Of 312 patients, 176 (56.4%) were diagnosed with non-alcoholic

steatohepatitis. During a median follow-up period of 4.8 years Paclitaxel mouse (range, 0.3–15.8), six patients (1.9%) developed HCC, and 20 (6.4%) developed extrahepatic cancer. Multivariate analysis identified fibrosis stage (≥3; hazard ratio [HR], 12.3; 95% confidence interval [CI], 1.11–136.0; P = 0.041) as a predictor for HCC and type IV collagen 7s (>5 ng/mL; HR, 1.74; 95% CI, 1.08–2.79; P = 0.022) as a predictor for extrahepatic cancer. Eight patients (2.6%) died during the follow-up period. The most common cause of death was extrahepatic malignancy. None died of cardiovascular disease. Multivariate analysis identified type IV collagen 7s (>5 ng/mL; HR, 3.38; 95% CI, 1.17–9.76; P = 0.024) as a predictor for mortality. The incidence of extrahepatic cancer was higher than that of HCC. Severe

fibrosis was a predictor for HCC. Patients with NAFLD and elevated type IV collagen 7s levels are at increased risk for extrahepatic cancer and overall mortality. “
“Association between genetic variations in alcohol-related enzymes Cisplatin mw and impaired ethanol biodisposition has not been unambiguously proven, and the effect of many newly described polymorphisms remains to be explored. The aims of this study are to elucidate the influence of genetic factors in alcohol biodisposition and effects. We analyzed alcohol pharmacokinetics and biodisposition after the administration of 0.5 g/kg ethanol; we measured ethanol effects on reaction time and motor time in response find more to visual and acoustic signals, and we analyzed 13 single nucleotide polymorphism (SNPs) in the genes coding for ADH1B, ADH1C, ALDH2, and CYP2E1 in 250 healthy white individuals. Variability in ethanol pharmacokinetics and biodisposition is related to sex, with

women showing a higher area under the curve (AUC) (P = 0.002), maximum concentration (Cmax) (P < 0.001) and metabolic rate (P = 0.001). Four nonsynonymous SNPs are related to decreased alcohol metabolic rates: ADH1B rs6413413 (P = 0.012), ADH1C rs283413 (P < 0.001), rs1693482 (P < 0.001), and rs698 (P < 0.001). Individuals carrying diplotypes combining these mutations display statistically significant decrease in alcohol biodisposition as compared with individuals lacking these mutations. Alcohol effects displayed bimodal distribution independently of sex or pharmacokinetics. Most individuals had significant delays in reaction and motor times at alcohol blood concentrations under 500 mg/L, which are the driving limits for most countries. Conclusion: Besides the identification of new genetic factors related to alcohol biodisposition relevant to whites, this study provides unambiguous identification of diplotypes related to variability in alcohol biodisposition. (HEPATOLOGY 2010;51:491–500.) Effects of alcohol drinking vary among individuals.

It thereby enhances the self-renewal ability of EpCAM+ liver CSCs. Conversely targeting the activation of the differentiation of CDX2 and GATA6 by miR-181s can maintain EpCAM+ liver CSCs in their undifferentiated MI-503 mouse state.43,44 More recently, studies from our group have also demonstrated a similar finding, whereby liver CSCs are regulated by dysregulated miRNA expression. By comparing the miRNA profiles of CD133+ and CD133- cells isolated from HCC primary

tumors and experimental cell lines, significantly elevated miR-130b expression was identified in CD133+ liver CSCs. miR-130b was found to be preferentially expressed in CD133+ spheres derived from HCC clinical samples and in chemotherapy-treated unsorted spheres enriched for CD133. Functional studies found that miR-130b was required for self-renewal, tumorigenicity and chemoresistance. CD133- cells overexpressing miR-130b displayed enhanced proliferation, superior resistance to chemotherapeutic agents, elevated expression of stem cell-associated genes, enhanced tumorigenicity in vivo and greater potential for

self-renewal in serial passages than control cells transduced with the empty vector alone. Conversely, the antagonization of miR-130b in CD133+ cells was shown to result in the opposite effect. Furthermore, the increased amount of miR-130b paralleled a reduction in TP53INP1, a known miR-130b target. The silencing of TP53INP1 in CD133- cells enhanced both self-renewal and tumorigenicity in vivo. Thus, our findings suggested that miR-130b regulates CD133+ liver CSCs by this website silencing TP53INP1.15 In addition to resistance to chemo-

and radiation therapies, CSCs seem selleck chemicals llc to be particularly adept in stimulating angiogenesis to promote tumor growth and increase the overall tumor aggressiveness before and after therapy. In fact, recent clinical studies have shown enhanced antitumor cell effects when anti-angiogenic therapy is combined with radiation or chemotherapy, suggesting that possibly radioresistance, chemotherapy resistance and angiogenesis in CSCs work in concert to initiate tumor recurrence in advanced or aggressive tumors. Given the evidence for the CSC dependence on tumor vasculature, combining radiation therapy or chemotherapy with anti-angiogenic therapies has promise in possibly mediating targeted anti-CSC effects in the promotion of prolonged recurrence-free survival. In HCC, there are currently two original articles that have documented a link between liver CSCs and angiogenesis. The first report, by Yang et al., found that high expression levels of hepatic stem/progenitor cell biomarkers, such as cytokeratin 19, ABCG2, CD133, nestin and CD44, are related to tumor angiogenesis and are indicative of high tumor recurrence and poor prognosis of surgically resected HCC.

Conclusions: These results demonstrate a role for Pol in HBV-mediated antagonization of IFN-α signaling and provide a possible molecular mechanism

by which HBV resists the IFN therapy and maintains its persistence. (HEPATOLOGY 2013;) Chronic hepatitis B (CHB) caused by hepatitis B virus (HBV) is a serious health problem worldwide. The mechanism by which chronic infection is established and maintained is unknown but is thought to be due, in part, to a suppressed host immune response. One key component selleck compound of the host antiviral responses is the interferon (IFN) system. Viral infection of the host initiates Histone Methyltransferase inhibitor the synthesis of

type I IFNs, which consist predominantly of IFN-α and IFN-β (IFN-α/β). By binding to type I IFN receptors, IFN-α/β triggers the oligomerization and tyrosine phosphorylation of the two tyrosine kinases of the Janus family, Janus kinase 1 and tyrosine kinase 2, which in turn phosphorylate a single tyrosine residue of signal transducer and activator of transcription (STAT) 1 and 2. The activated STAT1/2 heterodimerize with interferon regulatory factor 9 (IRF9) to form the ISGF3 transcription factor complexes and then translocate into the nucleus, where they bind to the interferon-stimulated response element (ISRE) in the promoter of interferon-stimulated genes (ISGs) to initiate transcription of ISGs.1 IFN-α has been shown to inhibit HBV replication in a variety of systems. However, about 70% of CHB patients respond poorly to exogenous IFN-α treatment.2, 3 Increasing evidence suggests that HBV has developed strategies to counteract the type I IFN system, which may contribute to the ineffectiveness of IFN-α therapy.4, 5 We have shown that HBV polymerase (Pol) is able to inhibit IFN-α–induced MyD88 selleck chemical induction

and nuclear translocation of STAT1.6 Consistently, it could be demonstrated in a chimeric mice model that HBV infection reduced IFN-α–mediated ISG production and STAT1 translocation.7 However, it is still unknown whether the translocation of STAT1 is impaired in chronic hepatitis B patients as well, and the molecular mechanism by which Pol interferes with the IFN responses remains unclear. In this study, we used cell and mouse models to gain a detailed understanding of how HBV and Pol interferes with IFN-α–induced STAT activation. Furthermore, liver biopsies of CHB patients were used to obtain more information on the blockage of IFN-α–induced STAT nuclear translocation by HBV.

03; Table 3). Disease severity at entry, as assessed by the total bilirubin level, Mayo risk score, and histological stage, did not seem to considerably affect the baseline bile acid composition, although patients with a baseline total bilirubin level ≥ 0.9

mg/dL had higher values of CA (P = 0.05). In a multivariate analysis model, the only significant relationship that was revealed was between colectomy (P = 0.001), a baseline alkaline phosphatase level ≥ 4 × ULN (P = 0.05), and low levels of DCA. Figure 1 shows the posttreatment percentage of each bile acid per treatment group. No significant changes between GSK-3 inhibitor treatment groups were detected for CA, DCA, or CDCA. UDCA was significantly increased (16.86 versus 0.05 μmol/L, P < 0.0001), and the total bile acid pool was significantly expanded (17.21 versus −0.55 μmol/L, P < 0.0001) in the UDCA group versus the placebo group. LCA was also markedly increased in the UDCA group versus the placebo group (0.22 versus 0.01 μmol/L, P = 0.001). The change in LCA levels after UDCA treatment seemed to positively correlate with the change in UDCA levels (P = 0.19). The UDCA and LCA enrichment did not show any significant relationship with the selleck screening library changes in the values of liver tests

(levels of alkaline phosphatase, aspartate aminotransferase, and bilirubin and Mayo risk scores; data not shown). However, female and older patients were more likely to have a greater increase in their LCA value after UDCA treatment (Table 4). Patients who had undergone colectomy (n = 7) tended to have less LCA increase after treatment than those who had not undergone colectomy (Fig. 2). However, patients who had undergone colectomy did not have worse outcomes, regardless of the treatment group. Patients in the UDCA group who reached clinical endpoints during therapy (n = 9) tended to have higher increases in their LCA and total bile acid levels in comparison with those who did not (Fig. 3). The increase in total bile acids was almost entirely

due to enrichment with UDCA. Table 5 summarizes the range of bile acid changes in these patients. The changes were similar selleck in all patients except for one patient (patient 5), and this possibly indicated noncompliance. UDCA has shown some beneficial effects in patients with PSC.2 The inability to demonstrate slowing of disease progression has resulted over the last decade in several studies designed to explore the effectiveness of different UDCA doses.3-6 In the most recent study, high-dose (28-30 mg/kg/day) UDCA treatment was associated with increased rates of serious adverse events without any obvious explanation.7 Modification of the bile acid composition has been speculated to potentially underlie the effects of the drug. In our present study, we investigated the serum bile acid composition in PSC patients under high-dose UDCA treatment. At the baseline, the primary bile acids CA and CDCA predominated.

PPRE sites in the rat MAT2A promoter were mutated using the QuikChange Lightning Site-Directed Mutagenesis Kit (Stratagene, La Jolla, CA). Primers were designed according to the kit, and three to four mutations were introduced in each PPRE site. Deletion mutants were generated

by PCR-amplifying each PPRE region (primers in Supporting Table 1) and placing it 5′ of the basal MAT2A fragment (b2A) cloned in pGL3-Basic. Nuclear extracts were prepared according to the NE-PER nuclear and cytoplasmic extraction protocol (Thermo Scientific, Rockford, IL). Extracts were subjected to electrophoretic mobility-shift assay (EMSA) and supershift (3 μg antibody) using the LightShift Chemiluminescent EMSA Kit protocol (Thermo Scientific) and probes described in Supporting KU-60019 cell line Table 2. Data are represented as the mean ± SE. Statistical analysis was performed using analysis of variance followed by Student t test. Significance was defined as P < 0.05. A 2.2-kb region of the rat MAT2A promoter has been previously cloned, and its sequence has been analyzed by Hiroki et al.19 The first 73 bp of this promoter include a canonical TATA box and a GC-rich element that confers constitutive transcription to this promoter in different cell types.19 Using the transcription element search

system and MATInspector analysis tools, we identified several PPREs in the MAT2A promoter spanning a 7-kb region upstream of the +1 transcription start site. Four distal PPREs were identified 5-7 kb upstream of the +1 GDC-0980 site. Six PPRE elements were identified in the proximal MAT2A promoter within a 2,061-bp region upstream of the +1 selleckchem transcription start site (Table 1). Good matches to the matrix had a similarity score of 0.8 or

more (Table 1). The distal PPRE sites of MAT2A had a matrix score <0.8 and did not qualify for this study. The scores of the proximal PPRE elements in the 2.2-kb region were >0.8 and provided the rationale for examining this region for functional regulation by PPARs. It is known that RSG induces the activity and expression of PPARγ, a marker of quiescent HSCs.7, 23 PPARγ expression was induced in BSC cells after RSG treatment (Fig. 1B), confirming previous findings. RSG treatment of BSC cells also induced other markers of differentiation such as C/EBPβ (Fig. 1B). RSG inhibited the expression of MAT2A messenger RNA (mRNA) and protein by 2.5-fold and 1.6-fold, respectively (Fig. 1A,B) and reduced MAT2A promoter activity by 1.6-fold compared with control cells (Fig. 1C). RSG treatment of primary rat HSCs also reduced the promoter activity of MAT2A (Fig. 1D), confirming the cell line results. RSG induced PPARγ binding on PPRE sites 1, 2, 4, 5, and 6 compared with that of control (Fig. 2A,B). No binding was observed with PPRE-3 (data not shown).

PPRE sites in the rat MAT2A promoter were mutated using the QuikChange Lightning Site-Directed Mutagenesis Kit (Stratagene, La Jolla, CA). Primers were designed according to the kit, and three to four mutations were introduced in each PPRE site. Deletion mutants were generated

by PCR-amplifying each PPRE region (primers in Supporting Table 1) and placing it 5′ of the basal MAT2A fragment (b2A) cloned in pGL3-Basic. Nuclear extracts were prepared according to the NE-PER nuclear and cytoplasmic extraction protocol (Thermo Scientific, Rockford, IL). Extracts were subjected to electrophoretic mobility-shift assay (EMSA) and supershift (3 μg antibody) using the LightShift Chemiluminescent EMSA Kit protocol (Thermo Scientific) and probes described in Supporting C59 wnt price Table 2. Data are represented as the mean ± SE. Statistical analysis was performed using analysis of variance followed by Student t test. Significance was defined as P < 0.05. A 2.2-kb region of the rat MAT2A promoter has been previously cloned, and its sequence has been analyzed by Hiroki et al.19 The first 73 bp of this promoter include a canonical TATA box and a GC-rich element that confers constitutive transcription to this promoter in different cell types.19 Using the transcription element search

system and MATInspector analysis tools, we identified several PPREs in the MAT2A promoter spanning a 7-kb region upstream of the +1 transcription start site. Four distal PPREs were identified 5-7 kb upstream of the +1 SCH772984 ic50 site. Six PPRE elements were identified in the proximal MAT2A promoter within a 2,061-bp region upstream of the +1 selleck kinase inhibitor transcription start site (Table 1). Good matches to the matrix had a similarity score of 0.8 or

more (Table 1). The distal PPRE sites of MAT2A had a matrix score <0.8 and did not qualify for this study. The scores of the proximal PPRE elements in the 2.2-kb region were >0.8 and provided the rationale for examining this region for functional regulation by PPARs. It is known that RSG induces the activity and expression of PPARγ, a marker of quiescent HSCs.7, 23 PPARγ expression was induced in BSC cells after RSG treatment (Fig. 1B), confirming previous findings. RSG treatment of BSC cells also induced other markers of differentiation such as C/EBPβ (Fig. 1B). RSG inhibited the expression of MAT2A messenger RNA (mRNA) and protein by 2.5-fold and 1.6-fold, respectively (Fig. 1A,B) and reduced MAT2A promoter activity by 1.6-fold compared with control cells (Fig. 1C). RSG treatment of primary rat HSCs also reduced the promoter activity of MAT2A (Fig. 1D), confirming the cell line results. RSG induced PPARγ binding on PPRE sites 1, 2, 4, 5, and 6 compared with that of control (Fig. 2A,B). No binding was observed with PPRE-3 (data not shown).

1, Table 1). Intracellular macroscopic lipid according to fat score increased in both ethanol-fed groups (Table 1). There were nonsignificant increases in inflammatory cells and necrosis in the heterozygote ethanol-fed group and no fibrosis in any mice. TUNEL assay revealed increased hepatocellular apoptosis in both genotype and ethanol feeding, with additive effects in the Het-E group (Table 1). Liver GSH, a measure of antioxidant defense capacity, was reduced in the heterozygous control and in both ethanol-fed

groups, with additive effects of ethanol feeding and genotype in the Het-E group (Table selleck chemical 1). There were no differences among the groups in liver homocysteine levels. Liver SAM was reduced and SAH was elevated in both

ethanol-fed groups, with an additive effect of genotype on SAH in the Het-E group. The SAM/SAH ratio of methylation capacity decreased in both ethanol fed groups, with interactive effects of genotype and ethanol in the Het-E group. The SAM/SAH ratio correlated negatively with the total pathology score (r = −0.57, P < 0.006) and TUNEL score (r = −0.52, P < 0.01). Scatter plots of these GSK3 inhibitor and subsequent regression analyses are shown in Supporting Figs. 1–5. ER chaperone GRP78 messenger RNA (mRNA) (Table 2) and its protein levels (Fig. 2A) increased in both ethanol-fed groups, with an interaction of genotype and ethanol on protein levels in the Het-E group. Protein levels of the ER stress transducer ATF4 increased in both ethanol groups with greatest and interactive selleck effects in the Het-E group (Fig. 2B). Activated ER stress transducer ATF6 increased by genotype and maximally in the Het-E group (Fig. 3C). Liver transcript levels of the pro-apoptotic

gene GADD153 increased in both ethanol-fed groups (Table 2), while protein expression rose with both genotype and ethanol feeding, with interactive effects in the Het-E group (Fig. 2D). Cleaved caspase 12, a protease that plays a central role in initiating ER stress-induced apoptosis, increased in both groups of ethanol-fed mice (Fig. 2E). Transcript and protein levels of SREBP-1c increased in both ethanol-fed groups, with additive and interactive effects of both treatments on mRNA expression in the Het-E group (Table 2, Fig. 2F). Ethanol feeding increased SREBP-1c targeted transcripts of acetyl-coenzyme A carboxylase, with interactive effects in the Het-E group, while fatty acid synthase expression rose by genotype only (Table 2). The SAM/SAH ratio of methylation capacity correlated negatively with protein levels of GRP78 (r = −0.43, P < 0.04), GADD153 (r = −0.62, P < 0.002), and cleaved caspase-12 (r = −0.73, P < 0.002). The percentages of methylated cytosine were similar among all groups: 4.01% ± 0.03 in wild-type controls, 4.0% ± 0.1 in heterozygous controls, 3.8% ± 0.01 in wild-type ethanol-fed, and 3.9% ± 0.2 in Het-E mice.

Acclimation to low salinity enhanced H. akashiwo’s ability to accumulate and grow in low salinity waters. In addition, the presence of a ciliate predator altered H. akashiwo swimming behavior, promoting accumulation in low-salinity surface layers inhospitable to the ciliate.

(3) Negative effects of low salinity on predation processes. Ciliate predation rates decreased sharply at salinities <25 and, for one species, H. akashiwo toxicity increased at low salinities. Taken together, these behaviors and responses imply that blooms can readily initiate in low salinity waters where H. akashiwo would experience decreased predation pressure while maintaining near-maximal growth rates. The salinity structure of a typical estuary would provide this HAB species a unique refuge from predation. Broad salinity tolerance in raphidophytes may have evolved in AZD0530 part as a response to selective pressures associated with predation. “
“Reactive oxygen species (ROS) are commonly produced by algal, vascular plant, and animal cells involved in the innate immune response as cellular signals promoting defense and healing and/or as a direct defense against invading pathogens. The production of reactive species in macroalgae upon injury, however, is largely

uncharacterized. In this study, we surveyed 13 species of macroalgae from the Western Antarctic Peninsula and show that the release of strong oxidants is common after macroalgal wounding. Most species released strong oxidants within 1 min of wounding and/or showed cellular MK0683 price accumulation of strong oxidants over an hour post-wounding. Exogenous catalase was used to show that hydrogen peroxide was a component of immediate oxidant release in one of five species, but was not responsible for the entire oxidative wound response as is common in vascular plants. The other component(s) of the oxidant cocktail released upon wounding are unknown. We were unable to detect protein nitration selleck chemical in extracts of four oxidant-producing species flash frozen

30 s after wounding, but a role for reactive nitrogen species such as peroxynitrite cannot be completely ruled out. Two species showed evidence for the production of a catalase-activated oxidant, a mechanism previously known only from the laboratory and from the synthetic drug isoniazid used to kill the human pathogen Mycobacterium tuberculosis. The rhodophyte Palmaria decipiens, which released strong oxidants after wounding, also produced strong oxidants upon grazing by a sympatric amphipod, suggesting that oxidants are involved in the response to grazing. ROS are the unstable partial reduction products of stable molecular oxygen (O2). ROS include molecules like superoxide (O2−), hydrogen peroxide (H2O2), and the hydroxyl radical (OH·), as well as reactive derivatives such as hypochlorite (ClO−) and the peroxyl radical (ROO·, Halliwell and Gutteridge 2007).

Imaging was performed with an Olympus microscope and analysis with the MetaMorph imaging software (Molecular Devices) in at least 3 fields per slide. Nuclear phospho-ERK expression was expressed as pERK-positive nuclei/total nuclei/mm2.

Thirty mg of frozen liver tissues was weighed and lysed in 300 μL HEPES buffer (20 mM HEPES, pH 7.4; 1.5 mM EDTA; 0.5 mM PMSF; 1× protease inhibitor mix [complete mini tablets, Roche]; 1× phosphatase inhibitor [PhosStop, Roche]). Homogenate was collected after homogenization and centrifugation at 14,000 rpm for 10 minutes at 4°C. Protein concentration was measured according to Lowry et al.14 The amount of

VEGF-A, PDGF-BB, and hepatocyte growth factor (HGF) present in whole liver protein extracts were measured Pembrolizumab datasheet using ELISA assays (VEGF-A, PDGF-BB measured with Quantikine immunoassay, R&D; HGF measured with RayBio ELISA Kit, RayBiotech) following the manufacturer’s instructions. Protein concentration of each liver homogenate was used to normalize the hepatic VEGF-A, PDGF-BB, and HGF levels. Scar tissue of the peritoneal and muscular abdominal this website wall were collected at harvest and embedded in paraffin. Tissue was stained with the chromotrope-aniline click here blue method (CAB trichromic assay).15 Microscopic evaluation was performed with an Olympus microscope by a blinded investigator. In order to evaluate wound healing in the different treatment groups, the scar margins of the abdominal wall were assessed for bridging reactions. Both the 72-hour and the 120-hour timepoints were studied. Bridging reactions were defined as loci where inflammatory cells transvade the thin layer of collagen formed on the cut edge, participating in the granulation tissue that fills the wound cleft, and eventually linking up

opposite scar margins. Data were analyzed with GraphPad Prism 4.0 software. Kruskal-Wallis and the Mann-Whitney test assessed the statistical significance of differences between mean values; P less than 0.05 was considered significant. Mice which were treated with sorafenib for 14 days and stopped treatment 1 day before partial hepatectomy showed no impairment in liver regeneration when compared to the control group that received the vehicle only (Figs. 1, 2A). In contrast, the animals receiving continuous sorafenib treatment presented significantly lower liver mass restoration at 120 hours in comparison to the animals treated with the vehicle (72% ± 12% versus vehicle 88% ± 15%, P < 0.02).

early endoscopy Presenting Author: HIROSHI KANIE Additional Authors: SATOSHI NOMURA, ISSEI KOJIMA, YU NOJIRI, TAKASHI YOSHIMINE, YASUAKI FUJITA, ATSUNORI KUSAKABE, TESSHIN BAN, TOMONORI YAMADA, KATSUMI HAYASHI, ETSURO ORITO Corresponding Author: HIROSHI KANIE Affiliations: Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini Red Cross Hospital, Nagoya Daini lambrolizumab Red Cross Hospital Objective: In July

2012, the Japan Gastroenterological Endoscopy Society (JSGE) published guidelines for gastroenterological endoscopy in patients undergoing antithrombotic treatment. (Digestive endoscopy 2014;26:1–14) The new edition of the guidelines (GL) includes discussions of gastroenterological hemorrhage associated with continuation of antithrombotic therapy, as well as thromboembolism associated with withdrawal of antithrombotic therapy. The aim

of this study is to clarify postoperative hemorrhage undergoing antithrombotic treatment. Methods: In a retrospective review of our database prospectively collected data between July 2011 and June 2013 (two years), we resected endoscopically colorectal tumors, total 1175 cases 2198 lesions. We compared the rate of postoperative hemorrhage between endoscopic treatment within the new guidelines (New GL group: 164 Selleckchem LEE011 learn more lesions),and within the old guidelines (Old GL group: 199 lesions),and undergoing no antithrombotic therapy (No medication group: 1834 lesions). We evaluated for risk factor of postoperative hemorrhage

after endoscopic treatment of colorectal tumors. Results: The lesions undergoing antithrombotic treatment were 363 lesions (16.6%). The rate of postoperative hemorrhage was 1.8%(3/164) in New GL group, 1.5%(3/199) in Old GL group, 0.60%(11/1834) in No medication group, and there were no significant defference. It was 1.4%(1/73) in continuation of aspirin, 0.8%(1/128) in withdrawal of aspirin, and there were no significant defference. The risk factor of postoperative hemorrhage was location (rectum), size (over 10 mm), pathological finding (cancer) and antithrombotic therapy (+) by univariate analysis. The significant independent risk factor of postoperative hemorrhage was size (odd ratio 14.80[95 % CI 3.22–67.96], p = 0.001), location(odd ratio 3.46[95 % CI 1.25–9.61], p = 0.017) and antithrombotic therapy(odd ratio2.96[95 % CI 1.07–8.21], p = 0.037) by multivariate analysis. Conclusion: The rate of postoperative hemorrhage is not increased by compliance of new guidelines, and it is reasonable to observe the new guidelines. Key Word(s): 1. postoperative hemorrhage; 2. antithrombotic treatment; 3.