[32] To address this question, we examined the

modulatory effects of CH5424802 clinical trial rHp-CPI on the differentiation of DC from BM precursors. Bone marrow cells were cultured in the presence of GM-CSF to induce DC differentiation and, in one group of cultures, rHp-CPI (50 μg/ml) was added on day 3 of culture. The two groups of BMDC were harvested on day 9 and analysed for cell surface co-stimulatory molecule expression by flow cytometry. Addition of rHp-CPI did not show apparent effects on the yield of BMDC (medium control group, 7·8 ± 1·0 × 106 total cells/plate, 79·1 ± 5·1% CD11c+ DC; rHp-CPI-treated group, 6·9 ± 1·2 × 106 total cells/plate, 74·7 ± 8·2% CD11c+ DC). We observed that, although the control and rHp-CPI-treated DC did not show significant differences in frequencies of CD40+, CD80+ and CD86+ cells in total CD11c+ DC and expression level (mean fluorescence intensity, MFI) of these co-stimulatory molecules, the BMDC that were exposed to rHp-CPI on day 3 of culture

showed reduced expression of the MHC-II molecule by 48% (Fig. 3). The DC that were exposed to rHp-CPI starting on days 5 and 7 of culture also showed reductions in MHC-II molecules by 37% and 14%, respectively, in comparison with the control DC (data not shown). To further analyse the effects of rHp-CPI on DC differentiation, bone marrow cells were cultured for 9 days with or without rHp-CPI, stimulated with the Toll-like receptor (TLR) ligands LPS and CpG and then co-stimulatory molecule expression was examined. filipin Both the control DC (cultured in medium alone) and rHp-CPI-treated EPZ-6438 in vitro DC showed increased expression of CD40 and CD86 in response to stimulation with LPS in comparison with unstimulated DC. Stimulation of control DC with CpG induced increased expression of CD40 whereas this CD40 expression response was absent in BMDC that were treated with rHp-CPI during the differentiation

stage. Similarly, LPS stimulation increased the CD86 expression in both groups of BMDC, but the rHp-CPI-treated BMDC showed significantly lower levels of CD86 expression following CpG stimulation than the control BMDC. Furthermore, BMDC that were exposed to rHp-CPI during the differentiation stage exhibited significantly decreased expression of the MHC-II molecule in response to stimulation with LPS and CpG compared with the control DC (Fig. 4a,b). The BMDC exposed to rHp-CPI also produced lower levels of IL-6, IL-12p40 and TNF-α cytokines following CpG stimulation compared with the BMDC generated in normal culture conditions (Fig. 4c). These results demonstrate that exposure of BMDC to rHp-CPI during the differentiation stage modified their ability to respond to the activation signal provided by the TLR9 ligand CpG. We next examined the modulatory effects of rHp-CPI on activation of immature BMDC.

Consistent with the flow cytometry data, there was a small amount of CD4

stored inside cells click here while a substantial amount of intracellular LAG-3 was detected (Fig. 1C and D). To exclude the possibility that this is an overexpression artifact of T-cell hybridomas, splenocytes from OTII TCR transgenic mice were stimulated with OVA326–339 peptide to induce LAG-3 expression and subjected to the same analysis. These data clearly show that a substantially greater proportion of LAG-3 is stored intracellularly, compared with CD4, in normal T cells (Fig. 1C and D). To further investigate the localization of CD4 and LAG-3 in activated CD4+ T cells, we used confocal microscopy to visualize intracellularly stored CD4 and LAG-3. CD4 were mainly expressed Ceritinib on the cell surface with only a small portion observed in intracellular locations. While LAG-3 was also expressed on the cell surface, there appeared to be substantially more LAG-3 in the small amount of T-cell cytoplasm that can be observed by confocal microscopy

(Fig. 2A and B). After pronase treatment of activated CD4 T cells, most of membrane CD4 and LAG-3 was removed and intracellular storage of CD4 and LAG-3 was observed by confocal microscopy (Fig. 2A). Importantly, Lag3−/− T cells were used to ensure Ab specificity. We next investigated the role of intracellular LAG-3 in T cells. We hypothesized that intracellular LAG-3 might facilitate its rapid translocation to the T-cell surface. We first examined the kinetics of surface LAG-3 restoration after pronase treatment. Activated T cells were treated with pronase

and surface recovery assessed by flow cytometry following incubation at different time Vorinostat points at 37°C. Surprisingly, restoration of LAG-3 cell surface expression was more rapid than CD4 (Fig. 3). One hour after pronase treatment, 30% of the starting cell surface expression of LAG-3 had been restored in contrast with 10% for CD4. For both molecules, this re-expression was partially blocked within the first hour by the protein synthesis inhibitor cycloheximide and to a slightly greater extent by the protein transport inhibitor Brefeldin A (Fig. 3). Re-expression essentially plateaus after 1 h in the presence of both inhibitors suggesting that the continued increase in LAG-3 and CD4 expression beyond the first hour is due to new protein synthesis. It is noteworthy that this plateau was higher for LAG-3 compared with CD4. In the presence of Brefeldin A for 3 h only 4% of the total surface CD4 compared with 14% of LAG-3 was restored suggesting that a greater proportion of LAG-3 was stored intracellularly, consistent with our previous observations (Fig. 3B and C). Overall, these results suggest that intracellular storage of LAG-3 facilitates its rapid translocation to the cell surface.

ITAMI NORITOMO1, UEMURA SUSUMU2, TSUNEYAMA KAZUSHI2, HAMADA HIROMI3, NAKAYAMA MASAAKI4 1Nikko Memorial Hospital, Kidney Center, Japan; 2Nikko Memorial Hospital, Dept. of Clinical Engineering, Japan; 3Nikko Memorial Hospital, Dept. of Surgery, Japan; 4Fukushima Medical University, Dept. of Nephrology, Japan Introduction: The beneficial effects of electrolyzed water hemodialysis such as a reduction in oxidative stress and inflammatory markers have been reported and improvements

in blood pressure and maintaining of cardiac function are expected. Presented is a comparative study on the cardiac function of maintenance hemodialysis patients who have undergone electrolyzed water hemodialysis for over two years. Methods: The subjects of our study were 19 maintenance hemodialysis

patients (6 male, 13 female) who had received electrolyzed water hemodialysis(EW-HD) Ruxolitinib in vivo for over two years at our hospital and in whom post-dialysis echocardiography was performed. Measured values were compared for the one year of standard hemodialysis(S-HD) prior to starting EW-HD, the first year of EW-HD(EW1st) and the second year of EW-HD(EW2nd). The measured values included: 1) Left ventricle mass index(LVMI), 2) Left ventricle ejection fraction(EF), 3) Left ventricle fractional shortening(FS), 4) Left ventricle diastolic performance(E/E’), and 5) Heart-lung ratio. Results: The values shown are the average ± standard deviation, with the critical rate calculated by Tukey’s test shown in parentheses. 1)  LVMI; S-HD: 103.0 ± 30.7 g/m2, EW1st: PF-02341066 mouse 101.3 ± 31.5 g/m2, EW2nd: 100.5 ± 28.2 g/m2 Conclusion: These results suggest the possibility that electrolyzed water hemodialysis can contribute to maintaining cardiac function in maintenance hemodialysis oxyclozanide patients. CHOI JOON SEOK1, KIM HA YEON1, OAK CHAN YOUNG1, LEE SEUNG HYOUNG1, KANG

YONG UN1, KIM CHANG SEONG1, BAE EUN HUI1, MA SEONG KWON1, KWEON SUN SEOG2, KIM SOO WAN1 1Department of Internal Medicine, Chonnam National University Medical School, Gwangju; 2Department of Preventive Medicine, Chonnam National University Medical School, Gwangju, Korea Introduction: Hyponatremia is a common electrolyte disorder associated with tumor-related conditions. However, the clinical impact of hyponatremia in patients with colorectal cancer has not been evaluated. Methods: We retrospectively assessed 2944 patients who had been admitted to Chonnam National University Hwasun Hospital with a diagnosis of colorectal cancer. In order to determine the relationship between serum sodium level and 3-year mortality, we categorized the patients according to the sodium level as having normonatremia or mild, moderate, or severe hyponatremia. Results: Hyponatremia, defined as a serum sodium level of <135 mEq/L, was evident in 27.6% of patients during hospitalization.

Each amplified DNA fragment covered the region from the 18th to 172nd of the lipase gene and that from the 541st to 711th of the 16S rRNA

gene, respectively. The annealing temperature of the oligonucletotides for lipase gene is 55°C and that for 16S rRNA is 51°C. The thermal protocol was 95°C for Rapamycin solubility dmso 3  min and then 35 cycles of 95°C for 10  sec and the annealing temperature indicated above for  30 sec and 72°C for 30  sec. Fluorescence was measured at the end of the 72°C step during every cycle. As a control, a reaction mixture without reverse transcriptase was prepared using same protocol. The threshold for fluorescence was properly positioned according to the manufacture’s ABT-199 datasheet protocol, and the number of cycles at which fluorescence reached the threshold line was determined. The relative transcriptional level of lipase gene was calculated according to the formula of the ΔΔCt method (26). In order

to comprehensively examine the effect of NaCl on production of extracellular proteins, we cultured two strains, wild-type strain (A. sobria 288 [asp+, amp+]) and two protease gene-deleted mutant strains (A. sobria 288 [asp−, amp−]), in NB (0.5) and NB (3.0) at 37°C for 24  hrs with shaking. We treated these culture supernatants with TCA, and collected and separated the precipitates yielded by SDS-PAGE as described in Materials and Methods. The results are shown in Figure 1. We applied samples of the wild-type strain, which we prepared by culturing in NB (0.5) and NB (3.0), to lanes 1 and 2, respectively. Compared with lane 2, the number of protein bands in lane 1 was small and their density low. We believe that both ASP and AMP were

produced in the wild type culture supernatant in NB (0.5) and that almost all proteins released into the culture supernatant were decomposed by these proteases. In contrast, we prepared the sample for lane 2 from the culture supernatant in NB (3.0). In NB (3.0), production of ASP and see more AMP is repressed (8, 17). Therefore, many proteins in the culture supernatant were not attacked by these proteases. Thus, the number of bands was large and their densities high in lane 2. The above results show that the protease activity of the culture supernatant strongly influences the appearance of protein in it. It is important to eliminate the influence of proteases when analyzing exoproteins released into the milieu from bacteria. We therefore analyzed the exoproteins of a two protease gene-deleted mutant strain (A. sobria 288 [asp−, amp−]).

Swine MHC, also termed swine leukocyte antigen (SLA), was discovered by Vaiman in 1970 (3). The SLA cluster of genes is divided Selinexor order into three groups of linked genes: SLA class I (SLA-I), SLA class II (SLA-II) and SLA class III (SLA-III). SLA-I has three functional loci: SLA-1, SLA-2 and SLA-3 (4,5). Among these, the SLA-2 locus is easily distinguished

from SLA-1 and SLA-3 by the longer signal peptide than the others. A further dissimilarity to the SLA-1 and SLA-3 loci is in three amino acid residues at the start of the signal peptide (6). The SLA-2 locus might have a more crucial role as an SLA-I molecule (the roles of which include binding and presenting antigen molecules) because it is more polymorphic than the other two SLA-I loci (5,7,8). The Hebao pig is a unique breed reared in China. To study its genetic characteristics, a cloning scheme for Hebao pig SLA-2 was designed and its molecular evolution was analyzed. Hebao pigs were bred on a farm belonging to the Institute of Animal Husbandry of Liaoning Province in China. Fresh spleen tissues were removed from four

pigs for analysis. pMD18-T easy vector, Escherichia coli JM109, avian myeloblastosis virus (AMV) reverse transcriptase, isopropyl β-D-1-thiogalactopyranoside (IPTG), 5-bromo-4-chloro-3-indolyl β-D-galactopyranoside (X-gal), T4 DNA Ligase and EcoR I restriction endonuclease were purchased from Takara Biotechnology

(Dalian, China). The TRIzol Total RNA Extraction Kit was purchased from selleck Invitrogen (Carlsbad, CA, USA). The GeneClean kit was purchased from BIO 101 (Vista, CA, USA). To amplify the SLA-2 gene from Hebao pig, a pair of primers was used as follows: S1, 5’-AGATGCGGGTCAGGGGCCCTCAAG-3’ (located at sites 24–47 in AF464049); S2, 5’ -CAGTCCCCACAAGGCAGCTGTCTC-3’. (complementary at sites 1119–1142 in AF464049), then, spleens were removed from four slaughtered Hebao pigs. One hundred milligrams of tissue was cut into aminophylline pieces and placed in 1.5-mL Eppendorf tubes to which was added 300 μL TRIzol reagent (Invitrogen). Total RNA was extracted from spleen tissues using TRIzol reagent per the manufacturer’s recommendations and the isolated RNA samples were stored at –80° until use for RT-PCR. RT-PCR was carried out according to Gao et al. (9). The PCR products were stored at –20°C for gene cloning. The PCR products were separated on a 1% agarose gel by 1× Tris-acetate-EDTA running buffer electrophoresis. The separated DNA was purified using a DNA recovery kit, and then the purified DNA was ligated to pMD 18-T easy vector according to the manufacturer’s recommendations. The mixture was incubated at 4°C overnight, and then transformed into competent E. coli JM109 coated on LB plates containing ampicillin (100 μg/mL), IPTG (40 μg/mL) and X-gal (200 μg/mL).

“
“Targeted gene disruption experiments in Trichophyton mentagrophytes are impeded by the dominant of repair of DNA double strand breaks Sunitinib order through a nonhomologous end joining pathway (NHEJ). Inactivation of human DNA ligase IV homologs, which is involved in the final step of the NHEJ pathway, has been shown to enhance homologous recombination (HR) frequency in filamentous fungi. To improve the frequency of HR in T. mentagrophytes, the lig4 homolog (TmLIG4) was disrupted. T. mentagrophytes lacking TmLIG4 showed no discernable phenotypic differences when compared to wild-type controls. Both mutant and parent

strains had almost identical growth ability, sporulation rate and sensitivity to DNA damaging agents. When four different loci were disrupted in the TMLIG4-deficient mutant, HR frequencies reached as high

as 93% depending on the locus, whereas they ranged from 0%–40% in the wild-type. These results suggest that studies in strains lacking TmLIG4 would help to improve our understanding of dermatophytosis by facilitating this website the genetic manipulation of dermatophytes. Trichophyton mentagrophytes is a member of a group of closely related superficial fungal pathogens that invade the outermost layer of skin, hair and nails in humans and animals causing superficial mycoses (so-called dermatophytoses) (1, 2). These specialized fungi are characterized by their ability to degrade keratinous tissue through a wide range of secreted endo- and exo-proteases, and are therefore of pathogenic importance (3). Understanding

the mechanism of protease secretion and relevant factors at the molecular level is a key approach towards elimination of dermatophytosis. Therefore, establishment of high-throughput molecular genetic approaches is the cornerstone of dermatophyte studies. Targeted gene disruption by homologous recombination is often carried out in fungal molecular genetic studies. However, DSBR in fungi takes place either through HR, requiring homologous sequences, MRIP or NHEJ (4). Unlike some yeasts (5, 6), fungi appear to favor NHEJ over HR, resulting in decreased gene targeting efficiency and making precise genetic manipulation laborious and time-consuming. In yeasts, the role of the RAD52 gene group in HR has been characterized, mainly been based on Saccharomyces cerevisiae, which possesses very efficient HR machinery(7). Accordingly, two approaches can be anticipated to improve fungal gene disruption efficiency: enhancing HR or impairing NHEJ. In several fungi the feasibility of the latter approach has been shown to be advantageous, through production of recipient cells lacking some of the NHEJ-related genes.

The construct was transformed into BL21 E.coli strains and protein expression induced by 1 mM isopropylthio-β-galactoside (Takara, Shiga, Japan) as a recombinant protein. Expression of the protein was induced in E. coli, the bacteria sonicated, and the supernatant separated from the pellet. Next, affinity purification was performed in order to obtain MPB64 as a polyhistidine tag fusion protein. After 6 M guanidine hydrochloride had been added to E. coli to denature proteins, the supernatant

was collected for adsorption to magnetic beads. Then elution buffer was added and samples collected as a purified fusion recombinant protein. The reactivity of serum samples from the patients with active TB was examined by western blotting. Samples were loaded onto 15% gels that were run at 36A for see more 60 mins. Following electrophoresis, one of the gels was stained with Coomassie brilliant blue. Nitrocellulose membrane, Hybond C extra (GE Healthcare, Piscataway, NJ, USA), was pre-soaked in 25 mM Tris containing 5% MeOH. The transfer stack was assembled in the following order: filter paper (pre-soaked in 0.3 M Tris containing

5% MeOH), gel, filter paper (pre-soaked in 25 mM Tris containing 5% MeOH), and another layer of filter paper (pre-soaked in 25 mM Tris containing 5% MeOH and 40 mM 6-aminohexanoic acid). Western blotting was performed at 144 A for 90 mins. Next, the membranes Midostaurin ic50 were washed twice many with TBST for 5 mins. After blocking, the membranes were again washed with TBST and then incubated with the primary antibody (serum samples from five patients diluted 1000-fold with TBST) at room temperature for 1 hr with shaking. After washing three times with TBST, the membranes were incubated with the secondary antibody (anti-human IgG/HRP) diluted 1000-fold with TBST) for 1 hr at room temperature with shaking. After washing three times with TBST, color was developed

by using a Protein Detector Western Blot Kit TMB system (KPL, Gaithersburg, MD, USA). Purified MPB64 antigen was diluted with 8 M urea (0.2 M Tris, pH 8.5) and dispensed to a nitrocellulose membrane, Hybond C extra (GE Healthcare), at 50 μL/well using Bio-Dot (catalog No.170–6545, Bio Rad Laboratories, Hercules, CA, USA). After vacuum suctioning for 5 mins, the membranes were incubated for 1 hr at room temperature in Block Ace (40 mg/mL, AbD Serotec, Raleigh, NC, USA) with shaking for the blocking. To each 10 μL aliquot of serum, 490 μL of TBST and 20 μL of E. coli lysate were added with shaking to block nonspecific binding. After blocking, the serum was diluted 400-fold with TBST and the membranes incubated in the serum for 1 hr at room temperature with shaking to allow reaction with the primary antibody.

Another, unique feature is their capability to prime naive

T cells and direct the nature of T cell responses. Fulfilling these different tasks, several DC subtypes can act either as ‘good guys’ or as ‘bad guys’ in allergic immune responses. Human DCs can be subdivided into two major subtypes, myeloid DCs (MDCs) and plasmacytoid DCs (PDCs). MDCs are localized in the peripheral tissue, the blood or secondary lymphoid Talazoparib organs [2]. PDCs can be detected in the blood and lymphoid organs and are characterized by expression of the α-chain of the interleukin (IL)-3 receptor (CD123) and the blood-derived DC antigen (BDCA)-2. They are interferon (IFN)-producing cells recognizing viral antigens by Toll-like receptor (TLR)-7 and TLR-9 [2]. Variations of the DC character depend upon the subtype of DCs, the microenvironment, the quantitative and qualitative nature of other DC subtypes and cells in the environment and their cross-talk and interaction with DCs, the maturation stage buy HKI-272 of DCs, pattern of surface receptors, etc. Having these

many-sided properties of DCs in mind it is important to understand, in as detailed a manner as possible, how DCs manage to induce or accelerate allergic immune responses as well as which qualities enable them to attenuate or prevent allergic inflammation or, moreover, promote the development of allergen-specific tolerance. One of the most impressive examples for these variations are DCs which express the high-affinity receptor for immunoglobulin (Ig)E (FcεRI). Depending upon the context, i.e. cell type and location of FcεRI-bearing DCs, allergic immune responses can be promoted such as in atopic dermatitis (AD) [3], prevented, as thought for FcεRIpos oral mucosal DCs during sublingual immunotherapy [4], or functions involved in virus defence may be altered, as observed for FcεRIpos PDCs [5]. In this work we summarize the versatile character of FcεRIpos human DCs exemplified in the context of allergic immune reactions. Epidermal DCs, which comprise about 2–5% of all epidermal cells, belong in non-inflamed skin mainly to the classical Langerhans

cells (LCs) which are characterized by the Amylase so-called Birbeck granules, visible by electron microscopy as tennis racquet-shaped vesicles. The Birbeck granules are thought to be connected to the C-type lectin Langerin expressed by these cells and involved in antigen presentation [6]. LCs are derived from monocytes as their direct precursors and are localized in the basal and suprabasal layers of the upper epidermis, where they reside in an immature state without renewal for months [7]. Transforming growth factor (TGF)-β is required for their differentiation [8]. In healthy, non-inflamed skin, LCs represent the only epidermal DC type. To some extent, LCs are believed to be able to maintain a state of tolerance in the skin [9].

The apoptotic cells are rapidly engulfed and digested by phagocytes such as macrophages and immature dendritic cells. The swift engulfment of cell corpses by phagocytes prevents the release of noxious or immunogenic debris from dying cells into the circulation. In the process of apoptosis, the dying cells expose phosphatidylserine on their external membrane in a caspase-dependent manner. This externalization of phosphatidylserine is one of the hallmarks of apoptosis and acts as an “eat me” signal for phagocytes Protein Tyrosine Kinase inhibitor 3. Recently, several molecules

that recognize phosphatidylserine have been identified 4–7. Systemic lupus erythematosus (SLE) is a chronic autoimmune disease caused by multiple genetic and environmental factors 8. Patients with SLE develop a broad spectrum of clinical manifestations affecting the skin, kidney, lungs, blood vessels, and/or nervous system. SLE is also characterized by the presence in sera of autoantibodies against nuclear components (anti-RNP

and anti-DNA antibodies). Unengulfed apoptotic cells can be found in the germinal centers of the lymph nodes of some SLE patients, and macrophages from these patients show a reduced ability to engulf apoptotic cells 9. Furthermore, circulating DNA or nucleosomes can also be found in the sera of SLE patients 10, 11. These results suggest that a deficiency in the clearance of apoptotic cells is one of the causes of SLE. Milk fat globule-EGF factor 8 (MFG-E8) is a glycoprotein. At the N-terminus, it has a EGF-like Selleckchem Acalabrutinib repeat(s), and at the C-terminus, there are two discoidin domains that bind phosphatidylserine. It was originally identified as a component of milk fat globules that bud from the mammary epithelia during lactation. But it is now known to play

important roles in various systems such as involution of mammary glands, adhesion between sperm and egg, repair of intestinal mucosa, and angiogenesis 12. MFG-E8 is secreted by activated macrophages and immature dendritic cells 13, and it promotes the engulfment of apoptotic cells by working as a bridging molecule between apoptotic cells and phagocytes 7. In MFG-E8-knockout mice, many apoptotic ADP ribosylation factor cells are left unengulfed in the germinal centers of the spleen 14. The MFG-E8−/− mice produce autoantibodies including anti-cardiolipin and anti-dsDNA antibodies and suffer from an SLE-type autoimmune disease. Human MFG-E8 is maintained at the optimal concentration to support the engulfment of apoptotic cells; in excess, MFG-E8 inhibits phagocytosis and causes autoimmune diseases 15, 16. In this report, we analyzed the human MFG-E8 gene of SLE patients, and found in two female patients an intronic mutation that caused aberrant splicing of intron 6, resulting in the inclusion of a cryptic exon in the transcript.

Thirty patients (35%) had postoperative complications, and 16 patients (19%) had a salivary fistula. The flaps used were: 39 fibula (45%), 25 radial forearm (29%), eight anterolateral thigh (9%), eight rectus abdominus

(9%), three scapula (4%), and three iliac crest (4%). The average length of bone used was 9 cm (range 5–16 cm). The average soft tissue area was 99.7 cm2 (range 24–300 cm2). Nine patients (10%) had either partial or total flap loss. The lower lip-split procedure for surgical exposure is unnecessary for both oncologic resection and reconstruction for locally advanced oral cancers. Clear margins, relatively facile flap inset with high success rates, and acceptable complication BMS-907351 rates can be safely achieved in this patient population. © 2011 Wiley-Liss, Inc. Microsurgery 2011. “
“Few evidence-based and detailed algorithms exist on the

management of failing breast free flaps, including use of the numerous salvage tools that are available. The purpose of this study was to analyze our outcomes with an algorithmic approach to breast free flap salvage after vascular compromise. A review of the literature is also presented. A retrospective review of all breast free flaps performed at our institution between 2007 and 2012 was performed. Flaps with intraoperative and postoperative vascular complications were analyzed. A Afatinib chemical structure total of 612 microsurgical breast reconstructions in 442 patients were reviewed. Of these, 72 (11.8%) flaps had intraoperative vascular complications, and 36 (5.9%) had postoperative vascular complications. The total flap loss rate was 2.8%. The most commonly used salvage modalities were anastomotic revision (72%), heparin irrigation (72%), systemic heparin (37%), Fogarty catheter thrombectomy (17.6%), thrombolytics

Adenosine (13%), and indocyanine green angiography (10.2%). In 53 (49.1%) cases, flap salvage involved use of 1 modality, whereas in 55 (50.9%) cases multiple modalities were used. Factors associated with failure of these flap salvage tools included intraoperative arterial rather than postoperative arterial compromise (P = 0.01), and situations requiring use of a greater number of salvage modalities (P < 0.001). We found that intraoperative compromise had significantly better prognosis than postoperative compromise. By organizing the numerous salvage modalities available to microsurgeons into a well-defined algorithm that is supported by the literature, we have established a best practices protocol that has achieved flap salvage rates that compare favorably to the published literature. © 2013 Wiley Periodicals, Inc. Microsurgery 33:505–513, 2013. "
“Orbital exenteration (OE) is a disfiguring procedure, which typically includes the removal of the entire eyeball including the globe, extraocular muscles, and periorbital soft tissues after malignancies excision or trauma.