) in C5-T1 avulsion injuries patients with an average of 64° shoulder abduction at follow up of 35 months. We believe that anterior approach is simple and easy for all axillary nerve transfers in brachial plexus injuries. © 2012 Wiley Periodicals, Inc. Microsurgery, 2012. “
“Peripheral neuropathy is the most common Resveratrol nerve disorder in human immunodeficiency virus (HIV) patients. Distal symmetrical sensory polyneuropathy (DSP) affects roughly one third of HIV patients. With the introduction of antiretrovirals, more patients are surviving longer, and chronic complications are surfacing. Three consecutive patients with at least a 5-year history of HIV presented during the period from 2007 to 2009. All three patients were on antiretrovirals and had no other comorbid conditions such as spinal pathology or diabetes. All patients had symptoms of pain, numbness, and weakness. Quantitative sensory testing and/or electromyography/nerve conduction testing (EMG/NCT) were performed preoperatively and correlated with the presence of Tinel signs. Targeted nerve releases were performed in four extremities, for a total of 18 nerves.

05 M bicarbonate buffer (pH 9.6), and then washed and blocked with 1% BSA (Biochemical Reagents, Kyoto, Japan). Washes were performed in between steps with PBST and PBS. Serum samples were diluted 1:200 with PBS

and applied Gemcitabine price to the plates in duplicate and in twofold serial dilutions to 1:1,638,400 for 2 hrs at 37°C. After washing, secondary antibody–alkaline phosphatase-conjugated anti-mouse IgG (Cell Signaling Technology, Danvers, MA, USA; 1:4,000) was added to the corresponding plates, which were again incubated at 37°C for 2 hrs. Finally, after extensive washing, 0.1 mL of p-nitrophenyl phosphate solution (Sigma–Aldrich) was added to each well and the OD read at 405 nm with a microplate reader (ImmunoMini Nj-2300; Nunc, Rochester, NY, USA). Values of end-point total IgG titers above the background cutoff level (in which the optical density was at least twofold greater in the OVA-coated wells than non-coated wells)

JNK high throughput screening were considered positive. Titers are shown as end-point dilutions. The end-point titers were expressed as means ± SEM and compared by nonparametric Mann–Whitney’s U-test. In all analyses, P < 0.05 was taken to indicate statistical significance. To characterize the ability of pyriproxyfen to enhance the immune response, we first examined the total IgG immune response to pyriproxyfen with OVA-immunized mice at different time points. Figure 2 shows the end-point titers of total IgG. As shown in Figure 2a, b, at Weeks 3 and 5 there were no significant differences in OVA-specific for total IgG titers between pyriproxyfen with OVA-immunized mice and controls. However, significant increases in OVA-specific total IgG titers were observed by Week 7, which increased by Week 8 (three- and fourfold greater, respectively) compared to controls (P = 0.04 and P = 0.02, respectively; Fig. 2c, d). OVA administered with

alum induced a rapid significant increase in OVA-specific total IgG titer by Week 3 (1.5-fold greater than control; P = 0.02, Fig. 2a) and finally increased by threefold at 7 and 8 weeks (P = 0.02 and P = 0.02, respectively; Fig. 2c, d). However, there were no significant differences in OVA-specific total IgG titers between mice immunized with pyriproxyfen and alum at Weeks 7 or 8. The observation that OVA with alum-immunized mice, the positive controls, showed significant enhancement of the total IgG immune response (Fig. 2c, d) confirms the accuracy of these experiments. Therefore, these observations suggest that pyriproxyfen enhances the total IgG immune response. A dose–response assay was performed to further characterize enhancement of the total IgG immune response by pyriproxyfen. Groups of six mice were immunized on Weeks 0, 3 and 6 with OVA in 5% ethanol, with or without alum, or increasing concentrations of pyriproxyfen (3, 9 and 15 mM), and blood samples were collected on Week 8 and subjected to ELISA to detect OVA-specific total IgG immune responses in sera.

A 33-year-old man was admitted for an episode biopsy; he had a serum creatinine (S-Cr) level of 5.7 mg/dL 1 year following primary kidney transplantation. Histological features included two distinct entities: (1) a focal, aggressive tubulointerstitial inflammatory cell (predominantly plasma cells) infiltration with moderate tubulitis; and (2) inflammatory cell infiltration (including neutrophils) in peritubular capillaries. Substantial laboratory examination showed that the patient had donor-specific antibodies for DQ4 and DQ6. Considering both the histological and laboratory findings, we diagnosed him with plasma cell-rich rejection accompanied by acute antibody-mediated rejection.

We started 3 days of consecutive steroid pulse Palbociclib mw therapy three times every 2 weeks for the former and plasma exchange with intravenous immunoglobulin (IVIG) for the latter Kinase Inhibitor Library manufacturer histological feature. One month after treatment, a second allograft biopsy showed excellent responses to treatment for plasma cell-rich rejection, but moderate, acute antibody-mediated rejection remained. Therefore, we added plasma exchange with IVIG again. After

treatment, allograft function was stable, with an S-Cr level of 2.8 mg/dL. This case report demonstrates the difficulty of the diagnosis of, and treatment for, plasma cell-rich rejection accompanied by acute antibody-mediated rejection in a patient with ABO-incompatible kidney transplantation. We also include a review of the related literature. Both plasma cell-rich rejection (PCAR) and acute antibody-mediated rejection (AMR) remain refractory rejection entities in spite of the recent development and establishment of immunosuppressive therapy. The former is characterized by the presence of mature plasma cells that comprise more than 10% of the inflammatory cell

infiltration in a renal allograft.[1] PCAR is a rare type of rejection noted in approximately 5–14% of patients with biopsy-proven acute rejection, but graft survival is poor and standard therapeutic options have yet to be generally established.[2] The latter is a well-recognized type of rejection that is due in large part to antibodies to human leukocyte antigen (HLA) alleles. Recent studies have focused on not only HLA-DR compatibility, Sodium butyrate but also on that of HLA-DQ, since de novo DQ donor-specific antibodies (DSAbs) are the predominant HLA class II DSAbs found after transplantation.[3] We report here a refractory case of PCAR accompanied by AMR due to de novo DQ DSAbs 1 year after ABO-incompatible, living-related kidney transplantation. A 33-year-old Japanese man was admitted to our hospital for an episode biopsy 1 year following primary kidney transplantation. He was diagnosed with IgA nephropathy at the age of 31 years and received a living-related kidney transplantation at the age of 32 from his mother. ABO blood types were incompatible, and HLA alleles were mismatched at two loci, B52 and DR8.

All patients were either untreated

or treated only with calcium channel blockers. Results: A total of 122 patients, 56 men and 66 women, with EH were enrolled in this study. The average age was 56 ± 12 years old, systolic blood pressure was 144 ± 16 mmHg, HbA1c was 5.6 ± 0.6%, eGFR was 76.9 ± 20.2 ml/min/1.73 m2, serum s(P)RR level was 19.0 ± 4.9 ng/ml, serum prorenin level was 1.27 ± 3.47 ng/ml, PRA was 1.24 ± 1.30 ng/ml/h, and PAC was 141.6 ± 76.9 pg/ml. Single regression analysis showed that eGFR was negatively correlated with s(P)RR (r = −0.337, P < 0.001), but not with prorenin level, PRA, or PAC. Multiple regression analysis of age, systolic blood pressure, HbA1c and s(P)RR levels revealed selleck chemical that age and s(P)RR levels were negatively correlated with eGFR (P < 0.05). Conclusion: These results support the presumption that the tissue RAS is more strongly associated with Poziotinib clinical trial renal function than the circulating RAS in patients with EH. Moreover, the correlation between the tissue RAS and renal function can be independent of age, blood pressure and HbA1c. WAKUI HIROMICHI, TAMURA KOUICHI, OHSAWA MASATO, KOBAYASHI RYU, UNEDA KAZUSHI, AZUSHIMA KENGO, TOYA YOSHIYUKI, UMEMURA SATOSHI Department of Cardiorenal Medicine, Yokohama City University

Introduction: Angiotensin II (Ang II) type 1 receptor (AT1R)-associated protein (ATRAP) was identified as a specific binding protein of AT1R. We have shown that the ATRAP promotes constitutive internalization of the AT1R and may function as an endogenous inhibitor to prevent pathological activation of the tissue AT1R signaling. The present study was designed to reveal a functional role of renal tubule ATRAP, with a focus on Ang II-dependent hypertension, by employing renal tubule-dominant Farnesyltransferase ATRAP transgenic mice (ATRAP-TG) and ATRAP deficient mice (ATRAP-KO). Methods: Experiment 1: Wild-type mice (WT) and ATRAP-TG were continuously infused with Ang II and blood pressure (BP) was measured by a radiotelemetric method. Metabolic cage

analysis was performed during the Ang II infusion to evaluate sodium balance. Renal expression of the major sodium transporters was also analyzed. Experiment 2: WT and ATRAP-KO were continuously infused with Ang II. Measurement of telemetric BP, metabolic cage analysis and renal expression analysis of sodium transporters were performed as in Experiment 1. Results: While ATRAP-TG showed a pattern of renal distal tubule-dominant overexpression of ATRAP, ATRAP-KO exhibited no ATRAP expression in all tissues, including renal tubules. At baseline, the telemetric BP of either ATRAP-TG or ATRAP-KO was similar to that of WT. However, in ATRAP-TG compared with WT, the development of hypertension in response to Ang II infusion was significantly suppressed, and the extent of positive sodium balance was significantly reduced during Ang II infusion.

New investigative tools such as gene expression profiling have begun to be applied to the problem of predicting vaccine response [2]. Most of these approaches have assayed vaccine-induced changes in gene expression in the PBMC compartment, a bellwether of changes at distant vaccine sites. Two studies have shown that changes in the expression of small numbers of genes in PBMC gene expression profiles a few days after vaccination predict the subsequent magnitude of the immune response measured several weeks later [3, 4]. These studies suggest that gene expression profiles from PBMC samples in vaccinated subjects can see more provide predictors of the

vaccine response. Such approaches would be especially useful both as tools to identify new biological features associated with vaccine response, and as correlates of immunity for the development of new vaccines. However there are two significant challenges to developing gene expression based predictors of clinical outcome following vaccination. First, the extent of biological change in PBMCs caused by direct interaction with the vaccine and PBMCs would be expected to be small. Although live attenuated vaccines such as those developed against yellow fever (YF-17D) are known to replicate

systemically and induce readily detectable interferon responses [4-6], nonreplicating subunit vaccines such as those against influenza would be expected to have a much smaller effect Protein Tyrosine Kinase inhibitor on the transcriptional profile of PBMCs. Thus the selection of individual genes that are strongly associated with response to vaccination can be difficult. The second challenge is that the biological meaning of gene expression based predictors is often hard to determine [3, 4]. One reason for this is that the analytical approaches to identify predictive genes are often different from those used to discover biological mechanisms evident in gene expression data. Predictive genes are selected on statistical rather than biological grounds [7], which tends to divorce the identity of the predictive genes from an understanding

of their role in vaccine Bacterial neuraminidase biology [8]. To address these limitations, we applied an approach to developing predictors of vaccine outcome from PBMC gene expression profiles following vaccination that has been used in other domains, e.g. stratifying cancer patients, but is novel to immunology. Rather than building a predictive model based on single differentially expressed genes, we used sets of coordinately regulated, biologically informative gene sets as predictive features in individual samples [9, 10]. As a source of gene sets, we use a compendium of signatures extracted from the published literature and from expert curation [11]. These signatures represent phenotypes of defined cell states and biological perturbations, providing specific biological contexts with which to interpret the predictive models.

The collected supernatant was then recentrifuged at 8000 g for 30 mins at 4°C. The final supernatant fluid was filtered through a 0.4–l µm filter before storage at 20°C until used in infectivity experiments. Copy number of WSSV in the supernatant fluid was calculated by competitive PCR [16, 17]. Fifty microliters of supernatant fluid containing 5.5 × 104 copy number of virus was injected i.m. into the lateral area of the fourth abdominal segment of

shrimp for challenge studies. Challenge tests were conducted in triplicate (20 shrimps per experimental group in a 120 L container for each time sampled, i.e. 20 animals × four salinities × five time intervals in triplicate). F. indicus were injected i.m. with WSSV inoculums (5.5 × 104 copy number) into the ventral sinus of the cephalothorax. After injection,

the shrimp were exposed to PS-341 clinical trial 5, 15, 25 (control) and 35 g/L salinities and monitored for pathological changes and mortality. The experiment lasted 120 hrs at 28 ± 0.5°C. Shrimp injected with equal volumes of sterile saline solution and exposed to 5, 15, 25 and 35 g/L seawater served as the unchallenged controls. Twenty healthy animals were allocated to each experimental salinity group (in triplicate–20 × 3) and injected i.m. with WSSV inoculums (5.5 × 104 copy number). After injection, the animals were exposed to varying salinities of 5, 15, 25 and 35 g/L for each assay; three WSSV-injected animals were randomly sampled from each tank at 24, 48, 72, 96 and 120 hrs pi. Hemolymph (100 µL) Ribonucleotide reductase was withdrawn individually from the ventral sinus of each shrimp into a 1 mL sterile Enzalutamide purchase syringe (25 gauge) pre-filled with 0.9 mL anticoagulant solution (30 mM trisodium citrate, 0.34 M sodium chloride,

10 mM EDTA, 0.115 M glucose, pH 7.55, osmolality 780 mOsm/kg) and stored at −80°C in aliquots (100 µL tubes) until the hematological and immunological assays. For every assay, 100 µL of hemolymph (collected in triplicate) was used. Total protein, carbohydrate, and glucose concentrations were examined in the hemolymph of WSSV-infected shrimp. Total protein was measured spectrophotometrically (O.D. 595 nm) [17], total carbohydrate using the anthrone method [18], glucose by the glucose oxidase method [19] and total lipids using the procedure described by Folch et al. [20]. Hemolymph samples collected from each experimental and control group (three random shrimps per group × triplicate), were separated into aliquots and processed for assessment of selected immunological indices. THC (cells/mL) were performed using a Burker hemocytometer [21]. The hemocytes were analyzed by phase contrast microscopy and counted manually in all 25 squares (=0.1 mm3). PO activity was measured spectrophotometrically by recording the formation of dopachrome produced from L-DOPA [22]. The optical density of the shrimp’s phenoloxidase activity for all test conditions was expressed as dopachrome formation in 50 µL of hemolymph.