Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0242379 (lung cancer)
 71,905 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Five known cardenolides, digitoxigenin (1), oleandrigenin (2), digitoxigenin alpha-L-cymaroside (3), digitoxigenin beta-gentiobiosyl-alpha-L-cymaroside (4), and delta 16-digitoxigenin beta-D-glucosyl-alpha-L-cymaroside (5), were isolated from the stems of Beaumontia brevituba Oliver by cytotoxicity-directed fractionation monitored by a cultured human lung cancer cell line. The cytotoxic activity of these compounds was evaluated with a panel of twelve human and murine cancer cell lines. The lignan glycoside, syringaresinol beta-D-glucoside, was obtained for the first time in the form of its levo-enantiomer.
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PMID:Cytotoxic activity of cardenolides from Beaumontia brevituba stems. 147 Jun 66

Using positron emission tomography, we studied the tumor uptake of 18F-2-fluoro-2-deoxy-D-glucose (18FDG) in five lung cancer patients before and after anti-cancer therapy (radiotherapy and/or chemotherapy). The tumor uptake of 18FDG was classified as positive and negative; the former, by increasing the uptake of 18FDG with time, and the latter, by decreasing or the constant uptake of 18FDG. Before therapy, all cases tested positive. After therapy, three cases were negative and two cases remained positive. All negative cases corresponded to complete second 18FDG study. Our findings in the 18FDG study correlate with the clinical results. 18FDG is a promising method for assessing therapeutic effects on cancer clinically.
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PMID:Clinical assessment of therapeutic effects on cancer using 18F-2-fluoro-2-deoxy-D-glucose and positron emission tomography: preliminary study of lung cancer. 217 Mar 2

Total sialic acid (TSA), lipid-bound sialic acid (LSA), hexoses (galactose and mannose) and mucoid proteins were analyzed by specific chemical methods from sera of 43 patients with lung cancer and 5 cases of benign lung diseases. The levels were compared with similar values obtained from 25 healthy individuals. The four biomarkers were significantly elevated in lung cancer patients as compared to controls as well as benign conditions (p less than 0.001). TSA, LSA and the hexoses levels were significantly higher in benign conditions as compared to controls (p less than 0.001, p less than 0.05, and p less than 0.001, respectively). Adenocarcinoma patients had lower mean values of all the four biomarkers than squamous-cell and small-cell carcinoma patients. Increased levels of LSA in squamous-cell carcinoma and TSA in small-cell carcinoma were statistically also significant as compared to adenocarcinoma (p less than 0.01 and p less than 0.05, respectively). LSA showed higher mean values in metastatic cancer than in primary lung cancer. The combination of these markers might be useful for differentiation between benign and malignant conditions and also for the diagnosis of metastatic lung cancer.
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PMID:Significance of serum sialoglycoproteins in patients with lung cancer. 253 69

A high molecular weight, mucous glycoprotein (MG) from the pleural fluid of lung adenocarcinoma was purified by the DEAE-cellulose, gel-filtration and wheat germ agglutinin affinity chromatography. Protein portion of the molecule was composed of amino acids rich in serine, threonine and proline, but methionine and tyrosine concentrations were relatively low. About 65% of the weight, was composed of galactose, galactosamine, glucosamine, fucose and sialic acid. The gel-filtration pattern on Sepharose 4B revealed Mr greater than 10(6) Da. The SDS-PAGE pattern revealed a main band at the position of the Mr about 350 kDa under the reducing condition. Rabbit antibody against this molecule recognized mainly the peptide portion, and the radioimmunoassay (RIA) using the double antibody method was developed by this antibody. Serum MG level was low in healthy subjects and in benign diseases (0.8 +/- 0.7 U/ml; mean +/- SD and 1.1 +/- 2.3 U/ml, respectively). Thus, 3 U/ml was used as the cut-off value. The mean of serum MG levels and positive rates in malignant diseases were significantly high; 4.4 U/ml and 32.3% in lung cancer, 20.1 U/ml and 77.5% in pancreas cancer 11.6 U/ml and 64.3% in gastric cancer, 12.9 U/ml and 57.1% in hepatoma, 12.3 U/ml and 77.8 in colon cancer. Other malignancies such as ovarial and uterus cancer showed also high levels. Elevated values in these malignancies were observed frequently in patients with metastasis. On the other hand, the false positive cases were found in 10% of benign diseases. Determination of MG seems to be useful for the detection of several kinds of malignancies, but it is not adequately sensitive as a screening method for early cancer detection.
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PMID:Clinical significance of mucin-like high molecular weight glycoprotein originated from lung cancer as tumor marker. 274 68

The cell surface glycoprotein (GP) profiles of cell lines representing the four major histopathological lung cancer entities, squamous cell (SQC)-, small cell (SCC)-, adeno (ADC)-, and large cell carcinoma (LCC), and two primary cultures of SCC and LCC, respectively, have been examined by the galactose-oxidase tritiated sodium-borohydride cell surface labelling method, The SCC specimens (five cell lines and one biopsy) had a characteristic pattern of major surface GPs, with common GPs at apparent molecular weights (MWs) of 54 -kilo (k) Daltons (D) and 88 kD, which was discriminative from the group of non-SCC (SQC, ADC and LCC). The non-SCC group constantly expressed GPs at apparent MWs of 80 kD and 110 kD, both as established cell lines and in the primary LCC culture. The GP patterns of the SCC cell lines and the LCC cell line were retained in comparison to corresponding primary biopsy material. The propagation of an established SCC cell line without supplementation of serum did not alter the GP expression at the cell surface. Taken together, the surface GP patterns for SCC versus non-SCC appear to be reliable and reproducible markers for these tumor entities, both in biopsy material and in established cell lines.
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PMID:Surface-glycoprotein patterns of established human lung cancer cell lines and primary cultures. 299 48

A monoclonal antibody (5E8) has been used to identify and structurally characterize a previously unreported macromolecule present on the surface of human lung tumors. This antibody was derived from a hybrid clone that was produced using spleen cells of mice immunized with a surgically excised squamous cell carcinoma. Using immunofluorescence, the 5E8 antibody was observed to stain many different human lung tumor cell lines and surgically excised human lung tumors including squamous cell carcinomas, adenocarcinomas, alveolar carcinomas, and a portion of the large cell tumors tested. With few exceptions, notably the basal layer of the skin, little or no detectable staining of 5E8 to normal human tissues (lung, brain, kidney, heart, stomach, breast, erythrocytes, or lymphocytes) was observed. The 5E8 antibody was used to immunoprecipitate detergent lysates of biosynthetically labeled or surface radioiodinated lung tumors. Analysis of the immunoprecipitates by sodium dodecyl sulfate gel electrophoresis revealed a major band and a faster migrating second minor band. The molecular weights of these two proteins were estimated to be 160,000 and 120,000, respectively. The addition of a reducing agent to the gels did not alter the migration pattern of the immunoprecipitated macromolecules. The removal of a terminal carbohydrate, sialic acid, did not restrict the binding of 5E8 to the tumor-associated antigen. However, labeling studies using galactose oxidase and tritiated borohydride revealed the presence of galactose on the immunoprecipitated protein. This major Mr 160,000 glycoprotein that was identified on two different human lung tumor cell lines was also found on a human large cell tumor tissue obtained by surgical biopsy. The 5E8 antibody and the Mr 160,000 glycoprotein that it recognizes represent two very useful components with which to test several new antibody-mediated drug delivery systems in the treatment of human lung tumors. The tumor-associated glycoprotein also represents a potential analyte for a diagnostic or prognostic immunoassay for lung cancer.
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PMID:Membrane-associated glycoprotein (gp 160) identified on human lung tumors by a monoclonal antibody. 353 80

Methods have been developed in an in vitro system (1) of assessing the number of disseminated tumor cells in peripheral blood and (2) of enriching tumor cells from peripheral blood samples for further characterization. Cells from three human carcinoma lines (E 14, ChaGo, and LEDWiDr) were mixed with leukocytes from normal individuals in various ratios. The proportions of tumor cells were determined by a quantitative assay using 3H-thymidine, 3H-leucine, and 3H-galactose incorporation. Determination of tumor cell proportions with this method was most accurate in the range of 5 X 10(4) to 5 X 10(3) tumor cells mixed with a constant number (5 X 10(5] of lymphocytes. It was possible to separate 75Se-labeled tumor cells from 51Cr-labeled blood leukocytes by centrifugation in isopyknic Percoll density gradients. These cells were mixed at different ratios and subjected to Percoll gradient centrifugation. By this approach as few as 5 X 10(3) tumor cells could by identified in the presence of 5 X 10(7) leukocytes, representing a ratio of 1: 10,000. Percoll centrifugation did not damage the tumor cells. In blood cells from two lung cancer patients with lung metastases the incorporation of 3H-thymidine and 3H-galactose was significantly enhanced compared with that in blood cells from patients with primary lung tumors and in cells from normal individuals. This difference became even more apparent when metabolically-labeled blood cells were subsequently separated by Percoll gradient centrifugation.
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PMID:Assay for the determination of human carcinoma cells in circulating blood. 398 May 60

Human lung cancer transplanted into athymic mice contains predominantly an acidic variant (designated B1) of lysosomal arylsulfatase B. B1 enzyme was suggested to be phosphorylated and sialylated (Gasa, S., Makita, A., Kameya, T., Kodama, T., Koide, T., Tsumuraya, M., and Komai, T. (1981) Eur. J. Biochem. 116, 497-503). In order to determine the localization of phosphate in B1 enzyme, we labeled in vivo the transplanted tumor with [32P]H3PO4 or [3H]glucosamine and purified B1 enzyme by immunoprecipitation. Bio-Gel chromatography of the labeled B1 enzyme treated with endoglycosidase H demonstrated that both the excluded and included materials were labeled with 32P and 3H. From acid hydrolysate of the excluded materials, phosphorylated serine and threonine were detected. Protein phosphorylation of arylsulfatase was confirmed by in vitro labeling experiments with [gamma-32P]ATP. By incubation of the tumor homogenate with ATP followed by isolation of the enzymes, B1 enzyme had a significant amount of radioactivity, whereas the B enzyme had little; by exogenous protein kinase, partially purified B enzyme was phosphorylated 35 times more than B1 enzyme. Acid hydrolysate of the included materials in the Bio-Gel column demonstrated mannose 6-phosphate and an unknown phosphorylated compound which migrates more than Man-6-P on electrophoresis and chromatography.
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PMID:Phosphorylation on protein and carbohydrate moieties of a lysosomal arylsulfatase B variant in human lung cancer transplanted into athymic mice. 640 42

The effect of glucose and other monosaccharide availability in culture medium on production of antibody by human hybridomas has been studied. Human hybridoma cells C5TN produce an anti lung cancer human monoclonal antibody, and the light chain is N-glycosylated at the variable region. When the cell line was grown in the presence of various concentrations of glucose, the antibodies produced changed their antigen-binding activities. Analysis of the light chains produced under these condition revealed that four molecular-mass variant light chains ranging from about 26 to 32 kDa were secreted. The twenty six-kDa species, which corresponds to a non-glycosylated form of the light chain, was recovered after enzymatic removal of all N-linked carbohydrate chains, indicating that the source of the heterogeneity of the light chain is due to the varied glycosylation. When the C5TN cells were cultured in medium containing either fructose, mannose or galactose instead of glucose, galactose elevated the antigen binding activity of the antibody more than the other sugars. These results suggest that change of glucose availability affects the antigen-binding activity of the antibody via the alteration of the glycosylation.
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PMID:Changes of monosaccharide availability of human hybridoma lead to alteration of biological properties of human monoclonal antibody. 776 43

Blood group antigen-related oligosaccharides have been implicated in growth regulation, cell mobility control and adhesion; we are therefore interested in the localization of receptors for these oligosaccharides in tumour cells. Labelled neoglycoconjugates that carry synthetic sugar structures are suitable tools to determine: whether such binding sites are present in human lung cancer; whether structural alterations of the glycoligand part will affect extent of binding; and whether cell type-associated alterations can be detected. Sections from 121 cases of lung cancer, representing small cell and non-small cell lung carcinoma, mesothelioma and metastases from extrapulmonary primary carcinomas were used to study the binding of nine synthetic AH- and Le-related oligosaccharides. Probes with fucose-alpha 1-3/4-N-acetylglucosamine-beta 1-R, an A-like disaccharide and 3'-sulfated galactose as ligand appear to bind less well to small cell than to non-small cell lung cancer cases, whereas Lec-disaccharide distinguishes mesothelioma from metastatic carcinoma. The latter ligand, A-like disaccharide and H (type III)-like trisaccharide exhibit evident cell type-associated differences in extent of binding. Thus, tailor-made neoglycoconjugates constitute a promising class of histopathological tools that warrants further study.
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PMID:Cell type-dependent alterations of binding of synthetic blood group antigen-related oligosaccharides in lung cancer. 787 30


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