Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0345904 (liver cancer)
 15,188 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

By means of immunohistochemical technique ABC, using monoclonal anti-transferrin receptor (TFR) antibodies WuT9 and OKT9, TFR expression in 30 cases of hepatocellular carcinoma (HCC) and in 6 cases of organs and tissues of normal human bodies was studied. It was revealed that large amount of TFR were expressed in liver cancer cells, but not in the surrounding mesenchymal cells as demonstrated by intense immunostaining in cancer nests, and even not in the surrounding mesenchyma of those HCC patients with negative AFP in their serum. In normal human body, only small amount of TFR in limited sites was found without free antigen in blood stream. Thus, it followed that TFR as a structural antigen of HCC was expressed with higher relative specificity than AFP, and TFR may be considered a tumor marker and therapeutic target of HCC.
 ...
PMID:[Immunohistochemical study of transferrin receptor expression in hepatocellular carcinoma]. 132 39

The expression of HBx protein in liver tissues from 48 cases of different liver diseases, including 32 cases of hepatocellular carcinoma (HCC), 10 of chronic hepatitis (CH), 2 of angioma and 4 cases of normal liver was studied. These samples were tested for HBx protein, HBsAg by modified ABC method. Positive rates of HBx in cancer and adjacent liver tissue were 75.0% and 62.5%, and positive rates of HBsAg were 37.5% and 78.1% respectively. The occurrence of HBx in the absence of HBsAg was more frequently observed in tissues from HCC (46.9%) than CH (0%). The results showed that expression of HBx was more active than that of HBsAg, and it is suggested that HBx might be a useful marker for the diagnosis of liver cancer.
 ...
PMID:[The HBx protein expression in liver cancer]. 165 95

Using 109 hepatocellular carcinomas (HCG), 34 cholangiocellular carcinomas (CCC), 4 mixed hepatocellular-cholangiocellular carcinomas (MHC) and 24 metastatic adenocarcinomas in the liver (MA), an immunohistochemical study on primary carcinoma of the liver was performed by means of the ABC method for carcinoembryonic antigen (CEA), epithelial membrane antigen (EMA), tissue polypeptide antigen (TPA) and keratin. The material consisted of surgical specimens of Kosin Medical College including 50 HCC, 17 CCC and 1 MHC, surgical specimens of 20 HCC from the University of Occupational and Environmental Health, Japan (UOEH) and autopsied specimens from UOEH that included 39 HCC, 17 CCC, 3 MHC and 24 MA. All the specimens were fixed with 10-15% formalin and embedded in paraplast manually at Kosin Medical College and by utilizing an automatic embedding machine with a decompressing procedure at UOEH. The antigenicity of TPA and keratin was preserved better in the specimens of Kosin Medical College than in those from UOEH. It is therefore assumed that manually embedded specimens are superior to specimens embedded by using an embedding machine with regard to the preservation of some antigenicities. The immunoreactivity of the 4 antigens in CCC cells was significantly higher than that in HCC cells, and the intracellular localization of antigens generally showed several characteristics in HCC and CCC. However, as the same localization of antigens is also seen in both HCC cells and CCC cells, it is considered that the immunohistochemical examination using plural antibodies is not always useful for a differential diagnosis between HCC and CCC, which is difficult in conventional sections. That TPA in HCC may be an oncodevelopmental antigen is suggested by the facts that the higher the grade of HCC, the higher the immunoreactivity of HCC cells, that hepatocytes with possible higher activity sometimes showed a positive reaction in the present study and that TPA is expressed in fetal hepatocytes in a fetus up to 20 weeks in the literature.
 ...
PMID:[An immunohistochemical study on primary carcinoma of the liver]. 248 71

Using the human liver cancer DNA transfected NIH/3T3 cell line, the human N-ras oncogene and the over expression of the oncoprotein P21ras was demonstrated, BALB/C mice were immunized. The spleen cells from the immunized mice were fused with SP2/0 myeloma cells. After the HAT medium selection and screening, two hybridoma cell lines, SCI-Oncogema 1 and 2, were established. In the immunoprecipitation test, the molecular weight of the protein reacting to Oncogema 1 was 21,000. This M.W 21,000 protein possessed the capability to bind with GTP, i.e. the character of P21ras. These data indicate that the Oncogema 1 is the monoclonal antibody against P21ras. Using Oncogema 1, specimens from 6 liver cancer patients were studied by immunopathology. With ABC stain, it was observed that the malignant cells in all the samples showed dark staining; the P21ras revealed over expression. Although the staining was heterogeneous, it implied that the ras oncogene was involved in the carcinogenesis of these six samples. No over expression was seen in the normal liver cells even in those around the cancerous lesion. However, dysplastic cells were moderately stained which means that the ras oncogene was activated and P21ras over expressed in these cells. The results suggest that the ras oncogene and P21ras play an important role in the early stage of liver cancer carcinogenesis.
 ...
PMID:[Localization of oncoprotein P21ras in the human liver cancer]. 330 83

C/EBP is a sequence-specific DNA-binding protein. In order to identify its distribution and localization, immunohistochemical technique (ABC method) was done using anti-C/EBP polypeptide antibodies 1103#, 425# in liver specimens from 20 normal adults, 5 neonates, 6 patients with hepatitis, 25 with liver cirrhosis, 80 with hepatocellular carcinoma (40 cases were associated with surrounding nontumorous tissues) and 26 patients with cholangiocarcinoma (15 cases were associated with surrounding nontumorous tissues). The results showed that C/EBP was diffusely distributed in nuclei and cytoplasm of differentiated liver cells and very low or undetectable in liver cancer cells. The manifestation of C/EBP correlated with degree of differentiation of tumour cells, and was obviously weaker than that in surrounding nontumorous tissues. C/EBP positive staining has also been found in regenerating epithelial cells of bile ductules. The results suggested that C/EBP should play an important role in establishing and maintaining the differentiation of liver cells.
 ...
PMID:Immunohistochemical demonstration of CCAAT/enhancer binding protein (C/EBP) in human liver tissues of various origin. 780 44

C/EBP is a sequence-specific DNA-binding protein. In order to identify its distribution, localization and function in liver specimens from 18 normal adult, 5 neonates and 79 hepatocellular carcinoma patients (40 cases associated with surrounding nontumorous tissues), immunocytochemical studies (ABC method) were performed by using anti-C/EBP polypeptide antibodies 1103#, 425#. Northern blot using synthesized C/EBP cDNA probe in liver tissues of 3 normal adult, one neonate and 10 hepatocellular carcinoma tissues (8 cases were associated with surrounding nontumorous tissues) were also studied. The results of immunocytochemical staining showed that C/EBP was diffusely distributed in nuclei and cytoplasm of differentiated liver cells and very low or undetectable in liver cancer cells. The expression of C/EBP was in proportion to the degree of tumor cell differentiation and was much less than in the nontumorous surrounding tissues. C/EBP positive staining has also been found in the regenerating epithelial cells of bile ductules. Northern blot examination matched closely with the immunocytochemical examination. The results suggest that C/EBP may play an important role in establishing and maintaining the differentiation of liver cells and may exert an inhibiting effect against transformation of liver cells and proliferation of neoplastic tissue.
 ...
PMID:[Determination and significance of C/EBP in hepatoma and various liver tissues]. 795 53

The question whether expression of drug metabolizing enzymes in human liver is altered by liver neoplasm remains controversial; however, the ability or unability of tumour cells to metabolize certain drugs may be important for developing therapeutic strategies. We therefore investigated the abundance and localization of two classes of drug metabolizing enzymes [cytochrome P4503A (CYP3A) and pi-type glutathione-S-transferase] by means of immunohistochemistry (standard ABC technique) in patients with hepatocellular carcinoma (HCC, n = 16) and with liver metastasis from adenocarcinoma (n = 53) in comparison to normal controls (n = 5). The distribution of CYP3A in normal liver samples showed a characteristic pattern of four to five layers of stained hepatocytes surrounding the central vein. Eleven out of 16 cases of HCC showed expression of CYP3A; staining was less intense than in normal liver and zonation was completely lost. In contrast, only 5 out of 53 samples of metastasis stained positively for CYP3A. The difference between primary and secondary neoplasm was statistically significant (chi-square, P < 0.0001). Pi-type glutathione-S-transferase (GST) stained positively in 9 out of 16 HCC and in 48 out of 53 cases of liver metastasis (chi-square, P < 0.01) indicating a higher percentage of immunostaining in liver metastasis. In summary, we observed differences in the abundance and distribution pattern of CYP3A and GST between primary and secondary neoplasma of human liver and in comparison to normal controls. In combination with established methods these data may contribute to the establishment of reliable test systems for distinguishing primary from secondary liver tumours.(ABSTRACT TRUNCATED AT 250 WORDS)
 ...
PMID:Differential expression of drug metabolizing enzymes in primary and secondary liver neoplasm: immunohistochemical characterization of cytochrome P4503A and glutathione-S-transferase. 840 68

Immunohistochemistry (ABC method) and in situ hybridization (DNA-RNA) were used to detect c-myc and p53 gene expression in tissues of human HCC and nearby non-tumorous liver (NT) from 23 patients. The results showed that the positive rates of P62c-myc were 87% (20/23) in HCC and 91% (21/23) in NT. The positive rates of P53 protein were 39% (9/23) in HCC as well as in NT. The positive rates of c-myc and p53 mRNA were 70% (16/23) and 56% (13/23) in HCC and NT respectively. The expression of c-myc and p53 at protein level was significantly correlated with that at mRNA level. These observations suggest a close association of c-myc and p53 gene overexpression with hepatocarcinogenesis. Immunohistochemistry (ABC method) on section of paraffin embedded tissue is a reliable method for detecting c-myc and p53 gene expression in HCC.
 ...
PMID:[Overexpression of c-myc and p53 gene in human hepato-cellular carcinoma--a study with immunohistochemistry and in situ hybridization]. 869 90

Cryosections of normal adult lung (n = 7) and pulmonary epithelial tumors, including squamous (n = 8), adeno (n = 8), bronchioloalveolar (n = 5), and large cell (n = 4) carcinomas (SCC, ACC, BAC, LCC), carcinoids (Cd, n = 7), and neuroendocrine carcinomas (NEC) of variable grades (n = 14) were immunostained by the avidin-biotin peroxidase (ABC) method with monoclonal antibodies to the alpha1-6 and alpha(v) and the beta1-4 integrin subunits. Normal adult alveolar septae showed variably intense immunoreactivity for alpha1,3,6 and beta1, whereas reactions for alpha5 and alpha(v) were weaker and uneven; the remaining integrin subunits were not detected. Bronchial and bronchiolar epithelium showed variably intense staining for alpha2.3,6,v and beta1,4. Reactions were often, though not invariably, basally polarized. SCC, ADC, and LCC showed variably intense reactions for alpha2.3,6,v and beta1,4. BAC were strongly and uniformly stained for alpha1.3 and beta1. In Cd, alpha1,2,3,v and beta1 reactions were noted, whereas in NEC, weak alpha1,3 and beta1 staining was detected with only traces of alpha6 and alpha(v). We conclude that alveolar epithelial cells do not express the hemidesmosome-associated, laminin-binding integrin alpha6beta4 of the bronchial epithelium but rather the alpha1beta1 and alpha3beta1, collagen IV, and laminin receptors, respectively. SCC, ADC, and sampled LCC express an integrin repertory qualitatively similar to that of the bronchial epithelium. Distinct from the latter, the integrin repertory of BAC parallels that of the alveolar epithelium by its strong expression of the multipotential alpha1beta1 and alpha3beta1 integrins. NEC tumors do not display the laminin receptors alpha6beta4 and alpha6beta1 shown by SCC and ADC but express instead alpha1beta1, a collagen IV-laminin receptor rarely found in epithelial neoplasms except for BAC. In NEC tumors, integrins, especially alpha2, decrease with dedifferentiation. Notably distinct from epithelial mesotheliomas, the major fibronectin-binding integrin alpha5beta1 was not found in any type of lung carcinoma.
 ...
PMID:Immunolocalization of integrins in the normal lung and in pulmonary carcinomas. 930 25

The level of sulfo-Lea (SO3-3Gal beta 1-3(Fuc alpha 1-4)GlcNAc) epitope recognized by monoclonal antibody (mAb) 91.9H in hepatic metastasis of colon carcinoma is known to be lower than at the primary sites. We examined 19 human colon carcinoma cell lines for their production of this epitope. Sixteen cell lines were found to produce high M(r) components that metabolically incorporated [35S]sulfate and were resistant to heparitinase I and chondroitinase ABC, and 8 of them were reactive with mAb 91.9H as shown by western blotting analysis. These were all of the 4 cell lines derived from well differentiated primary tumors (HCCP-2998, LS174T, GEO, and CBS), 2 of 10 cell lines (DLD-1 and HCT116) from moderately to poorly differentiated primary tumors, and 2 of 5 cell lines (SW480 and HCC-M1544) from metastases. Incubation of LS174T cells with benzyl-N-acetyl-alpha-D-galactosaminide abrogated the incorporation of [35S]sulfate and the reactivity of mAb 91.9H with high M(r) components in the cell lysates. Sodium chlorate, which inhibits the formation of 3'-phosphoadenosine 5'-phosphosulfate, also inhibited the [35S]sulfate incorporation and reactivity with mAb 91.9H. These treatments did not change the incorporation of [14C]threonine into high M(r) components. These results indicated that sulfo-Lea epitopes were expressed on O-linked carbohydrate chains in sulfomucins. Immunohistochemical studies of tumor tissues in nude mice indicated that sulfo-Lea was expressed at the site of orthotopic transplantation in the cecum. The expression appeared to be suppressed in liver metastatic foci in nude mice.
 ...
PMID:Expression of mucin-associated sulfo-Lea carbohydrate epitopes on human colon carcinoma cells. 1008 87


1 2 3 Next >>