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)

The effects of acute ethanol challenge on serum glycoprotein concentrations in man were studied. Serum levels of haptoglobin, alpha-2-macroglobulin and pre-albumin were measured fasting and 6 hr after oral ethanol 0.75 g/kg body weight in 8 healthy controls, 13 patients with alcoholic liver disease and 13 with non-alcoholic-related liver damage, both patient groups being further subdivided into those with and without cirrhosis. Basal levels of haptoglobin were significantly higher in non-cirrhotic alcoholics than controls and pre-albumin levels were lower in non-alcohol-related cirrhotic liver disease. In response to ethanol challenge, no consistent change was observed in any group, nor was there any significant difference between groups. There was, however, a significant correlation (r = 0.53, P less than 0.005) between the percentage changes in haptoglobin and alpha-2-macroglobulin. In 16 subjects (2 controls, 8 alcoholics and 6 non-alcoholics) blood levels of ethanol and acetaldehyde were measured serially: there was no relationship between the peak or mean concentration and the glycoprotein response. This study does not substantiate other reports which claimed to be able to predict the severity and reversibility of alcoholic liver disease on the basis of the serum glycoprotein response to ethanol: ethanol challenge with measurement of serum glycoproteins cannot substitute for proper histological assessment.
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PMID:Effect of ethanol challenge on serum glycoproteins in alcoholic and non-alcoholic liver disease. 244 17

Six acute phase proteins (haptoglobin, alpha 1-acid glycoprotein, alpha 1-antitrypsin, alpha 2-macroglobulin, C reactive protein and transferrin) have been measured in the sera of chronic liver disease (CLD) patients with different aetiology (viral, autoimmune and alcoholic) and histology (steatosis, chronic persistent hepatitis, chronic active hepatitis, cirrhosis), and in patients with liver cancer. 1) The most striking changes concerned alpha 2-macroglobulin (increased) and haptoglobin (decreased) levels. 2) Transferrin was lower in alcoholic liver disease than in viral CLD, CRP was lower in autoimmune than in viral or alcoholic CLD, and alpha 1-acid glycoprotein was lower in viral and alcoholic CLD than in autoimmune CLD. Acute phase protein assay may prove useful in differential diagnosis, particularly when specific markers are not available (autoimmune, non A, non B, alcoholic liver diseases). 3) No significant differences related to aetiology (B, non A non B, D viruses) were observed in viral CLD. 4) Patients who progressed to CLD after acute viral hepatitis type B or non A non B did not show different APP levels from those who had recovered when tested 8-12 months after the acute phase. 5) The pattern of APP changes observed in primary liver cell carcinoma was different from both the cirrhotic pattern and the pattern presented by other tumours with or without liver metastasis.
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PMID:Acute phase proteins in chronic and malignant liver diseases. 245 53

The monoclonal antibody MBr1 defines the blood group H determinant with beta 1----3N-acetylgalactosamine linkage (Fuc alpha 1----2Gal beta 1----3GalNAc----R) carried by type 3 or 4 backbone. The distribution of the antigen detected by this antibody was studied immunohistochemically in liver tissues. Although bile ducts with a diameter of more than about 100 microns normally expressed the MBr1-reactive antigen supranuclearly, smaller bile ducts and bile ductules did not express the antigen. In cirrhotic liver, proliferated bile ductules extensively expressed the MBr1-reactive antigen. In spite of the absence in normal liver cells, the antigen was expressed membranously in some cirrhotic liver cells. Under subcellular fractionation, MBr1 reactivity was almost exclusively recovered in the microsomal fraction. By HPTLC immunostaining, the major MBr1-reactive antigen was shown to be carried by type 4 chain H glycolipid (globo-H, Fuc alpha 1----2Gal beta 1----3GalNAc beta 1----3Gal alpha 1----4Gal beta 1----4Glc beta 1----1Cer). MBr1 reactive glycoprotein was not found. In conclusion, although type 4 chain H glycolipid is not expressed by normal bile ductules and liver cells, it is actively synthesized and expressed by proliferated bile ductules and some of the liver cells in cirrhosis in the absence of any neoplastic change.
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PMID:Type 4 chain H expression by bile ductules and hepatocytes in cirrhosis. 246 83

Two mouse monoclonal antibodies (MoAbs), KM-93 raised against human lung adenocarcinoma and KM-231 raised against human gastric cancer, were useful in serum diagnosis of several human cancer. KM-93 and KM-231 recognize sialyl Lex epitope and sialyl Lea epitope, respectively, expressed on glycoprotein and glycolipid. We established a new "cocktail" sandwich enzyme-linked immunosorbent assay system using the two MoAbs and the advantage of this assay system, which can simultaneously detect sialyl Lex and sialyl Lea antigens, is assessed in the present study. The new assay system is composed of a mixture of KM-93 and KM-231 as 1st antibodies and a mixture of biotinylated two MoAbs as 2nd antibodies. We evaluated the concentration of MoAbs and optimized it to gain high cancer-positivity. This assay system covered sialyl Lex positive and/or sialyl Lea-positive sera and gave a high rate of positive results in lung adenocarcinoma (62.3%), gastric cancer (32.5%), colon cancer (37.5%), pancreatic cancer (83.3%), bile duct and gall bladder cancer (66.7%) and hepatoma (76.9%), whereas positive results in healthy adults remained low. Positive results in benign diseases of lung (12.5%), pancreas (10.8%), gall bladder and bile duct (9.1%) were very low, but were higher in liver cirrhosis (33.3%), hepatitis and liver injury (34.8%). Simultaneous detection of two carbohydrate antigens, sialyl Lex and sialyl Lea was clearly superior to single detection.
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PMID:Advantage of cocktail-use of two anti-tumor monoclonal antibodies, KM-93 and KM-231, in serum diagnosis of cancer. 247 31

The binding of alpidem, a new anxiolytic drug, has been studied in plasma from 6 healthy subjects, 12 patients with renal failure, 12 patients with liver cirrhosis and 12 chronic uraemics maintained on haemodialysis, as well as in 12 serum samples from the placental cord, to represent the situation in the newborn. The unbound fraction was 0.61% (healthy volunteers), 1.31% (newborns), 0.86% (cirrhotic patients), 0.72 (patients with renal failure), 0.70% (before haemodialysis) and 0.79% (after haemodialysis). Binding in the volunteers was significantly different from that in neonates and cirrhotics only. Alpidem became bound to isolated albumin (45 g.l-1) and alpha 1-acid glycoprotein (0.75 g.l-1) to 97.2% and 97.1%, respectively. The bound fraction of the drug in a mixture of two proteins was 99.1%. For alpidem, it appears that alpha 1-acid glycoprotein may balance the effect of any decrease in the albumin concentration.
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PMID:Plasma protein binding of alpidem in healthy volunteers, in neonates and in liver or renal insufficiency. 257 11

To determine whether alterations of the carbohydrate moiety of human alpha 1-acid glycoprotein constitute a marker of hepatic damage we studied purified alpha 1-acid glycoprotein from healthy individuals and two groups of patients with benign liver diseases: alcoholic cirrhosis and acute viral hepatitis. The results indicate: (1) increased concanavalin A-non reactive forms in cirrhosis and hepatitis, (2) a markedly increased proportion of fucosyl residues in all cirrhotic and some hepatitis patients. Although hyperfucosylation is generally considered to be a tumor marker, the observation here in the two benign liver diseases indicates that an increased fucosyl content should be considered as a more general expression of pathological glycoconjugate metabolism.
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PMID:Microheterogeneity of the carbohydrate moiety of human alpha 1-acid glycoprotein in two benign liver diseases: alcoholic cirrhosis and acute hepatitis. 261 11

The protein binding of ethinyloestradiol (EE2) was investigated in the plasma from 14 healthy volunteers, 10 patients with hyperbilirubinemia, 10 patients with liver cirrhosis and 10 patients with renal failure. Binding assay was performed by equilibrium dialysis at 37 degrees C. The unbound fraction (mean +/- SD) of EE2 was 1.17 +/- 0.12 (volunteers), 2.74 +/- 0.77 (hyperbilirubinemics; p less than 0.001) 1.51 +/- 0.31 (cirrhotics; p less than 0.01) and 1.44 +/- 0.11 (renal failure; p less than 0.001). Studies with isolated albumin and alpha-1-acid glycoprotein showed that albumin is the major plasma protein to bind EE2. Warfarin (75 microM) and diazepam (75 microM) increased by 5.0% and 3.0%, respectively, the unbound fraction of EE2 when albumin concentration was 15 microM. Under similar conditions, digitoxin did not modify the binding of EE2. At therapeutic concentrations, warfarin and diazepam did not affect the binding of EE2 in plasma.
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PMID:Plasma protein binding of ethinyloestradiol: effect of disease and interaction with drugs. 277 26

DU-PAN-2 is a high-molecular-weight glycoprotein defined by a murine monoclonal antibody (MAb) elicited against a human pancreatic adenocarcinoma cell line. This MAb recognizes an oncofetal antigen present on the surface of normal pancreatic and bile-duct epithelium, normal bronchus epithelium, and some adenocarcinomas. Elevated levels of the antigen (greater than 400 U/ml) have been detected in the serum of 79% of patients with adenocarcinoma of the pancreas and in a small percentage of patients with other adenocarcinomas, by means of a competition radioimmunoassay. Here, we have studied DU-PAN-2 antigen levels in sera of patients with a spectrum of hepatobiliary diseases and controls. Serum DU-PAN-2 antigen was elevated in 59% of 112 patients with non-malignant hepatobiliary diseases and in 50% of hepatoma patients. None of 50 healthy controls had elevated serum DU-PAN-2 levels. Patients in every category of hepatobiliary disease studied had elevated median serum DU-PAN-2 levels; the highest median levels were seen in patients with primary biliary cirrhosis (1,296 U/ml) and the lowest in stable cirrhosis (300 U/ml). Elevated serum DU-PAN-2 levels in one patient with primary biliary cirrhosis and in one patient with hepatoma returned to normal following liver transplantation. Serum DU-PAN-2 levels did not correlate well with alkaline phosphatase, 5'-nucleotidase, bilirubin, or alpha-fetoprotein. Using an immunoperoxidase technique on formalin-fixed, deparaffinized liver sections, we showed that DU-PAN-2 MAb reacted heterogeneously with bile-duct epithelium but never stained hepatocytes or hepatoma cells. While serum DU-PAN-2 levels may be useful in detecting and monitoring pancreatic adenocarcinoma, they are not specific for this disease.
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PMID:Detection of an oncofetal antigen (DU-PAN-2) in sera of patients with non-malignant hepatobiliary diseases and hepatomas. 283 18

Serum cathepsin activity and serum level of glycoproteins were determined in patients with chronic liver disorders (cirrhosis, chronic persistent hepatitis, chronic active hepatitis, hepatoma. An increase of cathepsin activity was found in chronic persistent hepatitis and cirrhosis of the liver. Increased level of glycoproteins was observed, the most evident in patients with chronic active hepatitis. An increase of the ratio cathepsin activity/glycoprotein concentration was found in chronic persistent hepatitis, and a decrease of this ratio was observed in chronic active hepatitis.
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PMID:[Serum cathepsin activity in chronic liver diseases]. 303 88

Sera of patients with various liver diseases were examined for the presence of Hanganutziu-Deicher (H-D) antibodies by enzyme immunoassay with high-molecular weight glycoprotein (HMWGP) isolated from bovine red blood cell stromata. IgG class H-D antibodies were demonstrated in sera of 5.9% of acute hepatitis, 28.1% of chronic hepatitis and 21.9% of liver cirrhosis patients. H-D specificity of the antibodies under investigation was determined by absorption experiments. Evidence was also presented that the H-D antibodies in the liver disease sera are directed to N-glycolyl neuraminic acid (NGNA) and/or NGNA-dependent determinants of HMWGP.
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PMID:Studies on Hanganutziu-Deicher antigens-antibodies. I. Hanganutziu-Deicher antibodies of IgG class in liver diseases. 309 47


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