Animals ; Disease Models, Animal ; Liver ; pathology ; Liver Failure, Acute ; metabolism ; pathology ; Male ; RNA, Messenger ; genetics ; Rats ; Rats, Sprague-Dawley ; Transcription Factor RelA ; metabolism

Carcinoma, Hepatocellular ; metabolism ; pathology ; Core Binding Factor Alpha 3 Subunit ; metabolism ; Female ; Hepatocytes ; metabolism ; Humans ; Liver ; metabolism ; pathology ; Liver Neoplasms ; metabolism ; pathology ; Male ; RNA, Messenger ; genetics

Adult ; Case-Control Studies ; Humans ; Interleukin-12 ; blood ; Liver Diseases, Alcoholic ; blood ; Male ; Middle Aged ; Transforming Growth Factor beta1 ; blood

Adolescent ; Adult ; Asian Continental Ancestry Group ; Carcinoma, Hepatocellular ; genetics ; virology ; Ethnic Groups ; Female ; Genotype ; Hepatitis B ; genetics ; virology ; Hepatitis B virus ; genetics ; Humans ; Liver Cirrhosis ; genetics ; virology ; Liver Neoplasms ; genetics ; virology ; Male ; Middle Aged ; Mutation ; Young Adult

Adult ; Asian Continental Ancestry Group ; Elasticity ; Elasticity Imaging Techniques ; Humans ; Liver ; physiology ; Male ; Middle Aged

OBJECTIVETo investigate the effect of baicalin on liver fatty acid binding protein in oxidative stress model in vitro.

METHODS(1) Cellular oxidative stress in vitro was induced by incubating cells with 400μmol/L hydrogen peroxide (H₂O₂) for 20 minutes at 37 degrees C in the dark. After Chang liver cell line was treated with different dose of baicalin for 24, 48 and 72 hours. MTT assay was employed to detect cell viability, and then the hydrogen peroxide (TC50) of the different dose of baicalin was calculated. (2) Based on MTT assay, cells were treated with three different doses of baicalin (25, 50, 100 μmol/L) for 24 and 48 hours before being exposed to 400 μmol/L H₂O₂ for 20 minutes at 37 degrees C. Then, reactive oxygen species (ROS) assay and activity assays of superoxide dismutase (SOD) and reduced glutathione hormone (GSH) were evaluated. (3) Realtime PCR and Western blotting were applied to explore the influence of baicalin on the expression level of L-FABP. (4) One-way ANOVA was used for results statistical analysis.

RESULT(1) MTT assay showed baicalin treatment at 25, 50, 100 μmol/L for 24 and 48 hours was feasible (83.60% ± 3.47%, 72.36% ± 2.18%, 70.16% ± 2.04% for 24 hours; 84.93% ± 3.11%, 76.16% ± 2.45%, 72.72% ± 2.31% for 48 hours, P > 0.05, F = 386.24, 475.92 respectively). Meanwhile, we found by the linear regression model that the median toxic concentration of baicalin for 48 hours was 170.6 μmol/L, and the median toxic concentration of baicalin for 24 hours was 153.2 μmol/L. (2) ROS assay showed dichlorofluorescin in all baicalin-treated cells after stress was significantly reduced (37.0 ± 3.30, 22.90 ± 3.84, 29.60 ± 2.52 for 24 hours respectively, P < 0.05, F = 70.06; 35.77 ± 2.35, 21.80 ± 3.10, 23.87 ± 1.98 for 48 hours respectively, P < 0.05, F = 110.92) as compared with the H₂O₂-treated cells. Moreover, 50 μmol/L baicalin treatment for 48 hours was the optimal condition against ROS generation (21.80 ± 3.10, P < 0.01, F = 110.92). Furthermore, the activities of intracellular SOD and GSH was increased significantly (51.53 ± 1.91 μg/mg for SOD, P < 0.05, F = 93.81; 49.85 ± 1.45 U/mg for GSH, P < 0.05, F = 92.51). (3) Although realtime PCR analysis indicated 50 μmol/L baicalin treatment for 48 hours could have no changes of the level of L-FABP expression under the oxidative stress condition, western blotting analysis indicated 50 μmol/L baicalin treatment for 48 hours could increase up to about 80% for the level of L-FABP expression.

CONCLUSIONBaicalin was suggested to be able to enhance both L-FABP expression and activity of intracellular SOD and GSH, and therefore protected hepatocytes from oxidative stress.

Catalase ; metabolism ; Cell Line ; Fatty Acid-Binding Proteins ; metabolism ; Flavonoids ; pharmacology ; Glutathione ; metabolism ; Glutathione Peroxidase ; metabolism ; Hepatocytes ; metabolism ; Humans ; Hydrogen Peroxide ; Oxidative Stress ; drug effects ; Reactive Oxygen Species ; metabolism ; Superoxide Dismutase ; metabolism

OBJECTIVETo evaluate magnetic resonance venography (MRV) in diagnosing obstructive interface morphology of Budd-Chiari syndrome(BCS).

METHODSMRV examination was performed on 44 cases of BCS, and the images of obstructive interface morphology of the inferior vena cava were reviewed by two radiologists.

RESULTSIn all 44 cases, there were 37 cases with complete obstruction and 7 with incomplete obstruction. MRV showed 4 cases with membrane with hole of incomplete obstruction. The morphologies MRV demonstrated that the proximal part of the 37 cases with complete obstruction were mainly divided into the cone type (36 cases) and the planum type (1 case). Besides, the type of distal end of obstruction were the cone type (30 cases), the planum type (4 cases) and the irregular type (3 cases). The overall sensitivity, specificity, positive and negative predictive values for the diagnosis of MRV were respectively 100%%, 57.1%, 92.5% and 100% as compared to the DSA.

CONCLUSIONThe examination of MRV is capable of revealing the obstructive interface morphology of the inferior vena cava, especially for the distal end of obstruction. MRV can provide guidelines in interventional treatment of Budd-Chiari syndrome.

Adult ; Aged ; Angiography, Digital Subtraction ; Budd-Chiari Syndrome ; diagnostic imaging ; pathology ; Female ; Humans ; Magnetic Resonance Imaging ; Male ; Middle Aged ; Vena Cava, Inferior ; diagnostic imaging ; pathology ; Young Adult

OBJECTIVETo investigate the molecular mechanism of adiponectin inhibiting activation of hepatic stellate cells in non-alcoholic fatty liver fibrosis.

METHODSThe rat models of non-alcoholic fatty liver fibrosis were successfully established by fat-rich diet administration. The expression of adiponectin mRNA and protein were respectively detected by reverse transcription-polymerase chain reaction (RT-PCR) and Western blot. LX-2 cells were cultured in an adipogenic differentiation mixture to induce quiescent adipocytic phenotypes, and then they were treated with TGFβ1, adiponectin and TGFβ1 + adiponectin, respectively. RT-PCR and Western blot were used to determine the expressions of mRNAs and proteins of a-smooth muscle actin (a-SMA), Collagen, adenosine monophosphate-activated protein kinase (AMPK), inducible nitric oxide synthase (iNOS), and endothelial NOS (eNOS). The results were analyzed using one-way ANOVA, Student-Newman-Keuls test, and linear correlation analysis. A P value of less than 0.05 was considered as statistically significant.

RESULTSIn vivo, with the progress of non-alcoholic fatty liver fibrosis, the model rats gradually showed hepatic steatosis, inflammation, necrosis and fibrosis. Compared with the control group, the level of serum adiponectin (2.49 ± 0.86 vs 5.81 ± 0.87, P < 0.05) and hepatic expressions of adiponectin mRNA and protein (0.26 ± 0.04 vs 0.72 ± 0.08; 0.64 ± 0.07 vs 0.21 ± 0.07, all P < 0.05) were all decreased in the 24th week group, and were negatively correlated with the level of Collagen which increased gradually. In vitro, TGFβ1 could activate quiescent LX-2 cells by decreasing mRNA and protein expression of eNOS (0.30 ± 0.10 vs 0.44 ± 0.08; 0.30 ± 0.09 vs 0.46 ± 0.07, all P < 0.05) and increasing the expression of iNOS (0.53 ± 0.07 vs 0.37 ± 0.04; 0.55 ± 0.07 vs 0.39 ± 0.05, all P < 0.05). Recombinant adiponectin not only maintained the quiescent phenotype of LX-2 cells but also inhibited LX-2 cells activation due to TGFβ1 by increasing the expression of eNOS (0.43 ± 0.08 vs 0.30 ± 0.10; 0.42 ± 0.07 vs 0.30 ± 0.09, all P < 0.05) and phosphorylation of AMPK (0.43 ± 0.07 vs 0.24 ± 0.04, P < 0.05) and decreasing the expression of iNOS (0.44 ± 0.05 vs 0.53 ± 0.07; 0.46 ± 0.07 vs 0.55 ± 0.07, all P < 0.05).

CONCLUSIONSData suggested that adiponectin could play a protective role on the pathogenesis of non-alcoholic fatty liver fibrosis by inhibiting the activation of hepatic stellate cells via up-regulating the expression of eNOS, which might associate with increased phosphorylation of AMPK.

Adiponectin ; metabolism ; pharmacology ; Animals ; Disease Models, Animal ; Fatty Liver ; metabolism ; Hepatic Stellate Cells ; metabolism ; Liver Cirrhosis ; metabolism ; pathology ; Nitric Oxide Synthase Type III ; metabolism ; Non-alcoholic Fatty Liver Disease ; Rats ; Rats, Wistar ; Reverse Transcriptase Polymerase Chain Reaction ; Transforming Growth Factor beta1 ; metabolism ; pharmacology

OBJECTIVETo identify the role of p38 MAPK- NF-kB signaling pathway in TNF-α induced IL-8 production in human hepatocellular carcinoma cells.

METHODSThe concentrations of IL-8 from MHCC-97H cells were measured by an enzyme-linked immunosorbent assay (ELISA). The phosphorylation of p38 MAPK was analyzed by Western blot and immunofluorescence. NF-kB p65 protein nuclear translocation was determined by non-radioactive NF-kB p50 / p65 transcription factor activity kit and immunofluorescence.

RESULTSThe IL-8 production from MHCC-97H cells challenged with TNFa significantly increased in a time-dependent (F = 144.04, P < 0.01) and dose-dependent (F = 364.14, P < 0.01) manners, as compared with those without TNFa challenge. TNFa up-regulated the phosphorylation levels of p38 MAPK and increased the translocation of NF-kB p65 protein into the nucleus, also proved by immunofluorescence staining. p38 MAPK inhibitor (SB203580) could significantly inhibit IL-8 production in a dose-dependent manners (F = 65.47, P < 0.01), and partially inhibited NF-kB p65 nuclear translocation in a dose-dependent manner (F=141.20, P < 0.05).

CONCLUSIONTNF-α could increase the production of IL-8 in MHCC-97H cells and p38 MAPK- NF-kB pathways seem to play a central role in the regulation of IL-8 production.

Carcinoma, Hepatocellular ; metabolism ; Cell Line, Tumor ; Humans ; Interleukin-8 ; metabolism ; Liver Neoplasms ; metabolism ; Phosphorylation ; Signal Transduction ; Transcription Factor RelA ; metabolism ; Tumor Necrosis Factor-alpha ; pharmacology ; p38 Mitogen-Activated Protein Kinases ; metabolism

OBJECTIVETo investigate the clinical efficacy of cryotherapy ablation treatment for advanced hepatocellular carcinoma, and to analyse the predictive factors of cryotherapy ablation treatment.

METHODS190 patients of hepatitis B-related advanced HCC from 2005 to 2008 in our hospital underwent curative cryoablation. We used clinical cohort method to analyze cryoablation group (147 cases) and control group (43 cases). The median OS (over survival time) and TTP (time to disease progression) were compared. We also evaluated the clinical significance of age, gender, location of portal vein tumor thrombus, HBeAg, tumor histological grade, Child-Pugh classification, end-stage liver disease (MELD) score, advanced liver cancer prediction system (ALCPS) score and the Eastern Cooperative Oncology Group performance status (ECOG PS) score for predicting the efficacy of cryoablation. Two Groups were compared with the x² test. Survival rates were estimated by the Kaplan-Meier method and compared by the log rank test. The Cox proportional hazards model was used to determine the independent factors on survival based on the variables selected in univariate analysis.

RESULTSMedian survival time of cryoablation group and Control group were 7.5 (4.2 to 14.6) months and 3.2 (1.2 to 8.6) months, median TTP were 3.5 (2.5 to 4.5) months and 1.5 (1.0 to 3.5 months), the differences between were statistically significant (P < 0.05). Median OS and TTP of advanced HCC patients who had Well-differentiated tumor, Child-pugh A-class and low score of MELD score, ALCPS score; ECOG PS score were significantly longer than that of the poorly differentiated tumor, Child-pugh B-class and the high those scores (P < 0.05). ECOG PS (P less than 0.05, 95% CI 1.074 - 2.143) and ALCPS (P < 0.05, 95% CI 1.005-2.121) were independent predictors for OS of advanced HCC.

CONCLUSIONSCryoablation treatment can prolong median OS and TTP of advanced HCC. ECOG PS and ALCPS are important predictors for survival time of advanced HCC.

Azo Compounds ; pharmacology ; Carcinoma, Hepatocellular ; metabolism ; Cell Line, Tumor ; drug effects ; metabolism ; Gonanes ; pharmacology ; Humans ; Liver Neoplasms ; metabolism ; Proteomics