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)

Erythrocytosis (polycythemia) is a well-described paraneoplastic phenomenon in patients with hepatocellular carcinoma, but its pathogenesis remains uncertain. Using a radioimmunoassay, we have measured serum erythropoietin concentrations in 65 southern African blacks with this tumor and 61 matched controls. Four patients had an increased hemoglobin concentration and packed cell volume, and the remainder had normal values. Twenty-three percent of the patients with hepatocellular carcinoma (15/65) were found to have raised serum erythropoietin concentrations, the values ranging up to 344 mu/ml. Only one of these patients had an increased hemoglobin concentration and packed cell volume. This apparent anomaly could be explained if the erythrocytosis that would normally result from high serum erythropoietin values had been counteracted by the inhibition of erythropoiesis which occurs in advanced malignant disease. Alternatively, the erythropoietin produced by the tumor might not always be biologically active. Three patients had increased hemoglobin values and packed cell volumes in the presence of normal serum erythropoietin concentrations. One of these patients was hypoxic as a result of multiple pulmonary metastases, and the others may also have been. There was no correlation between serum erythropoietin and alpha-fetoprotein concentrations in individual patients.
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PMID:Serum erythropoietin concentrations in patients with hepatocellular carcinoma. 242 57

To evaluate the worth of intra- and postoperative blood transfusion in cirrhotic patients undergoing resection for hepatocellular carcinoma, we compared 13 patients receiving transfusions and 14 matched contemporary patients who did not receive blood. Preoperative hematological and biochemical parameters, the type and extent of liver resection, and the mean blood loss (862 and 870 ml) were similar in the 2 groups. The total volume of intra- and postoperative blood transfused ranged from 400 to 1,800 ml (mean, 1,223 ml) in the patients receiving transfusions. During various postoperative time intervals, the mean values of hematocrit, hemoglobin, serum total bilirubin, and lactic dehydrogenase activity were significantly higher in the patients who were transfused compared to those who were not. Mean serum transaminase activities were similar in the 2 groups at the same times. The mean hematocrit values decreased from 36.8% preoperatively to a postoperative minimum of 27.0% in the transfused group, and from 39.9% to 26.1% in the nontransfused group. Our experience and theoretical reasons have led us to withhold blood transfusion until the hematocrit values fall below 30% during hepatectomy and below 20% in the postoperative period (or unless circulatory instability cannot be corrected otherwise). Fresh frozen plasma is preferred for volume substitution and, if blood has to be given, only up to 60-70% of estimated losses should be replaced by fresh blood.
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PMID:Restrictive versus liberal blood transfusion policy for hepatectomies in cirrhotic patients. 255 98

The cellular uptake and lysosomal accumulation of 67Ga-labelled transferrin within tumors of different malignancy were examined using tissue fractionation and immunological techniques. As tumor models the slowly growing Morris hepatoma 5123 C, the moderately growing Novikoff hepatoma and the fast and aggressive Yoshida hepatoma AH130 were investigated. Isolation of subcellular fractions of tumor homogenates was performed by differential centrifugation and density-gradient centrifugation. The intracellular 67Ga-transferrin was found to be highly concentrated within the purified lysosomes. The transferrin within the lysosomal fraction was identified by radial immunodiffusion technique using monospecific antiserum. The accumulation of 67Ga-transferrin by the tumors resulted in a faster disappearance of 67Ga-transferrin from the blood. This loss of circulating 67Ga-transferrin correlated with the proliferation activity and the spread of the tumors. Since transferrin is indispensible for the utilization of iron by the heme-synthesizing red cell precursors, transferrin concentration in the blood is the limiting factor for the utilization of iron in hemoglobin synthesis. Thus, in a further series of experiments we investigated the development of anemia in tumor-bearing rats. With increasing tumor mass a progressive fall of hemoglobin concentration was found. The anemia was more severe in the faster growing Novikoff hepatoma than in the slowly growing Morris hepatoma. The most significant reduction of hemoglobin concentration was found in the very fast growing Yoshida hepatoma. After total tumor resection hemoglobin concentration and red blood cell count normalized completely within 6-8 weeks. We conclude from these data that the uptake of transferrin by the tumor cells results in a faster disappearance of transferrin from the blood.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Anemia in malignant tumor diseases. II. Tumor-induced loss of transferrin as a cause of the development of anemia based on a rat model]. 260 49

A cell line, CY-1, was selected in tyrosine free (tyr-) medium after fusion of mouse erythroleukemia (MEL) cells with mitomycin C-treated rat hepatoma cells. MEL cells do not express the enzyme phenylalanine hydroxylase (PH) and are unable to grow in tyr- medium, whereas the rat hepatoma cells constitutively express PH and are able to grow in tyr- medium. CY-1 cells resemble MEL cells morphologically, karyotypically, and in being inducible for hemoglobin synthesis. In contrast to MEL cells, CY-1 expresses PH and is therefore able to grow in tyr- medium. Using a rat cDNA probe for the PH gene, Southern blot analyses were carried out on DNA isolated from CY-1 and parental cells. CY-1 showed the characteristic mouse PH gene pattern but the gene copy number was amplified four- to eightfold compared to parental MEL cells.
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PMID:Amplification and expression of phenylalanine hydroxylase in mouse erythroleukemia cells. 298 35

The relationship of serum ferritin and transferrin levels to risk of cancer was examined in a population of 21,513 Chinese male government workers in Taiwan who have been followed prospectively since 1975. On the basis of a previous study in the Solomon Islands, increased ferritin and decreased transferrin levels were predicted for those men who developed cancer. The results were consistent with the prediction. The mean serum ferritin was higher at the start of the study in 192 men who had died of cancer or who had developed primary hepatocellular carcinoma (PHC) as of July 1983, as compared to their controls. The mean serum transferrin level was lower in men who had died of cancers other than PHC. The estimate of relative risk of cancer death for a man with 200 ng ferritin/ml and 200 mg transferrin/dl, as compared to a man with levels of 20 ng/ml and 400 mg/dl, respectively, is 2.9. These serum iron-binding protein levels are at the extremes of the "normal" range. Men who subsequently died of cancer had lower hemoglobin, lower hematocrit, lower albumin, and higher globulin levels at the start of the study than did the controls. These results are consistent with the hypothesis that increased iron stores increase the risk of cancer. However, direct assessment of iron stores prior to disease was not possible, and the same constellation of findings may be consistent with other explanations.
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PMID:Iron-binding proteins and risk of cancer in Taiwan. 300 43

A high-molecular-weight proteinase in rat ascites hepatoma AH109A cells was purified to apparent homogeneity by conventional chromatographic techniques. The purified proteinase degraded over the broad pH range, 7.0-9.0, not only denatured hemoglobin but also type I and IV collagen in the absence of calcium. Its activity was maximum at pH 8.0, heat-labile and affected by thiol reagents. Serine proteinase inhibitors such as diisopropyl fluorophosphate, soybean trypsin inhibitor, leupeptin, and antipain also partially inhibited its activity. The enzyme was found mainly in the cytosol fraction, and had a molecular weight of 450 kilodaltons (Kd) as determined by gel filtration chromatography and showed a single band on polyacrylamide gel electrophoresis under nondenaturing condition, although it was dissociated into lower-molecular-weight subunits, 25.5-32 Kd in the presence of sodium dodecyl sulfate and 2-mercaptoethanol. These properties suggested that it was a kind of a cytosolic high-molecular-weight proteinase. The collagenolytic activity of this proteinase may play an important role in cancer cell invasion and metastasis.
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PMID:High-molecular-weight neutral proteinase of rat ascites hepatoma cells and their collagenolytic activity. 305 24

Activity of neutral protease was increased in sera of rats bearing ascites hepatoma AH109A compared to those of normal rats. The protease was isolated from serum protein and partially purified approximately 1,150 times in specific activity after sequential column chromatography of hemoglobin affinity, lysine-Sepharose, Ultrogel AcA34 and TSK-gel G2000SW in that order. The protease fraction still seemed to contain at least two kinds of proteases, serine and cysteine protease. It had a molecular weight of 18-21 kilodaltons with broad optimal pH range of 7.0-9.0, maximum at 8.0. Intradermal injection of the crude preparation of the neutral protease fraction induced extravascular emigration of circulating tumor cells in vivo. Moreover, partially purified protease degraded pepsin-treated chains of bovine glomerular type IV collagen in vitro, but such an in vitro action of the protease was inhibited by an addition of soybean trypsin inhibitor or mercuric chloride. It failed to cleave salt-extracted rat skin type I collagen under the same digestive conditions for bovine type IV collagen. The serum neutral proteases of tumor-bearing host may play some cooperative roles during extravascular emigration of tumor cells by destruction of vascular basement membrane.
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PMID:Partial purification and characterization of serum protease from tumor-bearing rats which cleaves type IV collagen. 353 Oct 79

Forty patients with hepatoma and metastatic tumors of liver were treated with rapid arterial infusion administered simultaneously using 30-40 mg of adriamycin and 10-20 mg of mitomycin C into the hepatic artery by Seldinger catheter. They were 16 patients with breast cancer, 21 with gastrointestinal tumors including hepatoma; 6, gastric cancer; 5, colon cancer; 7, gallbladder cancer; 2, pancreas cancer; 1, and three with other malignancies, respectively. Partial responses were obtained in 14 of 40 patients (35%). The response rate in patients with breast cancer was 44% (7/16), while it was 29% (6/21) with gastrointestinal tumors. The median duration of response was relatively short, being 3.5 months in the former patients and 2.3 months in the latter patients. The median duration of survival was 4.0+ months. The results indicate that this arterial infusion therapy is one of the useful treatments in the management of malignant tumors of the liver. Leukopenia less than 4 x 10(3)/cmm was seen in 63%, while thrombocytopenia less than 100 x 10(3)/cmm in 38%, and decreased hemoglobin value of more than 2 g/dl in 13%, which were quite tolerable. Gastrointestinal symptoms and hair loss were milder than those from systemic chemotherapy. Renal toxicity was seen in three patients, and two patients died of renal failure, thus the renal toxicity, which may be related to contrast media as well as anticancer agents, should be carefully prevented by proper hydration.
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PMID:[Arterial infusion of combination chemotherapy using adriamycin and mitomycin C for hepatoma and metastatic tumors of the liver]. 630 77

A radioimmunoassay available for human aldolase A was developed for the direct quantification of aldolase A in human serum and tissues. The method was a double antibody technique using radio-iodinated purified aldolase A, chicken antibody to aldolase A, and rabbit antibody to chicken IgG. This radioimmunoassay was specific for the aldolase A subunit, with no cross-reactivity with human aldolase B subunit or human aldolase C subunit. Aldolase A was predominantly high in skeletal muscle, and relatively high in brain and cardiac muscle. Normal liver tissue contains only a small amount of aldolase A, whereas aldolase A predominates in liver cell carcinoma tissue. Aldolase A levels in the sera of normal subjects were 171 +/- 39 ng/ml (mean +/- 2SD). Aldolase A levels correlated closely with hemoglobin levels, so aldolase A levels were increased in the sera with hemolysis. Since skeletal muscle is the largest origin of aldolase A in any tissue, serum aldolase A levels were increased in patients with acute muscle injury due to abdominal operation and even in healthy subjects after hard exercise. Serum aldolase A levels in almost all of non-cancer patients of the digestive tract were less than 210 ng/ml. In contrast, about 80% of patients with cancer in the digestive tract showed increased serum aldolase A levels. Aldolase A levels were remarkably increased in the sera of cancer patients with distant metastasis. The CEA levels were increased only in 46% of the sera of patients with cancer in the digestive tract, whereas the aldolase A levels were increased in 86% of the patients. The AFP levels were higher than 100 ng/ml in 76% of the sera of 21 patients with liver cell carcinoma, whereas the aldolase A levels were markedly increased in 90% of them. From these results, it may be suggested that the determination of serum aldolase A by radioimmunoassay is a useful tool in the clinical diagnosis of cancer patients with cancer in the digestive tract.
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PMID:[Determination of aldolase A by radioimmunoassay. Experimental and clinical studies on the diagnosis of cancer of the digestive tract]. 631 5

In 15 patients with hepatocellular carcinoma (HCC) and 14 patients with liver cirrhosis (LC), urinary excretions of delta-aminolevulinic acid (ALA), porphobilinogen (PBG), uroporphyrin (UP), coproporphyrin (CP), and erythrocyte contents of CP and protoporphyrin (PP) were examined. In patients with HCC, urinary excretions of ALA and PBG and erythrocyte contents of CP and PP were not increased, but urinary excretions of UP and CP were significantly increased more than those of LC patients. Urinary excretions of UP and CP had no correlations with liver function tests and excretion of UP correlated slightly with blood hemoglobin level. After administration of ALA intravenously, urinary excretions of UP and CP were clearly increased in patients with HCC compared to normal controls. A Red fluorescent area was present at the cancerous area but not in the noncancerous cirrhotic area in a patient with HCC. These results suggest that aberrant porphyrin metabolism occurred in patients with HCC compared to other liver diseases.
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PMID:Aberrant porphyrin metabolism in hepatocellular carcinoma. 632 59


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