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)

Two extracellular matrix and basement-membrane components, fibronectin (Fn) and laminin, were studied by the indirect immunoperoxidase technique in ten primary human liver cancers. Similar distributions of both Fn and laminin were detected in the well differentiated hepatocellular carcinomas with trabecular and tubular pattern. Two moderately differentiated hepatomas contained Fn only. Neither Fn nor laminin were present, however, in the parenchyma of one poorly differentiated hepatoma. In three cases of cholangiocarcinoma, laminin surrounded the tumorous ducts, while Fn appeared mainly in the reactive connective tissue stroma. The present findings indicate that bile-duct cancers synthesize laminin, and not Fn while differentiated hepatocellular carcinomas produce both Fn and laminin in vivo. The presence of Fn even in moderately differentiated types of liver cancer is in contrast to the findings for carcinomas developing from other organs and it may serve as a marker for primary hepatocellular carcinomas in the differential diagnosis.
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PMID:Distribution of fibronectin and laminin in human liver tumors. 298 80

It is presently unknown what factors regulate the rate of intracellular transport of secretory proteins. The human hepatoma cell line Hep G2 is highly differentiated and secretes many of the proteins characteristic of normal hepatocytes. The secretion kinetics of nine proteins by Hep G2 cells in culture was investigated using pulse-chase techniques and immunoisolation of proteins with monospecific antibodies. Our results show that the export of nine proteins falls into three discrete kinetic classes: (i) a rapidly secreted class with an intracellular retention half-time of 30-40 min (albumin, fibronectin, alpha-fetoprotein and alpha 1-proteinase inhibitor), (ii) an intermediate secreted class with a half-time of 75-80 min (ceruloplasmin, alpha 2-macroglobulin and plasminogen), (iii) and a slowly secreted class with an intracellular retention half-time of 110-120 min (fibrinogen and transferrin). Our findings that there are three distinct kinetic classes of secretory proteins strongly suggests that intracellular transport is selective and that proteins of the same secretory class share structural features which influence their rate of export.
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PMID:Three secretory rates in human hepatoma cells. 299 May 78

Conditioned medium (CM) obtained from a human hepatoma cell line, SK-HEP-1, contains colony-stimulating factors (CSFs) active on murine and human bone marrow-derived granulocyte and macrophage colony-forming units (CFU-GM) and a factor capable of inducing granulocyte-macrophage differentiation (GM-DF) of murine myelomonocytic leukemic cells WEHI-3B(D+) and human promyelocytic leukemic cells HL-60 when assayed in semisolid agar cultures. The human active granulocyte-macrophage colony-stimulating factor (GM-CSF) for day 7 CFU-GM and the GM-DF for WEHI-3B(D+) and for HL-60 are not separable by acrylamide agarose column chromatography, eluting at an apparent molecular weight between 20,000 and 35,000 daltons, or by isoelectric focusing (isoelectric point, pH 5.4). In addition, SK-HEP-1 CM contains erythroid burst-promoting activity (BPA) and a factor that promotes the growth of human mixed colonies. SK-HEP-1 cells, which grow as an adherent monolayer, appear not to be endothelial or monocytic in origin since by immunofluorescent staining they are negative for Ia (HLA-DR), monocyte antigen 1 and 2, lysozyme, and factor VIII-related antigen. Positive immunofluorescent staining for keratin and fibronectin suggests the possibility that SK-HEP-1 is an epithelial cell line. Constitutive production of GM-DF as well as other hematopoietic activities including GM-CSF, erythroid BPA, and an activity that promotes the growth of human mixed colony progenitors by a human epithelial tumor cell line, SK-HEP-1, suggests that this cell line is a valuable resource for both large-scale production of these factors and the cloning of the gene(s) that code for these regulators.
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PMID:Constitutive production of leukemia differentiation, colony-stimulating, erythroid burst-promoting, and pluripoietic factors by a human hepatoma cell line: characterization of the leukemia differentiation factor. 299 Jun 10

An IgG1 monoclonal antibody, FDC-6, was established, which defines a unique fibronectin (FN) domain, located between the "Hep-2" and the "Fib-2" domains, in the COOH-terminal region of FNs isolated from hepatoma, sarcoma, and fetal fibroblasts. A systematic study with this antibody indicates the presence of two classes of human FNs. (i) FN from fetal connective tissue, placenta, amniotic fluid, hepatoma, and colon carcinoma as well as cell lines from fetal tissues (WI-38), hepatomas (HuH-6 and HuH-7), and sarcoma (VA13) was characterized by the presence of the FDC-6-defined domain and by a high molecular weight (subunit Mr, 310,000-335,000). (ii) In contrast, FN from normal adult tissues and plasma was characterized by a lower molecular weight (subunit Mr, 285,000-295,000) and lack of reactivity with FDC-6 and is therefore devoid of the FDC-6-defined domain. The FDC-6-defined domain is therefore called the "oncofetal" domain, and FN containing this domain is hereby called "oncofetal FN" (onf FN). The onf FN is similar to the previously known "cellular-form" FN. FN from normal adult tissues and plasma, lacking the oncofetal domain, is hereby called "normal FN" (nor FN). The nor FN is similar to the previously known "plasma-form" FN. Development of FN from fetal to adult form is associated with loss of the oncofetal domain defined by the FDC-6 antibody, and oncogenic transformation is associated with activation in synthesis of the oncofetal domain defined by the FDC-6 antibody.
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PMID:The oncofetal domain of fibronectin defined by monoclonal antibody FDC-6: its presence in fibronectins from fetal and tumor tissues and its absence in those from normal adult tissues and plasma. 299 69

Human serum spreading factor (SF) is a cell adhesion and spreading-promoting glycoprotein purified from serum or plasma that mediates effects in a wide variety of animal cell culture systems. HepG2 human hepatoma cells were found to synthesize and secrete SF into culture medium. Quantitative immunoassay of the protein indicated a concentration of about 1 microgram/ml in 48 hr-conditioned medium from confluent cultures. Although fibronectin also was synthesized and secreted into the culture medium, HepG2 cell spreading was observed in response to human serum SF, but not in response to human plasma fibronectin. Immunoprecipitation of SF from culture medium of cells metabolically-labeled with leucine, fucose or glucosamine identified a single form of the molecule of approximately 70,000 daltons. Treatment of cultures with tunicamycin inhibited incorporation of fucose and glucosamine into immunoprecipitated SF, but did not prevent synthesis and secretion of the protein. Electrophoretic analysis and cell spreading assays showed that SF secreted by tunicamycin-treated HepG2 cells was of molecular weight (mw) approximately 60,000, and was biologically active.
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PMID:Human spreading factor: synthesis and response by HepG2 hepatoma cells in culture. 299 38

Specific antibodies to fibronectin and type I collagen in rat livers were used to demonstrate these matrix proteins with direct immunoperoxidase method in paraffin sections of normal liver, DAB-induced hepatoma and CCl4-induced fibrotic liver. In normal livers, the immunoreactive products of both matrix proteins were found in the periportal regions, while the hepatocytes and most of the interstitial matrix remained unstained. The specimens obtained from DAB-treated liver showed a more intense reaction with fibronectin antibody in the perisinusoidal space including proliferated cholangiolar cells, as compared to no reaction with type I collagen antibody. In CCl4-fibrotic liver, apparent reactions were also found for both matrix proteins in the periportal interstitium and in progressing fibrotic area with severe fatty metamorphosis. These findings suggest that these matrix proteins have an advantage in the attempt to distinguish different patterns of neoplastic alteration in experimental rat livers.
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PMID:Distribution pattern of liver matrix proteins, fibronectin and type I collagen, in DAB-induced hepatoma of rat. 300 24

To evaluate the diagnostic accuracy of fibronectin levels in ascites to differentiate malignant from non-malignant ascites, the authors studied 30 patients with sterile uncomplicated ascites in chronic liver disease, 18 patients with malignant ascites and four patients with spontaneous bacterial peritonitis. Fibronectin concentration was significantly higher in malignant ascites than in sterile ascites (P less than 0.001). High values (greater than 85 mg/l) were found in four of six cases of hepatocellular carcinoma in liver cirrhosis with negative cytologic examination, and in six of seven peritoneal carcinomatoses. Low values (less than 85 mg/l) were found in four patients with liver metastases and in one patient with intrahepatic biliary duct carcinoma in cirrhosis. In four patients with infected ascites, the fibronectin level was low. Among all other parameters (total protein concentration, lactate dehydrogenase, gamma-glutamyl-transpeptidase, pH, amylase, triglycerides, leukocyte count, and cytologic examination), fibronectin yielded the best degree of discrimination (diagnostic accuracy, 79%).
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PMID:Diagnostic accuracy of fibronectin in the differential diagnosis of ascites. 302 17

In hepatocellular carcinoma, there is modification of cell-to-cell and cell-to-extracellular matrix interactions. Two cases of well-differentiated hepatocellular carcinoma that developed in noncirrhotic livers were explored by light and electron microscopy on perfusion-fixed liver biopsy specimens. In addition, immunocytolocalization of collagen types I, III, and IV, laminin, and fibronectin was assessed. The main features included the following: absence of collagen staining inside the tumor with Sirius red; decrease of collagen types I and III and the increase of collagen type IV, laminin, and fibronectin; widening of Disse's spaces containing numerous, discontinuous, and thick fragments of basement membrane-like material piled up beneath endothelial cells and around perisinusoidal cells; transformation of perisinusoidal cells into cells with the characteristics of fibroblasts and myofibroblasts; decreased numbers of fenestrae for endothelial cells with processes often overlapping and attached with tight junctions; and rarefaction of Kupffer's cells. Expression of cellular and extracellular material abnormalities are related to the tumor differentiation. The study of these abnormalities may have implications in prognosis.
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PMID:Hepatocellular carcinoma developed on noncirrhotic livers. Sinusoids in hepatocellular carcinoma. 302 15

The localization of fibronectin (FN) in human hepatocellular carcinoma (HCC) was studied in thirty-six HCC tumors (19 autopsy and 17 surgical specimens), two xenografted tumors of HCC to BALB/c mice and three HCC cell lines. The synthesis of FN was also examined in three HCC cell lines. FN was demonstrated on the endothelial surface of the blood spaces of cancerous tissue. Cytoplasmic and intercellular localization of FN was also observed. But there was no correlation between the localization pattern of FN and metastasis. In the two xenografted HCC tumors, FN was found in association with the blood vessels of the tumor tissue and between the HCC tumor cells. In all 3 HCC cell lines, FN was localized on the surface and in the cytoplasm of some HCC cells. FN was detected in the serum-free culture media of three HCC cell lines by immunoelectroblotting. The electrophoretic pattern of FN synthesized by these cell lines was different from that of plasma-FN and resembled that of cellular-FN synthesized by normal liver fibroblasts.
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PMID:Fibronectin in human hepatocellular carcinoma (HCC) and HCC cell lines. 303 89

A serum-free, hormone and attachment factor supplemented culture for rat H4 hepatoma cells was established. In the defined medium (Dulbecco's Modified Eagle's + Ham's F12 + insulin, transferrin, fibronectin liver cell growth factor, and sodium selenite), H4 cells grew equally well as in 10% fetal bovine serum supplemented medium. H4 cells in either defined or serum-containing culture conditions produce transferrin but not albumin or alpha-fetoprotein. In this paper we have studied the effect of various hormones and pressor peptides on the production of angiotensinogen by H4 cells cultured in defined conditions. Only glucocorticoid hormone had a significant effect on the production of angiotensinogen, whereas other hormones previously reported to exert their effect on angiotensinogen production had little or no effect.
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PMID:Control of angiotensinogen production by H4 rat hepatoma cells in serum-free culture. 329 26


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