Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0019204 (hepatocellular carcinoma)
71,386 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Vessels around the intrahepatic large bile ducts (peribiliary vascular plexus) were examined by histologic, immunohistochemical and scanning electron microscopic observations. The vessels within duct walls were mainly capillaries, while those around the duct walls were composed of capillaries and venules. A majority of vessels was positive for factor VIII-related antigen and Ulex europaeus lectin I. Scanning electron microscopy of hepatic arterial and biliary casts revealed that bile ducts were surrounded by the vascular plexus derived from hepatic arterial branches, and serial section observations in addition disclosed the vessels connecting the peribiliary plexus with portal venous branches ('internal roots'). The peribiliary vascular plexus was increased considerably in livers with portal hypertension, especially idiopathic portal hypertension, extrahepatic portal venous obstruction and hepatocellular carcinoma with portal venous tumor thrombi. Internal roots were also frequently found in the livers with portal hypertension. These results suggest that altered intrahepatic hemodynamics in portal hypertensive conditions involves the peribiliary vascular plexus, resulting in an increase of the number and frequent occurrence of 'internal roots', these vessels probably operating as intrahepatic collaterals.
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PMID:Vascular plexus around intrahepatic bile ducts in normal livers and portal hypertension. 254 Nov 96

Alpha-fetoprotein (AFP) subfractions were studied in 38 sera including 34 patients with primary hepatoma and 4 from patients with hepatic metastasis of gastric cancer. Fractionation of AFP was carried out by concanavalin A (Con A) or lentil lectin (LCH) crossed-line affinity immunoelectrophoresis. With use of Con A, fetal-liver-originated subfraction (peak a) was commonly found in both primary hepatoma and metastatic liver cancer, while yolk-sac-originated subfraction (peak b) was detected in 7 of 34 (20.6%) primary hepatomas and 4 of 4 (100%) metastatic liver cancers. With use of LCH, fetal-liver-originated subfractions (peaks A and/or C) were commonly found in both primary hepatoma and hepatic metastasis of gastric cancer, while yolk-sac-originated subfraction (peak B) was found only in metastatic liver cancer. These findings suggest that glycosylation of AFP in primary hepatoma differs from that in hepatic metastasis of gastric cancer. It is also suggested that AFP synthesized in hepatic cancers and fetal liver are differently glycosylated and AFP synthesis of hepatic malignancies are not always retrogenetically expressed, as in case of the fetal liver. Clinically, different patterns of AFP subfraction identified by Con A or LCH crossed-line affinity immunoelectrophoresis facilitate a differential diagnosis of primary hepatoma and hepatic metastasis of gastric cancer, in cases of elevated serum AFP levels. In the current study, attention was also given to the retrogenetic expression of AFP synthesis in hepatic metastasis of gastric cancer.
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PMID:Serum alpha-fetoprotein subfractions in patients with primary hepatoma or hepatic metastasis of gastric cancer. 257 79

A full-length cDNA clone for the 14 kDa soluble beta-galactoside-binding lectin of man has been isolated from a cDNA library from HepG2 hepatoma cells. The derived amino acid sequence is identical with that of the 14 kDa lectin from human placenta. The results of Northern and Southern blotting of several different human cell lines using a cDNA probe for the 14 kDa lectin suggest the presence of a single gene for this protein. Thus, although there are multiple proteins in the range 14-200 kDa which are antigenically related to this lectin, we would conclude from the present study that there is only one gene for the 14 kDa lectin.
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PMID:Evidence that the 14 kDa soluble beta-galactoside-binding lectin in man is encoded by a single gene. 271 46

The surface membrane glycoprotein patterns of spontaneous hepatic nodules, phenobarbitone induced nodules and hepatocellular carcinoma were studied in the C3H mouse using lectin histochemistry. The lectin binding patterns of hepatocellular carcinoma cells were markedly different to those of non-tumour cells and similar to the pattern in chemically induced hepatocellular carcinomas. This supports the hypothesis that changes in surface glycoprotein are a consistent feature associated with malignancy. Similar changes in the distribution of lectin binding sites were also seen in the phenobarbitone induced eosinophilic nodules and in a proportion of spontaneous basophilic nodules. Two populations of early basophilic nodules were identified on the basis of their lectin binding patterns, and this may indicate a link between one nodular type and carcinoma.
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PMID:The lectin binding characteristics of spontaneous and phenobarbitone induced hepatic lesions in C3H/He mice. 276 66

Structures of the sugar moieties of gamma-glutamyl transpeptidases purified from the kidney and the liver of rat, mouse, and cattle were studied after being chemically released as oligosaccharides. The results indicated that both organ-specific and species-specific differences exist in the sugar chains of the enzyme. Comparative studies of sugar chains of the heavy and light subunits of the rat kidney enzyme revealed that high mannose-type sugar chains are found only in the heavy subunit. By the same analysis of the oligosaccharide fractions obtained from four isozymic forms of the rat kidney enzyme, it was found that all these enzymes contain 2 mole of neutral sugar chains but different numbers of acidic sugar chains in one molecule. Comparative studies of oligosaccharides obtained from the enzymes purified from rat AH-66 hepatoma and from normal rat liver revealed that more than 40% of the sugar chains of the hepatoma enzyme contain bisecting N-acetylglucosamine residues which are not found in those of the liver enzyme. By making use of the structural changes associated with malignant transformation, a new diagnostic method or hepatoma was developed. In principle, the method consists of affinity chromatography of the desialylated serum enzyme using an erythroagglutinating lectin agarose column.
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PMID:[Structural changes in the sugar chains of gamma-glutamyltranspeptidase by malignant transformation]. 287 94

During the first stage of infection, the paramyxovirus Sendai virus attaches to host cells by recognizing specific receptors on the cell surface. Productive virus-cell interactions result in membrane fusion between the viral envelope and the cell surface membrane. It has recently been shown that the ganglioside GD1a and its more complex homologs GT1b and GQ1b are cell surface receptors for Sendai virus. We report in this paper that the temperature-sensitive mutant ts271 of the Enders strain of Sendai virus lacks the viral attachment protein HN and the biological activities of hemagglutination and sialidase activity associated with it when the virus is grown at 38 degrees C. This HN- virus was unable to infect or agglutinate conventional host cells that contained receptor gangliosides and were readily infected by the parental wild-type virus. The HN- virus did, however, attach to and infect Hep G2 cells, a line of hepatoma cells that retains the asialoglycoprotein receptor (ASGP-R) upon continuous culture. This receptor is a mammalian lectin that recognizes galactose- or N-acetylgalactosamine-terminated proteins. In accordance with the known properties of this receptor, infection by the HN- virus was abolished by treatment of Hep G2 cells with sialidase, by the presence of Ca2+ chelators, and by competition with N-acetylgalactosamine, asialoorosomucoid, and antibody to the receptor. F, the only glycoprotein on the HN- virus, was shown to compete with the galactose-terminated protein asialoorosomucoid for the ASGP-R. The ability of the HN- virus to cause cell-cell fusion of Hep G2 cells indicated that attachment of this virus to the ASGP-R still permitted viral entry by its usual mode--i.e., membrane fusion at the cell surface. These results open up the possibility that enveloped viruses, which contain glycosylated proteins or lipids, may make use of naturally occurring lectins in addition to their normal receptors as a means of attachment to host cells.
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PMID:An alternative route of infection for viruses: entry by means of the asialoglycoprotein receptor of a Sendai virus mutant lacking its attachment protein. 298 37

Bacterially fermented mistletoe preparations (BFMP) were tested on rat hepatoma tissue culture (HTC) cells and human leukemia Molt 4 cells. A dose-dependent inhibition of the growth rate of the cells was observed. For both cell lines, cytostatic concentrations, expressed in weight of fresh plant, were 0.5 mg/ml culture medium for oak BFMP and 1 mg/ml for apple tree BFMP. However, the action of the two preparations was markedly different on each cell line. Non-viable HTC cells were not stained by trypan blue while non-viable Molt 4 cells were fully colored by this reagent. A lysis of cellular membranes of HTC cells was observed by electron microscopy. Furthermore, oak BFMP inhibited the growth of virus transformed 3T3-SV40 cells more than that of non-transformed 3T3 cells. In contrast to BFMP, non-fermented extracts and a purified mistletoe lectin showed a greater inhibition of the growth of Molt 4 cells than of HTC cells. Samples withdrawn at different times during fermentation gradually lost their inhibitory effect on the growth of Molt 4 cells while their action on HTC cells increased up to the 4th day of fermentation. These results are discussed in relation to the cytotoxic substances of mistletoe already characterized.
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PMID:Effects of mistletoe (Viscum album L.) extracts on cultured tumor cells. 301 72

Two cDNA clones were isolated by immunoscreening a human hepatoma cDNA library with an antiserum that bound specifically to a human soluble beta-galactoside-binding lectin with Mr of approximately 14,000. The deduced amino acid sequences of the inserts of these two clones show considerable homology with each other, the sequence of chicken skin beta-galactoside-binding lectin, and eight peptides derived from purified human lung lectin of Mr approximately 14,000. However, the sequence differences between the two hepatoma clones as well as among each clone and the lung peptides suggest that at least three variants of the gene encoding this lectin are expressed in human tissue.
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PMID:Evidence that a human soluble beta-galactoside-binding lectin is encoded by a family of genes. 302 May 51

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

On polyacrylamide gradient gel electrophoresis, normal serum cholinesterase was separated into seven isozymes (I-VII from the anodic to the cathodic side). The enzyme of the conditioned medium of the HuH-7 cell line, established from a human hepatoma, had two main isozymes. The one migrating faster was located slightly to the cathodic side of band II of the normal serum enzyme, and the other, a slower one, electrophoresed at the same position as that of band VI of the normal serum enzyme. Aside from these two isozymes, a faint band with enzyme activity sometimes appeared at a position just cathodic or very close to the position of band I of the normal serum isozymes. The effect of some inhibitors and activators on both the normal serum enzyme and the enzyme of the conditioned medium was similar, but lectin-binding properties of the two enzymes were different with Ricinus communis agglutinin I, concanavalin A and wheat germ agglutinin. These results suggest that the difference in sugar moieties of both enzymes is expressed in D-galactose, D-mannose and N-acetylglucosamine.
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PMID:Novel cholinesterase expression in the HuH-7 cell line. 303 81


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