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Query: UMLS:C0242379 (lung cancer)
 71,905 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Human lung cancer cell line, T3M-30, has been shown to produce a growth factor that stimulates proliferation of peripheral blood monocytes. In the presence of this factor, human circulating monocytes were able to proliferate in vitro. Gel exclusion chromatography of the conditioned medium revealed a single peak of monocyte growth-promoting activity at an apparent molecular weight of 16,000. The growth-promoting activity was adsorbed to an anion-exchange column, Mono Q, and eluted with a salt gradient as a single peak of bioactivity at 300 mM NaCl. When the sample was applied to a Vydac C4 column, a reverse-phase high-performance liquid chromatography column, a single peak of activity was observed at a concentration of 76% acetonitrile in 0.1% trifluoroacetic acid. The monocyte growth-promoting activity was heat stable at 56 degrees C. It was partially destroyed by trypsin. The activity was lost after treatment with 2-mercaptoethanol.
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PMID:A human monocyte growth factor produced by lung cancer cells. 216 45

We have studied the pattern of chromogranin A (CgA)-related species in different human endocrine cells that produce CgA and also express the calcitonin gene. Antibodies against CgA peptides that span its linear sequence were used in Western analysis of cell lines derived from medullary thyroid carcinoma (MTC), small cell lung cancers (SCLC), epidermoid cell lung cancer (ECLC) and a pulmonary carcinoid tumor (CRND). Each of the cell lines demonstrated a distinct pattern of CgA-related species. Gel filtration studies also revealed multiple and different forms of immunoreactive CgA in the cell lines. Although proteolysis may contribute to our results, these observations suggest that native CgA is processed to smaller species in a tissue-specific pattern by different endocrine cells. More conclusive studies, however, are necessary to establish that cell processing leads to the specific CgA moieties that we have observed.
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PMID:Distinct patterns of chromogranin A-related species can be demonstrated in endocrine cells. 216 12

From nude mouse tumors, in which malignantly transformed Bloom's syndrome (BS) B-lymphoblastoid cell lines were successfully transplanted into s.c. tissues, we have detected strong expression of malignant lymphoma (ML)-associated antigen on the cell surface, by using diluted sera of ML patients and indirect immunofluorescence. Even though carcinogen-treated BS B-lymphoblastoid cell lines expressed various types of cancer antigens (ML, ovarian cancer, stomach cancer, lung cancer, liver cancer, etc.) on the cell membrane as a mixed population (Y. Shiraishi and H. Soma, Proc. Natl. Acad. Sci. USA, 85:8211-8215, 1988), the finding that BS malignant cells originating from nude mouse tumors expressed specific ML-associated antigen seemed significant for ML diagnosis. BS nude mouse tumors were successively transplantable from nude mice to nude mice (100%). Histopathological studies using an electron microscope demonstrated that most tumor cells in s.c. tissues of nude mice were lymphoid malignant cells. Gel electrophoresis and Western blotting analyses demonstrated that the antigen which characterized ML was a single band (Mr 97,000) and did not cross-react with the sera of other cancer patients or with normal sera. Chromosome analysis showed that the cell clones with ML-associated antigen had marker chromosomes involving t(6;?)(p25;?),t(9;?)(q34;?), del(10)(p13),t(12;14)(q24;q11). The expression of ML-associated antigen was also discussed in relation to the marker chromosomes.
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PMID:Malignant lymphoma antigen expressed in nude mouse tumor cells derived from carcinogen-transformed Bloom's syndrome B-lymphoblastoid cell lines. 218 81

One hundred thirty-seven fluid samples from patients with malignant diseases, including 58 with lung cancer and 36 with gastric carcinoma, were screened for three tumor-associated carbohydrate antigens. The antigens tested were sialylated Lewis (SLEX) antigen, sialylated SSEA-1 (SLX) antigen, and sialylated Lewis (CA19-9) antigen. Thirty-four fluid samples from patients with benign diseases including 20 with tuberculous pleurisy were also tested for these three antigens as a control. SLEX antigen had the highest positivity rate among the three antigens both in the pleural effusions of patients with pulmonary adenocarcinoma and for all types of lung cancer (64.1% and 46.6%, respectively). In cancers of digestive system, the percentage of SLEX positivity was almost same as that for CA19-9, and higher than that for SLX. A combination assay using the three antigens resulted in an increased rate of detection of tumor-associated antigens (68% of 58 lung cancers including 83% of 39 adenocarcinomas, as well as 77% of 63 digestive system cancers including 84% of 36 gastric carcinomas). Gel filtration of pleural effusions or bile using sephacryl S-1000 showed that these three antigens were eluted in the void volume, indicating a molecular weight of greater than 2 X 10(6). Thus, all 3 antigens possibly exist on carrier protein with a high molecular weight. These observations suggest the potential application of these antigens to distinguish between benign and malignant fluid, and to monitor the effects of the treatment of various types of cancer.
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PMID:Detection of three sialylated tumor-associated antigens in malignant serous effusions. 224 89

Although serum CA 19-9 is considered to be a useful and specific tumor marker for pancreatic cancer, some patients with benign pulmonary diseases show elevated serum CA 19-9 levels. We measured serum CA 19-9 levels of 156 patients with benign pulmonary diseases (55 with asbestosis, 11 with bronchial asthma, 32 with bronchiectasis, 16 with idiopathic pulmonary fibrosis (IPF), 13 with healed pulmonary tuberculosis (HPT) and 29 other benign diseases). The percentage of patients with positive serum CA 19-9 was 42.3% (14.5% in asbestosis, 27.3% in bronchial asthma, 59.4% in bronchiectasis, 81.3% in IPF, 61.5% in HPT and 51.7% in others). In some patients, serum CA 19-9 levels were as high as those found in malignant gastrointestinal diseases. Serum CA 19-9 levels correlated well with disease activity. Immunohistochemically, CA 19-9 was expressed in mucous cells of the bronchial gland and surface of the bronchiolar surface epithelium cells in benign pulmonary disease. Gel filtration study suggested some difference in molecular weight between the serum CA 19-9 antigen of lung cancer and that of benign pulmonary diseases. It is suggested that serum CA 19-9 increases in the case of hyperplasia of the bronchiolar epithelium cells or the mucous cells of the bronchial gland. We conclude that benign pulmonary disease is one of the factors that affect serum CA 19-9 levels.
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PMID:[CA 19-9 in patients with benign pulmonary diseases]. 227 61

We reported previously a human lung cancer which induced marked granulocytosis both in the patient and in the tumor-transplanted nude mice (G-1 mice), and whose conditioned media (G-1-T-CM) contained both human-active colony-stimulating activity (h-CSA) (810 colonies/ml) and mouse-active colony-stimulating activity (m-CSA) (530 colonies/ml), suggesting that the CSA produced by the tumor caused granulocytosis both in the patient and in G-1-mice. We reported here another human lung cancer which induced marked granulocytosis both in the patient and in the tumor-transplanted nude mice (G-2-mice). However, in contrast to the tumor reported by us previously, the conditioned media of this tumor (G-2-T-CM) contained only very weak m-CSA (86 colonies/ml), although h-CSA was very strong (7332 colonies/ml). The ratio of m-CSA to h-CSA in G-1-T-CM (0.654) was 55-fold higher than that in G-2-T-CM (0.012). Gel filtration of G-2-T-CM on a Sephadex G-150 column denied the presence of colony-inhibiting activity which inhibited m-CSA in G-2-T-CM. Since the addition of serum obtained from G-2 mice did not enhance m-CSA in G-2-T-CM, it seems unlikely that the G-2 tumor produced an inactive form of m-CSA which was activated in G-2 mouse serum. G-2-T-CM tended to maintain the number of colony-forming units in spleen in mouse bone marrow during liquid cultures, while G-1-T-CM did not. These results may indicate that the G-2 tumor produced a humoral factor which has very weak CSA and acts on stem cells rather than on committed progenitors.
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PMID:Human colony-stimulating activity-producing tumor: production of very low mouse-active colony-stimulating activity and induction of marked granulocytosis in mice. 387 6

The ectopic secretion of calcitonin (CT) by a wide variety of nonthyroidal human tumors has been studied by CT RIA, but little information is available concerning the biosynthesis of CT in these tumors. In the present study, a human lung cancer cell line (BEN), secreting high mol wt forms of CT was investigated to characterize the CT gene products synthesized. When conditioned medium from BEN cells was chromatographed through a Bio-Gel P-30 column, larger species of immunoreactive CT were detected with mol wt of approximately 8,000 and 18,000. Little, if any, CT of 3,500 mol wt was detected. To examine CT gene products produced in BEN cells, poly A+ RNA was isolated from BEN cells and subjected to cell-free translation assays and DNA/RNA hybridization assays. In the wheat germ cell-free translation assay, a single BEN cell product which migrated on sodium dodecyl sulfate-polyacrylamide gels with an apparent mol wt of 17,000 could be specifically immunoprecipitated with CT antisera. A similar sized CT-related translation product is produced in wheat germ assays programmed by mRNA prepared from human medullary thyroid carcinomas. In DNA/RNA hybridization assays, a single BEN cell mRNA species of 1,000 base pairs, identical in size to human thyroidal CT mRNA, hybridized to a radiolabeled CT cDNA probe. Hybridization of the CT cDNA probe with BEN cell mRNA was confirmed by RNA dot blot hybridization and cytoplasmic RNA blotting procedures. These results indicate that larger mol wt forms of CT secreted by BEN cells are derived from a translation product and a mRNA which are of similar, if not identical, size as CT gene products produced in human thyroidal tissues. The inability of lung tumor cells to process the CT precursor to calcitonin of 3,500 mol wt may reflect a lack of specific prohormone processing enzymes in these tumor cells or may be due to structural polymorphism in the CT precursor expressed in the lung cells.
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PMID:Biosynthesis of calcitonin by human lung cancer cells. 396 26

A case of hyperamylasemia with lung cancer is described. Macroamylasemia was excluded by a normal amylase/creatinine clearance ratio and by a sedimentation constant obtained by sucrose density gradient centrifugation. Positive immunofluorescent staining of tumor cells with a specific antibody against human salivary amylase and significant amylase activity in the primary tumor and metastases support the hypothesis of independent production of amylase by the lung tumor. Cellulose--acetate membrane electrophoresis demonstrated three bands of amylase activity. The major component corresponded to normal salivary amylase in electrophoretic mobility, isoelectric point and molecular size. The minor bands, one of which occupied about 10% of the total amylase activity in serum, urine and tissue homogenates, demonstrated a lower electrophoretic mobility and a more acidic isoelectric point. Gel filtration and electrophoresis disclosed that these minor bands were derived from an amylase isozyme with a larger molecular size than that of normal salivary amylase. The results suggest ectopic tumor production of heterogenous amylase isozymes, with the larger form being secreted into the circulation.
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PMID:Amylase-producing lung cancer: case report and review of the literature. 617 Apr 23

Immunoreactive corticotropin-releasing factor (I-CRF) and ACTH (I-ACTH) were examined using RIA, immunoaffinity chromatography, and gel filtration chromatography in human hypothalamus, adrenal (cortex and medulla), lung cancer, and pheochromocytoma. I-CRF and I-ACTH were present in these tissues. Gel filtration of I-ACTH in the adrenal, pheochromocytoma, and lung cancer showed the presence of larger amounts of I-ACTH with large molecular weight forms in contrast to the hypothalamus. Gel filtration of I-CRF in these tissues showed the main peak eluted at the position of synthetic rat CRF. High performance liquid chromatography of this main peak showed two components which eluted in the positions of synthetic rat CRF and oxidized CRF. These elution positions were the same in all tissues and identical with those in the hypothalamus. These results suggest the presence of I-ACTH and I-CRF in these tissues and that CRF outside the brain is identical to hypothalamic CRF.
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PMID:Immunoreactive corticotropin and corticotropin-releasing factor in human hypothalamus, adrenal, lung cancer, and pheochromocytoma. 632 18

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


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