Similar results were obtained for NS5A by western blotting (Supporting Fig. 3). All together, these data show that EGCG does not inhibit viral replication or virion assembly and egress. Because EGCG has an antiviral activity at an early step of the HCV life cycle, we further investigated its mode of action on HCV entry. To test whether EGCG would act on the viral particle or on the target cells, HCVcc was preincubated with EGCG before contact with target cells. Tyrosine Kinase Inhibitor Library chemical structure In these conditions, EGCG should have a higher inhibitory effect, especially if it acts on the viral particle. In contrast, the antiviral action of EGCG should not be modified if EGCG acts

on the cell. Preincubation of the virus with 50 μM of EGCG, followed by a dilution to 5 μM during infection, led to a stronger inhibition of infection than the one observed with the same concentration of EGCG during the inoculation, with no preincubation (Fig. 5A). Together with the inhibition of HCVpp infectivity, AZD4547 in vivo these data strongly suggest that EGCG inhibits HCV entry by affecting the HCV envelope. The mechanism of HCV entry is a complex multistep process involving binding of the viral particle to the cell surface, interaction with several entry factors followed by endocytosis, and fusion of the viral envelope with an internal membrane. To determine which step of HCV entry is impaired by

EGCG, virus binding was performed at 4°C. Then, the cells were shifted to 37°C to allow endocytosis and fusion, with EGCG being added at different times (Fig. 5B). Heparin, a known inhibitor of HCV binding, was used as a positive control. 29 A strong decrease in HCV infection was observed when

EGCG was added at 4°C during the first hour (i.e., binding step), whereas no inhibition was observed when EGCG was added after virus binding, even before endocytosis. As expected, similar results were obtained with heparin. selleck compound These results are consistent with a direct action of EGCG on the viral particle, as suggested before, for the antiviral effect to take place. To determine whether EGCG impairs directly the binding of particles to the cell surface or a later step of virus entry, we analyzed virus binding in the presence of EGCG. Cells were inoculated with purified HCVcc at 4°C in the presence of EGCG or heparin, and the amount of bound viruses was determined by quantifying HCV genomic RNA (gRNA). As expected, heparin strongly reduced HCV attachment to the cell surface (Fig. 5C). In the presence of EGCG, a strong decrease in virus binding was also observed. Together, these results show that EGCG, likely by acting on the virion, inhibits virus entry by impairing virus binding to the cell surface. After infection of Huh-7 cells with HCVcc, progeny viruses are transmitted to adjacent cells, resulting in focal areas of spreading infection (i.e., foci).

We next explored the methylation status of the PAX5 promoter by using MSP (Fig. 2A). Full or partial methylation was detected in HCC cell lines (Hep3B, huH4, huH6, Mahlavu, SNU398, and PLC5), which showed silenced or down-regulated PAX5 expression, whereas methylation was not detected in the cell lines with PAX5 expression (hUH7, SNU475, RAD001 and SNU449) (Fig. 2A). The methylation density within the PAX5

promoter region was then characterized and validated by BGS (Fig. 2B). The BGS results were consistent with those of MSP in which dense methylation was found in methylated cell lines by MSP, but not in normal liver tissues (Fig. 2B). To confirm whether the promoter methylation is involved

in the silencing of PAX5, five cell lines with silenced PAX5 expression including Hep3B, HepG2, SNU387, SNU398, and PLC-5 were treated with 5-Aza combined with or without trichostatin A. This treatment resulted in the restoration of PAX5 expression in all cell lines examined (Fig. MG 132 2C), further implicating that the transcriptional silence of PAX5 was mediated by promoter methylation. The frequent inactivation of PAX5 in HCC cell lines but not in normal liver tissue suggested that PAX5 may play a role in tumor growth. We thus examined the growth-suppressive effect through ectopic expression of PAX5 in HepG2 and Hep3B, which showed no PAX5 expression. Reexpression of PAX5 in the stable transfected HepG2 and Hep3B cells was confirmed by RT-PCR (Fig. 3A1) and western blot (Fig. 3A2). Ectopic expression of PAX5 in these HCC cell lines caused a significant decrease in cell viability (Fig. 3B). The inhibitory effect on HCC cell growth was further confirmed by colony formation assay. The colonies formed in PAX5-transfected cells were significantly fewer in number and smaller in size than in empty vector-transfected

cells (down to 44%-54% of vector control, P < 0.01) (Fig. 3C). We examined the contribution of apoptosis to the observed growth inhibition in HCC cells derived by PAX5. The number of HepG2 cells with sub-G1 DNA content after PAX5 transfection was substantially increased compared with the control vector transfection learn more (24.75% ± 2.09% versus 33.11% ± 2.06%; P < 0.05). Apoptosis was further assessed by immunoblot detection of the active form of caspase-7, caspase-8, caspase-9, and poly (ADP-ribose) polymerase (PARP). As shown in Fig. 3D, overexpression of PAX5 enhanced the levels of active caspase-7, -8, -9, and PARP. The subcutaneous tumor growth curve of Hep3B stably transfected with PAX5 or empty vector in vivo is shown in Fig. 4A. The tumor volume was significantly lower in PAX5-transfected nude mice as compared to the vector control mice (P < 0.0001). At the end of experiments tumors were isolated and weighed.

We next explored the methylation status of the PAX5 promoter by using MSP (Fig. 2A). Full or partial methylation was detected in HCC cell lines (Hep3B, huH4, huH6, Mahlavu, SNU398, and PLC5), which showed silenced or down-regulated PAX5 expression, whereas methylation was not detected in the cell lines with PAX5 expression (hUH7, SNU475, Selleckchem AZD2014 and SNU449) (Fig. 2A). The methylation density within the PAX5

promoter region was then characterized and validated by BGS (Fig. 2B). The BGS results were consistent with those of MSP in which dense methylation was found in methylated cell lines by MSP, but not in normal liver tissues (Fig. 2B). To confirm whether the promoter methylation is involved

in the silencing of PAX5, five cell lines with silenced PAX5 expression including Hep3B, HepG2, SNU387, SNU398, and PLC-5 were treated with 5-Aza combined with or without trichostatin A. This treatment resulted in the restoration of PAX5 expression in all cell lines examined (Fig. selleck chemical 2C), further implicating that the transcriptional silence of PAX5 was mediated by promoter methylation. The frequent inactivation of PAX5 in HCC cell lines but not in normal liver tissue suggested that PAX5 may play a role in tumor growth. We thus examined the growth-suppressive effect through ectopic expression of PAX5 in HepG2 and Hep3B, which showed no PAX5 expression. Reexpression of PAX5 in the stable transfected HepG2 and Hep3B cells was confirmed by RT-PCR (Fig. 3A1) and western blot (Fig. 3A2). Ectopic expression of PAX5 in these HCC cell lines caused a significant decrease in cell viability (Fig. 3B). The inhibitory effect on HCC cell growth was further confirmed by colony formation assay. The colonies formed in PAX5-transfected cells were significantly fewer in number and smaller in size than in empty vector-transfected

cells (down to 44%-54% of vector control, P < 0.01) (Fig. 3C). We examined the contribution of apoptosis to the observed growth inhibition in HCC cells derived by PAX5. The number of HepG2 cells with sub-G1 DNA content after PAX5 transfection was substantially increased compared with the control vector transfection check details (24.75% ± 2.09% versus 33.11% ± 2.06%; P < 0.05). Apoptosis was further assessed by immunoblot detection of the active form of caspase-7, caspase-8, caspase-9, and poly (ADP-ribose) polymerase (PARP). As shown in Fig. 3D, overexpression of PAX5 enhanced the levels of active caspase-7, -8, -9, and PARP. The subcutaneous tumor growth curve of Hep3B stably transfected with PAX5 or empty vector in vivo is shown in Fig. 4A. The tumor volume was significantly lower in PAX5-transfected nude mice as compared to the vector control mice (P < 0.0001). At the end of experiments tumors were isolated and weighed.

Macroscopic and microscopic observations were made. Gene expression and intracellular signaling pathways were analyzed. Oxidative stress, antioxidant, and macrophage deletion treatments were also performed in parallel with Cygb siRNA or CYGB overexpressing vectors transfection. Results: Model 1: 25 or 0.05 ppm DEN treatment for 25 or 36 weeks induced liver tumor formation in 1 00 or 43% of Cygb-KO mice, respectively, Belnacasan research buy compared to 44 or

0% of WT mice. In KO mice, there was liver fibrosis, increased inflammatory gene expression and augmented oxidative stress. Model 2: with as little as 8 weeks of CDAA treatment, Cygb-KO mice showed marked steatohep-atitis, which resulted in advanced fibrosis at 16 weeks, compared MK-8669 manufacturer with the WT. Surprisingly, at 32 weeks, 100% of Cygb-KO mice of both genders developed liver cancer, compared to 0% in WT mice. At all time points, there was severe inflammation associated with activated liver cancer pathways in the Cygb-KO mice. Cygb-KO HSC (HSC isolated from Cygb-KO mice) and Cygb siRNA-transfected WT-HSC were both primed, as indicated by markedly increased

expression of αSma, collagen 1α1, Tnfα, Tgfβ1, Il-1β, Il-6, Ccl-2, Ccl-3, and Ccl-4 mRNA and superoxide production compared to controls. Oxidative stress and antioxidant defense PCR arrays showed altered expression of 31 genes involved in the metabolism of reactive oxygen species in Cygb-KO mice. N-acetyl cysteine treatment for 2 weeks eliminated the oxidative stress in CDAA-fed Cygb-KO mice in vivo, and in cultures of isolated Cygb-KO HSC. Macrophage deletion after 8 weeks of CDAA feeding reduced the inflammatory reaction, oxidative stress, and fibrosis in Cygb-KO mice. Moreover, Hep-G2 cells overexpressing CYGB showed decreased proliferation under hypoxia compared with plasmid controls, selleck chemicals llc as well as downregulated expression of fibrosis- and angiogenesis-related genes. Conclusion: Cygb deficiency promotes liver

cancer development via HSC priming and augmented inflammation, local fibrosis, and oxidative stress. Disclosures: The following people have nothing to disclose: Thuy T. Le, Yoshinari Matsumoto, Hoang Hai, Katsutoshi Yoshizato, Norifumi Kawada Objective Overexpression of platelet-derived growth factor-C (PDGF-C) in the liver of mice (Pdgf-c Tg) induces hepatic fibrosis, followed by the development of hepatocellular carcinoma. We identified differentially expressed miRNAs in Pdgf-c Tg mice and evaluated their functional relevance in the progression of hepatic fibrosis and the development of HCC. Materials and Method We used TaqMan® Array Rodent MicroRNA A Cards v2.0 containing 384 miRNA assays. miRNAs were knocked down by locked nucleic acid (LNA)-modified antisense oligonu-cleotides (LNA-antimiR) in immortalized human stellate cells, Lx-2. Pdgf-c Tg mice at 32 months of age were injected with LNA-antimiR-214 via the tail vein six times (50 μg each) with 3-week intervals by using Invivofectamine® 2.0.

Lastly, experience with the use of pdVWF/FVIII concentrate is also available from a prospective, naturalistic study

conducted in haemophilia centres in Italy (n = 9) and Spain (3) [20]. Between 1999 and 2005, 17 patients received ITI therapy with pdVWF/FVIII concentrate (Fanhdi®; Grifols S.A., Barcelona, Spain). All patients had poor risk features for successful treatment: all were aged 7 years or older at the start of therapy, including 10 adults; only one patient had an inhibitor for less than 2 years; two patients had peak inhibitor titres of >200 BU. At the start of treatment, four patients had inhibitor titres of >10 BU, and four patients had failed previous ITI therapy. Nine patients were initiated on a low-dose regimen [50 IU kg−1 (three times a week)] and eight on a high-dose regimen (100 or 200 IU kg−1 day−1). Patients received ITI for anywhere from 4 to 33 months. In terms of check details patient outcomes, 9 of 17 patients (53%) achieved complete success after a median of 24 months (Table 3), including two of the four patients who

had failed previous ITI therapy. Seven patients achieved a partial success (Table 3), with sustained low inhibitor titres (median 1.5 BU, range 1.1–2.8) but with abnormal FVIII recovery and/or half-life, while the remaining patient withdrew from treatment after 12 months when the inhibitor titre was still 70 BU. Based on the evidence available to date, it is not possible to state with confidence that pdVWF/FVIII is the product of choice when initiating patients on ITI therapy. Of the few published studies, all have their limitations: patient numbers were selleck small, none of the studies was randomized, and all used different ITI therapy protocols. Although the 53% complete response rate reported by Gringeri and colleagues appears promising [20], this is counteracted to some extent by the 32% complete response rate reported by Kurth et al. [19]. Despite this uncertainty, recommendations published by European [21] and International [22] consensus see more panels state that ‘FVIII concentrates containing VWF should be considered for patients who fail ITI using high purity

FVIII’. Some reasons have been postulated as to why pdVWF/FVIII concentrates may enhance ITI therapy compared with recombinant products. In brief, one of these postulates centres around a potential protective effect of the presence of VWF. The VWF binds to different epitopes in the A3 and C2 domains of FVIII which may offer it protection against degradation by proteinases. Similarly, most inhibitors are also directed at epitopes on the A3 and C2 domains along with the A2 domain. As such, the presence of VWF on the FVIII molecule leads to (i) masking of epitope sites by VWF thereby preventing inhibitors (neutralizing antibodies) from binding to the FVIII molecule and (ii) increased stability (i.e. reduced clearance) of the FVIII molecule.

These data indicate that IFN-γ treatment reverses the TLR2 deficiency-enhanced progression of HCC by restoring the p53/p21/pRb-dependent

senescence and autophagy flux in TLR2−/− liver tissue (Fig. 8F). We observed increased ROS accumulation, cellular proliferation, and p62 aggregation as well as decreased DNA repair, programmed cell death, and autophagy flux in the TLR2−/− liver tissue in this study. All of these changes are attributable to the ICG-001 cell line loss of cellular senescence as a result of TLR2 deficiency in the liver. Because ASK1/P38MAPK/NF-κB signaling or inflammatory cytokines can initiate and sustain cellular senescence,26-29 the failure of senescence induction can be attributed to the broad-spectrum reductions in the immune responses to DEN injury in the TLR2−/− livers. Indeed, senescent cells enter a unique state characterized by senescence-associated changes, including growth arrest, an arrested cell cycle, SA β-gal expression, a lack of responsiveness

to cell death signals, and the senescence-associated secretory phenotype (SASP).33 SASP causes a robust increase in the expression and secretion of numerous cytokines, chemokines, growth factors, and proteases in these cells. These factors, particularly IL-1α, can activate tumor-suppressive pathways to establish and/or maintain senescent growth arrest.33 These findings are supported by observations that treatment of TLR2−/− mice with IFN-γ, a typical Th1 cytokine and positive modulator of senescence,30 attenuates HCC progression by restoring p53/p21-dependent Small molecule library ic50 senescence in the liver. Thus, our studies demonstrate a protective role for TLR2-mediated p21- and p16/pRB-dependent

senescence in DEN-induced carcinogenesis. Indeed, DEN-induced ROS production and DNA damage can trigger programmed cell death and maintain a low level of cell proliferation in check details WT mice because intact TLR2 activity can induce a senescence response after DEN administration.20-22 Moreover, the accumulated ROS can be cleared, and damaged DNA can be repaired by the activation of the ASK1/p38 MAPK/NF-κB signaling networks26, 29 in DEN-treated mice. Together, these networks diminish the development and progression of DEN-induced HCC in WT mice. However, suppressed activation of the ASK1/p38 MAPK/NF-κB signaling pathway results in the persistent accumulation of ROS, which prevents the repair of damaged DNA, decreases programmed cell death, and increases hepatocyte proliferation; the ultimate result is the promotion of HCC development and progression in TLR2−/− mice. These observations are consistent with the findings presented in previous studies. Specifically, it has been reported that the activation of the ASK1/p38 MAPK/NF-κB pathway is critical for both neutralizing ROS/ER stress and repairing damaged DNA in stressed cells.29 The activation of this pathway is sufficient to activate and maintain cellular senescence.

Chronic alcohol drinking is a major cause of chronic liver disease worldwide and encompasses

a spectrum of liver injuries, including fatty liver, alcoholic hepatitis, drug discovery cirrhosis, and hepatocellular carcinoma.[1, 2] Many mechanisms underlying the pathogenesis of alcoholic liver disease (ALD) have been identified.[1, 2] These include direct hepatotoxicity of ethanol and its metabolites, oxidative stress generated by ethanol metabolism, activation of innate immunity, elevation of pro-inflammatory cytokines and chemokines, and many other mechanisms. Among the cytokines and chemokines involved in progression of ALD, tumor necrosis factor-α and monocyte chemoattractant protein-1 have been shown to play an important role in the development of early alcoholic liver injury,[3,

4] whereas interleukin-6 (IL-6), via the activation of signal transducer and activator of transcription 3 (STAT3) in hepatocytes during early alcoholic liver injury, plays an important role in ameliorating steatosis and hepatocellular damage.[5, 6] Although the hepatoprotective function of IL-6 has been well documented, clinical application of IL-6 for ALD treatment is limited by the many potential side effects of Selleck Cyclopamine IL-6, which likely result from the ubiquitous expression of IL-6 receptor. This led us to explore another hepatoprotective cytokine IL-22, which activates similar signaling selleck chemicals llc pathways (such as STAT3) as those activated by IL-6 in hepatocytes.

Importantly, IL-22 receptor expression is restricted to epithelial cells, which suggests that IL-22 treatment would likely produce fewer side effects than IL-6, and is an attractive candidate for ALD therapy. Initially identified as a gene induced by IL-9 in mouse T lymphocytes, IL-22 shares 22% amino acid identity with IL-10 and belongs to IL-10 family.[7] Both IL-10 and IL-22 utilize the ubiquitously expressed IL-10R2, but IL-10 signaling also requires IL-10R1, which is expressed on immune cells, whereas IL-22 signaling needs IL-22R1, which is expressed on epithelial cells.[8] Thus, IL-10 targets immune cells and acts as an important anti-inflammatory cytokine; IL-22 targets epithelial cells and plays an important role in promoting tissue repair. After binding to IL-22R1 and IL-10R2, IL-22 predominantly induces STAT3 activation, and to a lesser extent, activation of other signaling pathways such as STAT1, STAT5, mitogen-activated protein kinases in epithelial cells, followed by upregulating expression of many genes that control anti-microbial immunity and tissue repair.

[12] This is suggestive of an in vitro/in vivo correlation for resistance to asunaprevir in GT1a. A relationship between baseline resistance and virologic breakthrough was unclear. Patient 7, with a preexisting NS3-R155K, was expected to experience virologic breakthrough but did not. Instead, three of six virologic breakthroughs had preexisting NS3-Q80 polymorphisms. Given the polymorphic nature of NS3-80 in GT1a sequences, its this website correlation

with virologic failure requires further investigation. The dual combination of daclatasvir and asunaprevir was sufficient to suppress viral breakthrough in Patient 7, who had a preexisting 1a-NS3-R155K. Although relapse was observed at Week 4 posttreatment in this patient, preexistence of the asunaprevir-resistant variant did not result in a delayed decline of HCV RNA. It is unknown if a cure could have been achieved with the addition of an interferon or third direct-acting selleck chemicals antiviral. NS3-R155K was detected as the major emergent variant in GT1a patients failing treatment with boceprevir or telaprevir, whereas the other emergent resistance-associated variants to asunaprevir NS3-D168Y/E/T have also been detected in patients treated with TMC435 and vaniprevir.[18, 19] Emergent daclatasvir-resistant

variants NS5A-Q30E/R, L31V/M, and Y93C/N have also been detected by other first-generation NS5A inhibitors that are based on the structure of daclatasvir.[20, 21] In contrast, treatment of GT1 prior null responders, the majority of whom were infected with GT1a, with 24 weeks of the quadruple therapy (daclatasvir, asunaprevir, peginterferon alfa-2a, and ribavirin) resulted in a durable response with no confirmed relapse through 48 weeks of follow-up.[7] Interestingly, the regimen click here was robust enough to result in cure even with the early transient

emergence of daclatasvir-resistant variants.[7] This suggests that the drug combination was sufficient to ultimately suppress the emergence of virally fit high level drug-resistant variants. Addition of peginterferon alfa-2a and ribavirin to daclatasvir and asunaprevir as rescue or intensification therapy resulted in a cure for 33% (2/6) of patients (Patients 5 and 6) who experienced viral breakthrough to daclatasvir and asunaprevir.[7] These two patients had rapid declines in viral load at Week 2 (<25 IU/mL) but experienced virologic breakthrough at weeks 10 and 12, respectively. The HCV RNA levels were low (<10,000 IU/mL) at the time of treatment intensification, although they had detectable signature resistance variants to both daclatasvir and asunaprevir. Retreatment of prior null responders with peginterferon alfa and ribavirin normally results in <10% SVR. However, in the cases presented here, patients were able to respond to the quadruple combination.

An excess of subviral particles over infectious virions in plasma is common during viral infections. For instance, HBV surface antigen (HBsAg) circulates in the blood as nucleocapsid-free, envelope-containing subviral particles that

also outnumber HBV DNA–positive Dane particles by 1 × 103 to 1 × 105.36 Subviral, nucleocapsid-free particles, bearing the envelope glycoprotein, are also frequently found during dengue virus or tick-borne encephalitis virus Flavivirus infections.37, 38 Subviral particles appear to exert biologically relevant properties. For example, HBsAg inhibits TLR9-mediated activation and interferon-α production in plasmacytoid dendritic cells (DCs).39 Similarly, HCV LVPs interfere with Toll-like receptor 4–triggered maturation of DCs, inducing a shift in DC function that stimulates T helper 2 cells Lumacaftor research buy instead of T helper 1 cells.40, 41 Recombinant

LVPs also fuse with liposomes in a fusion process leading to the coalescence of internal contents of TRL particles and liposomes.32 The presence of such high proportions of modified lipoproteins during hepatitis C may modify the physiologic functions of lipoprotein, particularly if they have membrane fusion property, and participate to some HCV-induced metabolic dysfunctions. We Ensartinib also observed the presence of low-density viral particles that did not contain detectable apoB. Because we could not quantify the envelope glycoproteins, and because the number of glycoproteins per particles is not known, the proportion of nucleocapsid-positive and -negative particles could not be estimated. Thus, it remains to be determined whether subviral, nucleocapsid-negative, and apoB-negative low-density particles, either resembling HCVcc or the recombinant glycoprotein subviral particles produced by Huh7 cells, are also produced in vivo. For four patients, such particles were the only low-density viral particles and they may also be present in unknown proportion in all patients. These particles could contribute to the high molar ratios of neutral lipid over apoB, assuming that they could be coimmunoprecipitated with apoB-positive LVPs; their presence would further increase the overall proportion of subviral particles.

It should check details be stressed, however, that for some patients, all HCV RNA are immunoprecipitated by anti-apoB antibody.8 In conclusion, the HCV circulating viral particle populations are complex and include several forms, such as apoB-positive and -negative as well as nucleocapsid-positive and -negative LVPs that may contribute in different extent to the pathophysiology of chronic hepatitis C. We acknowledge the contribution of the AniRA – Laboratoire L3/UMS platform of SFR Biosciences Gerland-Lyon Sud (UMS344/US8) for their help. We thank Patricia Barbot, Virobiotec, Center for Biological Resources, Hospices Civils de Lyon, and Claude Vieux for patient and sample management. We thank Vincenzo Vinzi (ESSEC, Cergy-Pontoise, F95000) for his help with statistical testing.

Methods: By using Fluorescence activated cell sorting analyse, we isolated CD90+ cells from the HCC cell lines SMCC7721 and Huh-7. And the “stemness” of CD90+ cells ware identified by sphere formation assay, colony formation assay or matrigel invasion and transwell migration assay, respectively. Immunohistochemical staining techniques was used to detect the expression levels of CD90 and CD44 in 38 hepatocellular carcinoma patients undergoing curative resection between 2008 and 2011 in our hospital. Clinicopathologic data for these patients anti-PD-1 monoclonal antibody were investigated. The prognostic

effects of CD90 and CD44 were evaluated using the wilcoxon sum rank test and compared using the log-rank test. Results: Freshly isolated CD90+ cells

were found to be more quiescent, with a greater ability to form tumors in vitro, and an ability GSK-3 inhibitor to self-renew, and metastasis. The clinical impact of CD90 was also addressed, and it was found to significantly correlate with portal vein invasion (log-rank test, p < 0.05). In another hand, CD44 were independent predictors for overall survival and disease-free survival. The expression of CD44 was associate with postoperative recurrence (log-rank test, p < 0.05), overall survival and disease-free survival rates (wilcoxon sum rank test, p < 0.01). Conclusion: CD90 and CD44 could be used as markers for human liver cancer and as potential predictors of clinical predictors of postoperative recurrence in HCC and target for the individualized therapy of this malignancy. Key Word(s): 1. HCC; 2. LCSCs; 3. CD90; 4. CD44; Presenting Author: SUN YEONG CHO Additional Authors: SEOK BAE KIM, HYUNG JUN KIM, SUNG SOO RA, YEONG KWANG CHOO, SEONG MIN JEON, HYUN DEOK SHIN, JUNG EUN SHIN, HONG JA KIM, IL HAN SONG Corresponding learn more Author: SEOK BAE KIM Affiliations: Dankook University Hospital Objective: 18F-FDG PET-CT (18F-fluorodeoxyglucose positron emission tomography-computed

tomography) has been widely used in many kinds of malignant tumors. However, the efficacy of 18F-FDG PET-CT in hepatocellular carcinoma (HCC) is still controversy. We aimed to evaluate the usefulness of 18F-FDG PET-CT in staging and treatment of HCC. Methods: We analyzed the HCC patients retrospectively who took 18F-FDG PET-CT examination from January 2008 to December 2012. We compared the stage and treatment between before and after 18F-FDG PET-CT to know the efficacy on HCC. We reviewed the medical record, biopsy result, follow-up CT and follow-up data to know the confirmation of the extrahepatic metastasis which was suspected in 18F-FDG PET-CT. Results: Total 160 HCC patients were analyzed. 27 patients (16.9%) of them were suspected as extrahepatic metastasis on 18F-FDG PET-CT. High FDG uptake on lung was observed on 18 patients. 13 patients of them were already suspected as hematogenous lung metastasis in liver CT. 3 patients of them were diagnosed as benign lesion on chest CT and biopsy.