3. Cirrhosis MICE Obesity Promotes Liver Inflammation and Cancer by Enhancing Pro-Inflammatory Cytokines Inflammation
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14. The ‘Anti-inflammatory’ Pentoxifylline For Patients With Advanced Cirrhosis Marcellin et al. N Engl J Med 2008 Tenofovir vs. Adefovir For Chronic Hepatitis B Telaprevir and Peginterferon With or Without Ribavirin For Chronic Hepatitis C Hézode et al. N Engl J Med 2009 Lebrec et al. Gastroenterology 2010 Survival Without Complications Pentoxifylline (n=164) Placebo (n=171) P =0.03
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Notes de l'éditeur
Slide 76 NAFLD: Spectrum of Hepatic Pathology The next several slides illustrate the histopathology of NAFLD. As mentioned earlier, nonalcoholic fatty liver disease (NAFLD) is a spectrum of hepatic pathology that ranges from fatty liver (steatosis) on the most clinically-benign end of the spectrum to cirrhosis on the opposite extreme where most liver-related morbidity and mortality occur. Nonalcoholic steatohepatitis (NASH) is an intermediate form of liver damage that sometimes progresses to cirrhosis. Some individuals who become cirrhotic from NAFLD develop hepatocellular carcinoma. Brunt EM. Nonalcoholic steatohepatitis. Semin Liver Dis 2004;24:3-20.
Slide 76 NAFLD: Spectrum of Hepatic Pathology The next several slides illustrate the histopathology of NAFLD. As mentioned earlier, nonalcoholic fatty liver disease (NAFLD) is a spectrum of hepatic pathology that ranges from fatty liver (steatosis) on the most clinically-benign end of the spectrum to cirrhosis on the opposite extreme where most liver-related morbidity and mortality occur. Nonalcoholic steatohepatitis (NASH) is an intermediate form of liver damage that sometimes progresses to cirrhosis. Some individuals who become cirrhotic from NAFLD develop hepatocellular carcinoma. Brunt EM. Nonalcoholic steatohepatitis. Semin Liver Dis 2004;24:3-20.
On the right Residues 186–192 (shown in pink stick presentation) of the D2 domain of gp130 that are deleted in IHCAs are intimately involved in interactions with IL-6, as shown in the crystal structure of the IL-6R–IL-6–gp130 complex (PDB: 1P9M)7. IHCA deletions 173–177 and 215 (labelled in red) are also predicted to disrupt the IL-6–gp130 interface. The numbering of residues corresponds to the IL6ST complementary DNA, which has 22 additional amino-terminal residues compared with the polypeptide chain due to the peptide signal.
On the right Residues 186–192 (shown in pink stick presentation) of the D2 domain of gp130 that are deleted in IHCAs are intimately involved in interactions with IL-6, as shown in the crystal structure of the IL-6R–IL-6–gp130 complex (PDB: 1P9M)7. IHCA deletions 173–177 and 215 (labelled in red) are also predicted to disrupt the IL-6–gp130 interface. The numbering of residues corresponds to the IL6ST complementary DNA, which has 22 additional amino-terminal residues compared with the polypeptide chain due to the peptide signal.