Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0023890 (cirrhosis)
 42,195 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An antibody-lectin enzyme immunoassay (EIA) technique was developed for the analysis of sugar chains of serum alpha-fetoprotein in various liver diseases. The anti-'alpha-fetoprotein'-IgG was coated on a microtiter plate and then treated with periodic acid. A serum sample was added to the plate and then a 'peroxidase'-conjugated lectin was added. The amount of lectin bound to the sugar chain of the 'alpha-fetoprotein' was estimated from the 'peroxidase' activity. The 'peroxidase' activities of 4 different lectins, LCA, Con A, LCA and EPHA, were compared. The LCA/'wheat germ agglutinin' activity ratio and LCA/EPHA activity ratio were increased in liver diseases and LCA/'wheat germ agglutinin' ratio showed a statistically significant difference between the chronic hepatitis and the liver cirrhosis groups (p less than 0.05). Furthermore, when serum samples were pretreated with sialidase, a statistically significant difference was observed in the LCA/EPHA and LCA/Con A ratios between the chronic hepatitis and the hepatoma groups (p less than 0.05). These results indicated that low sialylation at the non-reduced end of the sugar chains of 'alpha-fetoprotein' occurs in liver cirrhosis and that high fucosylation at the reduced end of N-acetylglucosamine residue of 'alpha-fetoprotein' occurs in hepatomas.
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PMID:Alpha-fetoprotein antibody-lectin enzyme immunoassay to characterize sugar chains for the study of liver diseases. 246 50

Gangliosides isolated from 5 cases of normal liver tissues, 11 cases of liver cirrhosis and 5 cases of hepatocellular carcinoma were compared in their concentrations and compositions. Quantitative analysis revealed no significant change of ganglioside levels between normal and cirrhotic liver tissues or hepatocellular carcinoma. There was also no significant difference (p greater than 0.05) between cirrhotic liver tissues and hepatocellular carcinoma. Two dimensional thin-layer chromatography of the total ganglioside preparations of liver tissues from both liver cirrhosis and hepatocellular carcinoma showed proliferation of GM2, GD3, GD1 and at least two unidentified components, named provisionally spots Nos. 1 and 2 in the present report, and loss of GM3. Sialidase treatment and thin-layer chromatography showed the components of these spots to be sialidase-labile monosialogangliosides and distinctly different from GD3 which was described elsewhere.
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PMID:Ganglioside variations in human liver cirrhosis and hepatocellular carcinoma as shown by two-dimensional thin-layer chromatography. 285 12

Enhanced fucosylation has been suggested as a marker for serologic monitoring of liver disease and hepatocellular carcinoma (HCC). We present a workflow for quantitative site-specific analysis of fucosylation and apply it to a comparison of hemopexin (HPX) and complement factor H (CFH), two liver-secreted glycoproteins, in healthy individuals and patients with liver cirrhosis and HCC. Label-free LC-MS quantification of glycopeptides derived from these purified glycoproteins was performed on pooled samples (2 pools/group, 5 samples/pool) and complemented by glycosidase assisted analysis using sialidase and endoglycosidase F2/F3, respectively, to improve resolution of glycoforms. Our analysis, presented as relative abundance of individual fucosylated glycoforms normalized to the level of their nonfucosylated counterparts, revealed a consistent increase in fucosylation in liver disease with significant site- and protein-specific differences. We have observed the highest microheterogeneity of glycoforms at the N187 site of HPX, absence of core fucosylation at N882 and N911 sites of CFH, or a higher degree of core fucosylation in CFH compared to HPX, but we did not identify changes differentiating HCC from matched cirrhosis samples. Glycosidase assisted LC-MS-MRM analysis of individual patient samples prepared by a simplified protocol confirmed the quantitative differences. Transitions specific to outer arm fucose document a disease-associated increase in outer arm fucose on both bi- and triantennary glycans at the N187 site of HPX. Further verification is needed to confirm that enhanced fucosylation of HPX and CFH may serve as an indicator of premalignant liver disease. The analytical strategy can be readily adapted to analysis of other proteins in the appropriate disease context.
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PMID:Quantification of fucosylated hemopexin and complement factor H in plasma of patients with liver disease. 2530 77