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)

A newly synthesized mycophenolic acid (MPA) derivative, ethyl O-[N-(p-carboxyphenyl)-carbamoyl]-mycophenolate (CAM, NSC-297879D) was tested for antitumor activity, when given orally, against transplantable murine tumors. The compound was markedly effective against transplantable murine tumors. The compound was markedly effective against leukemia P388 and L1210, lymphoma L5178Y, mastocytoma P815 and sarcoma Meth-A, moderately effective against sarcoma-180, C3MC2 and BAMC1, Ehrlich carcinoma, Lewis lung carcinoma and melanoma B16 and marginally effective against hepatoma MH134. The antitumor effects were manifested not only in growth inhibitory effects on subcutaneously transplanted tumors but also in the prolongation of life span of mice int which the tumors had been inoculated intraperitoneally or subcutaneously. The growth of primary transplants of a mammary tumor which developed spontaneously in a C3H/He mouse was inhibited by consecutive administration of CAM frm the 34th day after the transplantation. Oral CAM was more potent than its mother compound, MPA, in the tumor models examined. These results indicate that orally administered CAM has a wide antitumor spectrum.
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PMID:Antitumor activity of a new compound, ethyl O-[N-(p-carboxyphenyl)-carbamoyl]-mycophenolate, against various experimental tumors upon oral administration. 727 50

Tumors of various histological patterns (squamous-cell carcinoma of uterine cervix SCC. Lewis lung carcinoma, hepatoma-22a, mammary adenocarcinoma-755, sarcoma-180 and hemocytoblastosis La) were transplanted in mice aged 3, 12-18 months. Tumor SCC, hepatoma-22a, sarcoma-180 and adenocarcinoma-755 grew faster in older animals (18 months) than in younger one (3 months), while Lewis lung carcinoma and hemocytoblastosis La developed at the same rate in old and young animals. It is suggested that tumor growth in senescent organism is determined by both hormono-metabolic shifts, degree of immunologic vigor and a number of biological characteristics of tumor.
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PMID:[Effect of age on the growth of transplantable tumors in mice]. 728 93

A new platelet aggregation inhibitor compound, 5-(2-chlorobenzyl-4,5,6,7-tetrahydrothieno[3,2-C]pyridine hydrochloride (ticlopidine), was examined for its inhibitory effects on blood-borne metastasis using three different rodent tumors (B16 melanoma, Lewis lung carcinoma, and rat ascites hepatoma, AH130). Ticlopidine was administered p.o. to the rodents. It inhibited the aggregation of platelets induced by adenosine diphosphate, thrombin, crude extract of AH130, and viable AH130 and B16 melanoma cells and also resulted in a significant decrease of pulmonary metastasis induced by i.v. injection of B16 melanoma and AH130. Spontaneous pulmonary metastasis of Lewis lung carcinoma was also inhibited by p.o. administration of ticlopidine. This new compound may be a useful agent for inhibiting platelet aggregation caused by various agents and for suppressing hematogenous pulmonary metastasis.
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PMID:Effects of 5-(2-chlorobenzyl)-4,5,6,7-tetrahydrothieno[3,2-c]pyridine hydrochloride (Ticlopidine), a platelet aggregation inhibitor, on blood-borne metastasis. 730 88

Adrenal 4 binding protein (Ad4BP) is a transcription factor that regulates the expression of the steroidogenic enzymes and is expressed primarily in steroidogenic cells. We immunolocalized Ad4BP in adrenocortical carcinoma (eight cases) and various malignancies that histologically simulate an adrenocortical carcinoma to evaluate the value of Ad4BP as an immunohistochemical marker of adrenocortical carcinoma. These malignancies examined were renal cell carcinoma (20 cases), hepatocellular carcinoma (10 cases), malignant melanoma (eight cases), ovarian (six cases) and uterine (three cases) clear cell carcinoma, large cell carcinoma of the lung (five cases), and pheochromocytoma (three cases). Nuclear Ad4BP immunoreactivity was observed only in adrenocortical carcinoma cases but not in other tumors examined. Almost all of the adrenocortical carcinoma cells were immunohistochemically positive for Ad4BP including cells associated with bizarre nuclei. These results show that application of Ad4BP immunostain can contribute greatly to the differential diagnosis of adrenocortical carcinoma.
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PMID:Transcription factor adrenal 4 binding protein as a marker of adrenocortical malignancy. 755 51

The human hepatoma cell line G2 (Hep G2) has been compared to lung carcinoma, sarcoma and skin fibroblasts for the expression of intermediate filaments, i.e. vimentin and cytokeratin. The immunofluorescence study revealed that, in contradiction to Szecheng et al. (1987), cytokeratin and vimentin are absent in Hep G2. Human skin fibroblasts and sarcoma cells expressed vimentin as expected for their mesenchymal origin, but a positive reaction to vimentin could also be shown in lung carcinoma cells. However, the vimentin filament structure of both these tumour cell lines was different in comparison with skin fibroblasts. Therefore determining the exact tissue origin of tumour cell lines by means of intermediate filament characterization remains doubtful.
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PMID:Characterisation of human tumour cell lines using antibodies to intermediate filaments. 769 76

The expression pattern of E- and P-cadherin in human carcinomas has been reported by many laboratories. However, little is known about the involvement of other cadherin types in human carcinomas. cDNA clones for a cadherin molecule were isolated from a cDNA library of human hepatocellular carcinoma cells which lacked E- and P-cadherin expression but exhibited cell aggregation activity mediated by an unknown cadherin, and they were subjected to sequence analysis. The overlapped clones covered 4315 nucleotides and were found to encode a typical cadherin molecule consisting of 790 amino acids. Since the deduced amino acid sequence was identical to a partially available human cadherin-6 sequence except for two amino acid residues, the clones were considered to be human cadherin-6 cDNAs encoding the entire open reading frame. The deduced amino acid sequence also showed extremely high homology with recently reported rat K-cadherin, 97% for the putative mature protein, suggesting that cadherin-6 is the human counterpart of rat K-cadherin. Expression of cadherin-6 in various human normal tissues and carcinoma cells was examined by Northern blot analysis using a specific probe corresponding to the signal and precursor sequence. Among normal tissues examined, brain, cerebellum, and kidney showed strong expression of cadherin-6, whereas lung, pancreas, and gastric mucosa showed weak expression. Transcripts of cadherin-6 were not detected in normal liver, whereas four of six hepatocellular carcinoma cell lines examined expressed cadherin-6 abundantly. As reported for rat K-cadherin, three renal carcinoma cell lines also expressed cadherin-6 strongly. The most interesting finding was obtained for small cell lung carcinoma lines. Among 15 of such cell lines examined, all of 11 cadherin-6-positive lines were classified into the classic type, whereas the negative cell lines were all of the variant type. The present results suggest that besides E- and P-cadherin, other cadherin molecules are expressed in human cancers and are responsible for additional biological properties of the carcinoma cells.
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PMID:Isolation and sequence analysis of human cadherin-6 complementary DNA for the full coding sequence and its expression in human carcinoma cells. 774 25

Cell surface ATPase (ectoATPase) activity is detected on many mammalian cells. Previous documentation in the rat hepatocyte-hepatoma system indicated that ectoATPase activity increased during tumorigenesis with accompanying changes in enzymatic properties and localization. These results, combined with the recently established characteristics of two distinct ectoATPases, a mercurial-sensitive ectoATPase, and a mercurial-insensitive ectoATPase, suggest that the former is increased, whereas the latter is decreased, during hepatoma formation. We found that the mercurial-sensitive ecto-ATPase was also expressed at high levels in three lines of human small cell lung carcinoma (SCLC) cells. During purification of this enzyme from an SCLC xenograft, four isoforms of this enzyme, with similar biochemical properties but different ionic charges were detected. The elution of two proteins of 170 and 150 kDa from a DEAE-cellulose column appeared to correlate with elution of ATPase activity. These characterizations should be useful in the further investigation of the molecular structure and function of the SCLC mercurial-sensitive ectoATPase which may be an important cell surface marker of SCLC cells.
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PMID:Prevalence of the mercurial-sensitive EctoATPase in human small cell lung carcinoma: characterization and partial purification. 797 96

In an earlier phase I study, we reported that the maximal tolerated dose (MTD) of prochlorperazine (PCZ) given as a 15-min i.v. infusion was 75 mg/m2. The highest peak plasma PCZ concentration achieved was 1100 ng/ml. The present study was conducted to determine if PCZ levels high enough to block doxorubicin (DOX) efflux in vitro could be achieved and sustained in vivo by increasing the duration of i.v. infusion from 15 min to 2 h. The treatment schedule consisted of i.v. prehydration with at least 500 ml normal saline (NS) and administration of a fixed standard dose of 60 mg/m2 DOX as an i.v. bolus over 15 min followed by i.v. doses of 75, 105, 135, or 180 mg/m2 PCZ in 250 ml NS over 2 h. The hematologic toxicities attributable to DOX were as expected and independent of the PCZ dose. Toxicities attributable to PCZ were sedation, dryness of mouth, anxiety, akathisia, hypotension, cramps, and confusion. The MTD of PCZ was 180 mg/m2. Large interpatient variation in peak PCZ plasma levels (91-3215 ng/ml) was seen, with the plasma half-life (t1/2 alpha) being approximately 57 min in patients given 135-180 mg/m2 PCZ. The volume of distribution (Vd), total clearance (ClT), and area under the curve (AUC) were 350.1 +/- 183.8 1/m2, 260.7 +/- 142.7 l m2 h-1 and 1539 +/- 922 ng ml h-1, respectively, in patients given 180 mg/m2 PCZ and the respective values for patients receiving 135 mg/m2 were 48.9 +/- 23.76 l/m2, 33.2 +/- 2.62 l m2 h-1, and 4117 +/- 302 ng ml h-1. High PCZ plasma levels (> 600 ng/ml) were sustained in all patients treated with 135 mg/m2 PCZ for up to 24 h. DOX plasma elimination was biphasic at 135 and 180 mg/m2 PCZ, and a > 10-ng/ml DOX plasma level was maintained for 24 h. Partial responses were seen in three of six patients with malignant mesothelioma, in two of ten patients with non-small-cell lung carcinoma, and in the single patient with hepatoma. Our data show that PCZ can be safely given as a 2-h infusion at 135 mg/m2 with clinically manageable toxicities. The antitumor activity of the combination of DOX and PCZ needs to be confirmed in phase II trials.
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PMID:Phase I and pharmacokinetics studies of prochlorperazine 2-h i.v. infusion as a doxorubicin-efflux blocker. 807 4

Molecular weight of human hepatocellular carcinoma (HCC)-associated antigen-HL2 antigen was detected to be about 50,000 dalton by SDS-PAGE and Western blot. One hundred and twenty-seven paraffin sections of cancers and pathological liver tissue were tests by ABC immunohistochemical staining. MAb HL2 reacted with 62.7% HCC and also with 8 of the 10 stomach carcinomas but only with a few other digestive system carcinomas (pancreas carcinoma, rectum carcinoma and duodenum carcinoma) and hepatitis. MAb HL2 was negative in hepatocirrhosis and other tumors (vesica carcinoma, skin carcinoma, breast carcinoma, neurogliocytoma and carcinoma of the lung). The results suggest that MAb HL2 has values in diagnosis of HCC and differential diagnosis between HCC and other tumours. HL2 antigen might be a new tumor-associated antigen (TAA). Further study of HL2 antigen will significantly show the actions of TAA in the occurrence and development of tumor.
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PMID:[Immunohistochemical observation of anti-human hepatocellular carcinoma monoclonal antibody HL2 in cancers]. 807 Jul 68

We previously characterized and cloned a unique human hepatic dihydrodiol dehydrogenase (DDH) that exhibits high affinity binding for bile acids (Stolz, A., Hammond, L., Lou, H., Takikawa, H., Ronk, M., and Shively, J. E. (1993) J. Biol. Chem. 268, 10448-10457). This hepatic dihydrodiol dehydrogenase demonstrates significant sequence homology with the cytosolic rat bile acid binder 3 alpha-hydroxysteroid dehydrogenase and other members of the monomeric oxidoreductase gene family. We now report the genomic organization and chromosomal localization of the human hepatic DDH in order to further define its physiological role and provide additional insight into the development of this gene family. The 15-kilobase human hepatic DDH gene was contained in an overlapping cosmid and lambda genomic clones and is composed of nine exons. A major transcriptional start site was determined to be 30 base pairs upstream from the ATG initiation methionine by both primer extension and S1 nuclease mapping studies. The human hepatic DDH gene was mapped by chromosomal in situ hybridization and analysis of human-mouse somatic cell hybrids to the tip of the short arm of chromosome 10 at p14. Strict conservation of the intron-exon junctions in the human hepatic DDH and two other members of the monomeric oxidoreductase gene family, aldose reductase and mouse major vas deferens protein suggests evolution from a common ancestral gene. Human hepatic DDH mRNA was identified in both human hepatoma Hep G2 and human lung carcinoma cell line NCI-H322 by RN'ase protection; thus, these cell lines will be useful in examining the regulation of the gene.
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PMID:Genomic organization and chromosomal localization of a novel human hepatic dihydrodiol dehydrogenase with high affinity bile acid binding. 813 67


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