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 purpose of this paper is to provide a histopathologic basis for abnormalities in immune-complex clearance in liver disease. Fc receptors in CCl4-induced liver cirrhosis in rats were studied by applying peroxidase-antiperoxidase immunoglobulin G complex as a ligand to the frozen sections. Intravenous injection of bovine serum albumin-antibovine serum albumin complexes or colloidal carbon was combined with histological staining for endogenous peroxidase, fibronectin, laminin, or a lectin, Bandeiraea simplicifolia agglutinin I. In the cirrhotic process, sinusoidal Fc receptors showed a weakened reactivity to the ligand with focal absence, and the length of the Fc receptor-positive portion of the sinusoids in unit area decreased to about 50% of the normal value in the advanced cirrhosis. Fibronectin and the lectin showed the presence of sinusoids where Fc receptors were absent. The endothelium in Fc receptor-negative areas did not take up either immune complexes or carbon, and Kupffer cells were absent in these areas. A disturbed immune-complex metabolism was thus suggested to occur in association with the defect of sinusoidal Fc receptors in liver cirrhosis. These abnormalities appeared to not be directly related to perisinusoidal laminin deposition, i.e., capillarization of the sinusoid.
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PMID:Defect of sinusoidal Fc receptors and immune complex uptake in CCl4-induced liver cirrhosis in rats. 234 26

Serum from 38 patients with liver disease and elevated serum AFP concentration was subjected to affinity chromatography on concanavalin A (Con A) and lentil lectin. More than 70% of the serum AFP of the 18 patients with primary liver cancer (PLC) or the 12 patients with cirrhosis or chronic active hepatitis (BLD) bound to Con A, less than 70% of the serum AFP of 8 patients with metastatic liver disease (MLD) bound to Con A. On the other hand less than 20% of the serum AFP of the BLD patients but more than 20% of the serum AFP of the PLC or MLD patients bound to lentil lectin. Thus reactivity of serum AFP towards Con A and lentil lectin provides a simple test that can be used in the differential diagnosis of BLD, PLC and MLD.
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PMID:Differential reactivity of alpha-fetoprotein with lectins and its usefulness in the diagnosis of various liver diseases. 244 65

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

The sinusoidal endothelial cells of human liver can be identified by light and electron microscopy, but there appear to be no specific immunocytochemical markers of these cells. Among specific markers available for vascular endothelial cells in general, Ulex europaeus I lectin (UEA I) is the most sensitive. In the present study, 37 liver biopsies were examined for UEA I binding and for Factor VIII related antigen (F VIII RAg) to determine if sinusoidal endothelial cells were positive. The material included normal liver, biopsies from patients with cirrhosis and biopsies in a variety of other liver diseases. Three embryonal human livers were also included in the immunocytochemical analysis. Eleven oesophageal rings obtained at mechanical transection for variceal bleeding in cirrhotic patients were used as control tissue. Sinusoidal endothelial cells of normal liver did not stain with UEA I, but six of seven with alcoholic cirrhosis and only one of 25 non-cirrhotic liver specimens (a case of acute hepatitis with bridging necrosis) were positive. In two of the six cirrhoses the sinusoidal endothelial cells were stained for F VIII RAg as well. Embryonal sinusoidal endothelial cells were stained with UEA I but were negative for F VIII RAg. The results of the study confirm that sinusoidal endothelial cells of normal adult human liver are phenotypically different from those lining blood vessels in other sites. In cirrhosis, positive staining may be related to the transformation of hepatic sinusoids into true capillaries and thus be a marker of the severity of physiological disturbance in the liver.
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PMID:Hepatic sinusoidal endothelium: Ulex lectin binding. 249 24

The activity of dipeptidyl aminopeptidase IV was studied in the sera of 378 hospitalized patients. The mean activity of dipeptidyl aminopeptidase IV was elevated significantly in patients with neoplasmata and hepatitis, but not in patients with liver cirrhosis. Significant correlations (p less than 0.001) existed with gamma-glutamyl transferase, glutamate dehydrogenase, alkaline phosphatase and leucine aminopeptidase. A significant correlation with lactate dehydrogenase existed only in patients with neoplasmata. Principal component analysis, performed with aspartate aminotransferase, alanine aminotransferase, alkaline phosphatase, leucine aminopeptidase, lactate dehydrogenase and dipeptidyl aminopeptidase IV, revealed correlations between the activities of aspartate aminotransferase and alanine aminotransferase, and between alkaline phosphatase and leucine aminopeptidase, but neither dipeptidyl aminopeptidase IV nor lactate dehydrogenase showed any correlation with either of these two groups. In lectin affinity chromatography with concanavalin A and wheat germ lectin sepharose, serum dipeptidyl aminopeptidase IV from liver cirrhosis patients showed the same binding pattern as that from healthy subjects. The activity and glycosylation of dipeptidyl aminopeptidase IV in serum and hepatic plasma membranes was investigated in rats, following the induction of hepatitis with galactosamine. In the serum, dipeptidyl aminopeptidase IV activity was elevated as early as 6 h after galactosamine injection, and the elevated activity persisted until the 7th day. At the same time dipeptidyl aminopeptidase IV activity was also elevated in the hepatic plasma membrane. Ninety eight percent of hepatic dipeptidyl aminopeptidase IV bound to concanavalin A as well as to wheat germ lectin and this value was unchanged during hepatitis. In the serum of control rats, 90% of dipeptidyl aminopeptidase IV bound to concanavalin A but only 39% to wheat germ lectin.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Dipeptidyl aminopeptidase IV in hospitalized patients and in galactosamine hepatitis of the rat: Activity and lectin affinity chromatography in serum and hepatic plasma membranes]. 257 17

Metastases in livers with cirrhosis are a rare event in comparison to metastases in normal livers. This fact is of great importance for clinical differential diagnosis of tumours of the liver. High metalloproteinase inhibitor contents and especially altered lectins or lectin binding sites in cirrhosis of the liver may help to explain the rare event "metastasis in cirrhosis".
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PMID:[Why are metastases in cirrhotic livers so rare?]. 267 14

The variation of the carbohydrate chain of gamma-glutamyltransferase was studied in 45 liver patients by means of lectin affinity chromatography. Five lectins were used: concanavalin A, Ricinus communis I and II, Maclura pomifera and Ulex europaeus agglutinin. The binding towards Con A was shown to be independent from the binding towards the other lectins. Parallel variations of binding results against the galactose- and fucose-recognizing lectins were obtained. In liver steatosis, the binding results were comparable to those obtained in normal patients. Cirrhosis and metastasis patients showed a decreased binding towards Con A, while the binding against the various galactose- and fucose-recognizing lectins was increased. After neuraminidase treatment, an increased affinity towards all lectins was observed. However, differences in RCA I and RCA II binding between patients and controls still persisted. Besides sialic acid, also galactose and fucose residues contribute to serum gamma-glutamyltransferase heterogeneity.
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PMID:Lectin-affinity chromatography of serum gamma-glutamyltransferase in liver disease. 288 78

Ricinus communis agglutinin II-reactive glycoproteins from the ascites of patients with hepatocellular carcinoma were prepared using lectin affinity chromatography. Normal serum- and cirrhotic ascites-components were removed by columns with immobilized antibodies against them. Ricinus communis agglutinin II-reactive glycoproteins thus obtained were supposed to be hepatocellular carcinoma-associated and less than 0.1% of the protein in the starting material. Polyacrylamide gel electrophoresis of these glycoproteins revealed more than 10 major polypeptides with molecular weights ranging from 20K to 200K daltons. The rabbit antiserum raised against them reacted with at least three components of 45, 52 and 55K daltons. The serum level of this antibody-reactive glycoproteins was assessed by an enzyme-linked immunosorbent assay. It was elevated in 91% of cases of hepatocellular carcinoma, 70% of cases of other gastrointestinal carcinoma, 88% of cases of liver cirrhosis, 55% of cases of chronic hepatitis, and 25% of cases of acute hepatitis. The mean value of hepatocellular carcinoma was significantly greater than those of other groups. These results suggest that some of Ricinus communis agglutinin II-reactive glycoproteins in hepatocellular carcinoma patients may be cancer-associated glycoproteins and that their serum levels are increased in hepatocellular carcinoma patients.
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PMID:Ricinus communis agglutinin II-reactive glycoproteins from the ascites of patients with hepatocellular carcinoma and their use in enzyme-linked immunosorbent assay. 303 39

alpha 1-Acid glycoproteins (alpha 1-AG) were collected from the ascites of patients with liver cirrhosis or liver cancer, respectively, and their physical, chemical, and biological properties were compared. The substance obtained from patients with liver cancer showed a 2-3 times higher inhibitory effect on [3H]thymidine uptake by human peripheral lymphocytes stimulated with PHA than that obtained from patients with cirrhosis. The two substances showed differences in their affinity to wheat germ agglutinin (WGA) and concanavalin A (Con A). Of the fractions obtained by lectin affinity chromatography, the Con-A bound fraction showed the greatest lymphocyte proliferation inhibitory activity. The alpha 1-AG levels were elevated in both the patients with cancer and those with infectious disease, but the level of the Con-A bound fraction was elevated only in those with cancer. This study suggests that the molecular variants of alpha 1-AG differ in their carbohydrate structure with the disease, and that the cellular immunity of the host way be partially controlled by changes in the content of these molecular variants.
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PMID:Comparative study of alpha 1-acid glycoprotein molecular variants in ascitic fluid of cancer and non-cancer patients. 338 35

Lectin affinities of AFP were analyzed using Con A sepharose chromatography and crossed immuno-affino-electrophoresis. With Con A, AFP was divided into three subfractions, nonbound, loosely-bound and tightly-bound by chromatography, or two subfractions, nonbound and bound by electrophoresis. Con A nonbound subfraction was small in percentage in hepatocellular carcinoma (HCC), neonatal hepatitis, congenital biliary atresia (CBA), liver cirrhosis (LC) and cord sera. In contrast with these, the increase of Con A non-bound AFP was observed in yolk sac tumor (YST) and metastatic liver cancer (Meta). With LCA, AFP was divided into three subfractions: nonbound, loosely bound and tightly bound. Loosely bound fraction was very small in every specimen. AFPs from cord sera and LC showed uniform LCA affinity pattern, but AFPs from HCC were not uniform. Our data suggest that the analyses of lectin affinity of AFP serve as a diagnostic tool in differentiating (1) HCC from YST, (2) HCC from Meta, (3) CBA or neonatal hepatitis from YST and (4) LC from some cases of HCC.
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PMID:[Analysis of lectin-affinity of alpha fetoprotein-diagnostic approach]. 619 65


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