Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0684249 (lung carcinoma)
 23,830 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Murine monoclonal antibody CF511, raised against human ovarian clear cell carcinoma, detects a glycoprotein (Mr 600 kDa) called CF511 antigen which is elevated in the serum of many patients with ovarian carcinoma. A competitive enzyme-linked immunosorbent assay was developed to detect CF511 antigen in human serum and used to detected CF511 antigen in subjects with ovarian carcinoma and other diseases. No raised levels (less than 18 unit (U) ml-1) of the antigen were found in the serum of 220 normal individuals or of patients with germ cell tumours (n = 6), granulosa theca cell tumour (n = 1), gastric carcinomas (n = 10) and colo-rectal carcinomas (n = 8). Raised serum levels of CF511 antigen were found in 6/46 patients (13.0%) with benign gynaecological tumours (including endometriosis or ovarian cyst), in 5/7 patients (71.4%) with breast carcinoma and 16/21 (76.2%) lung carcinoma patients. In patients with ovarian carcinoma, 42.3% (11/26) of stage I and II, and 96.0% (24/25) of stage III and IV had levels of greater than or equal to 18 U ml-1. In all patients with serial determination of CF511 antigen levels before and after the surgery, the levels of antigen correlated with the clinical course of disease. Determination of CF511 antigen levels may be useful for detection of ovarian carcinoma as well as lung and breast carcinomas and for monitoring progress of disease and response to therapy.
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PMID:An evaluation of ovarian carcinoma-associated antigen defined by murine monoclonal antibody CF511 in sera from patients with ovarian carcinoma. 189 54

Tumor H-59 is a variant of the Lewis lung carcinoma which is metastatic to the liver. In previous studies we have shown that liver metastasis in this tumor model correlates with adhesion in vitro to hepatocyte monolayers (Brodt, P., Clin. Exp. Metastasis, 7: 525-539, 1989). In an attempt to identify the adhesion molecule(s) involved, monoclonal antibodies were produced. One monoclonal antibody (MAb C-11) was highly specific to hepatocyte-adherent tumor cells. The antibody (an IgG1) and F(ab)2 fragments blocked tumor cell attachment to hepatocytes while having no effect on tumor cell adhesion to basement membrane proteins coated onto culture dishes. Western blot analysis of solubilized 11-59 plasma membranes or cell lysates showed that the antibody recognizes an Mr 64,000 protein. Treatment with N-glycosidase F prior to Western blot analysis revealed that N-linked carbohydrate residues constitute approximately 43% of the total weight of this molecule. This glycoprotein is only weakly expressed on tumor M-27, a lung-specific subline of the Lewis lung carcinoma (Brodt, P., Cancer Res., 46: 2442-2448, 1986), is undetectable in plasma membrane preparations obtained from spleen cells and thymocytes, but can be detected on cultured hepatocytes and in hepatocyte cell lysates. Pretreatment of the hepatocytes with MAb C-11 also resulted in inhibition of tumor cell adhesion. These results suggest that this glycoprotein mediates the attachment of H-59 cells to hepatocytes.
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PMID:Identification of an Mr 64,000 plasma membrane glycoprotein mediating adhesion of tumor H-59 cells to hepatocytes. 205 93

Spleen cells from inbred Biozzi mice, immunized against the human breast cancer cell line T47D, were fused with murine myeloma SP2O cells to generate monoclonal antibodies. One of these, 1BE12, of IgM isotype, reacted with five of six human breast tumor cell lines, while no binding was detectable with normal lymphocytes, RBC, or fibroblasts. The antigen recognized by monoclonal antibody 1BE12 was localized on the surface of T47D and MCF7 cells and was detected in cell-free supernatants of cultures. The antigen was found also on the surface of milk secretory cells. Immunohistochemical staining of frozen and paraffin-embedded sections of human tissues showed apical polarized reactivity in normal breast glands, while in all breast cancers staining was either cytoplasmic or membranous and heterogeneously distributed. Immunostaining was also observed in some other normal epithelia, including salivary gland, gastroduodenal mucosa, exocrine pancreas, and cervix. The antigen was not detectable in secretory endometrium, whereas proliferative endometrium was strongly stained. Colon carcinoma, and cancers of the bladder and endometrium were strongly reactive. No staining was detected in melanoma, lymphoma, mesothelioma, non-small cell lung carcinoma, and thyroid, renal, and ovarian carcinomas. Lectin absorption of MCF7 membrane extracts reduced 1BE12 binding. A large reduction in 1BE12 reactivity was observed after digestion of T47D and MCF7 membrane extracts with proteases. Treatment with sodium periodate resulted in complete loss of antigenicity, while neuraminidase treatment did not affect 1BE12 binding. These findings suggest that the 1BE12 epitope is expressed on the carbohydrate moiety of a glycoprotein and does not contain sialic acid. Immunoblotting of the perchloric acid-soluble fraction of MCF7 membrane extracts after electrophoresis in 1% agarose detected the antigen as a high molecular weight species (Mr greater than 900,000). The antigen was purified by perchloric acid extraction of MCF7 membrane preparations followed by affinity chromatography on 1BE12 antibody coupled to Sepharose-4B and gel exclusion fast protein liquid chromatography. No reactivity of the purified material was found with monoclonal antibodies directed against human milk fat globule membrane-associated mucins HMFG1 and DF3.
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PMID:Characterization and distribution in human tissues of a glycoproteic antigen defined by monoclonal antibody 1BE12 raised against the human breast cancer cell line T47D. 222 61

The mechanism of action of 5-hexyl-2-'deoxyuridine (HUdR), a compound with antitumor activity, has been investigated in the HM cell lines derived from the highly metastatic variant of Lewis lung carcinoma (3LL-HH). It was shown that this pyrimidine analog did not inhibit the biosynthesis of nucleotides but modified the biosynthesis of glycoconjugates. The incorporation of [14C]-glucosamine into cytoplasmic glycoconjugates [glycosaminoglycan (GAG), glycolipid (GL), glycoprotein (GP), neutral polysaccharide (NP)] decreased to a similar level. The [14C]-glucosamine derived radioactivity was reduced to about 60-70% of the untreated controls in the presence of 15 micrograms/ml HUdR, which caused no inhibition of cell proliferation. These results might be explained by the reduced conversion of glucosamine into uridine-5'-diphospho-hexosamine. As more reduction was observed in the glucosamine labeling of glycoconjugates in nuclei and extracellular compartment, it may be conceivable that the intracellular transport of certain glycoconjugates (GAG, GP) is also affected by HUdR. In the extracellular compartment the reduced level of GAG labeling was the most apparent change. However, at a higher concentration of HUdR (75 micrograms/ml) there was a higher radioactivity in the combined GL + GP fraction. Using [35S]-labeling, the GAG fractions also showed a decreased radioactivity but only at the concentration of 75 micrograms/ml HUdR.
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PMID:Modulation of glycoconjugate biosynthesis by 5-hexyl-2'-deoxyuridine in highly metastatic Lewis lung carcinoma cells. 223 12

Spontaneously occurring microscopic lung and lymph node metastases (in athymic mice) of a low metastatic human lung carcinoma cell line, UCP3, and its high metastatic variant, MV522, were isolated. Characterization of the variants included karyotypic and isoenzyme analyses; assessment of spontaneous metastatic capabilities in athymic mice, and monoclonal antibody analyses. The high metastatic variant LNT had barely detectable amounts of a glycoprotein molecule with apparent Mr 73 kd and 90 kd, which was present in the other cell lines. This molecule was detected in 20/24 primary human neoplasms but only in 3/18 metastatic neoplasms, suggesting a loss during the metastatic disease process.
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PMID:Spontaneously metastasizing variants of a human lung carcinoma cell line: monoclonal antibody characterization. 224 63

Two murine monoclonal antibodies, MAb 8 (immunoglobulin G3 kappa) and MAb 15 (immunoglobulin G1 kappa), were produced after immunization with TKB-2, a variant cell line of human small cell carcinoma of the lung. In enzyme-linked immunosorbent assay, these antibodies reacted with four major types of lung cancer cell lines and various extrapulmonary tumor cell lines. Immunohistological study, however, showed highly specific binding to lung cancers; MAb 8 bound to 68% of 65 lung cancers, and MAb 15 bound to 72% of them. Interestingly, both antibodies were more reactive with non-small cell than small cell lung cancers and bound most frequently to large cell carcinoma. Most extrapulmonary tumor tissues were negative in staining with a few exceptions; endodermal sinus tumor (two of two) was positive to both antibodies, breast carcinoma (one of five) to MAb 8, gastric carcinoma (one of three), and malignant melanoma (one of one) to MAb 15. Cross-reactions with normal tissues were limited; MAb 8 reacted with adult and fetal lung, and MAb 15 with esophagus and renal tubules. MAb 8 recognized a Mr 48,000 glycoprotein antigen (carbohydrates as its epitope), and MAb 15 recognized two proteins (Mr 85,000 and 45,000) (peptides as their epitopes). These two antibodies, detecting novel antigens extensively associated with and highly specific to lung cancers, are potentially useful for the study of lung cancer.
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PMID:Two murine monoclonal antibodies against human lung cancer-associated antigens. 243 Jun 95

Monoclonal antibodies with specificity for mucin-like antigens have shown great promise for the diagnosis and therapy of human cancer. Heterogeneity in the expression of mucin-like antigens by tumor and normal cells has been noted in several previous studies. An understanding of the nature of this heterogeneity has important implications for the diagnostic and therapeutic usefulness of antibodies to mucin-like antigens. We have studied the mechanism of variability in expression of epitopes on a mucin-like antigen defined by monoclonal antibodies W1, W5, and W9 in the lung carcinoma cell line, Calu-1. Using the fluorescence activated cell sorter and clonal analysis, we have demonstrated that intercellular variability in mucin antigen expression by Calu-1 cells can be explained in part by heritable variation in the tumor cell population. Clonal cell lines were isolated which differ greatly in levels of epitopes for all three mucin directed antibodies. Levels of all three epitopes showed significant variation between different clonal lines but in general were coordinately regulated. Differences in epitope expression between two lines studied in detail could be attributed to a dramatic difference in expression of a high molecular weight mucin-like glycoprotein. In immunoblotting experiments the binding of all three antibodies to this glycoprotein was affected by sodium periodate and/or neuraminidase treatment, suggesting that the antibodies recognize carbohydrate epitopes. Thus, heterogeneity in expression of mucin-like glycoprotein antigens can result from heritable variations which affect expression of multiple carbohydrate epitopes.
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PMID:Heritable variation in expression of multiple tumor associated epitopes on a high molecular weight mucin-like antigen. 243 Jun 97

Cell lines derived from human squamous lung carcinoma release large amounts of a soluble glycoprotein into the culture media, having very high molecular weight (greater than 2 X 10(6] and mucin-like properties. A monoclonal antibody called 43-9F has been generated that recognizes a carbohydrate epitope on the glycoconjugate. The epitope is also present on a diverse set of smaller glycoproteins (Mr 50,000-200,000) distributed primarily on the surface of the squamous lung carcinoma cells. A sensitive assay using the 43-9F antibody in a dot blot procedure has been devised that is able to detect an amount of antigen less than that possessed by a single squamous lung carcinoma cell. This assay, and also conventional immunofluorescence and immunohistochemical assay procedures, have been used to screen different normal cells, normal tissues, cancer cells, and tumor biopsy specimens for the antigen. In the normal lung the 43-9F antigen is found only on cells of some of the seromucous glands. In the normal digestive system it is associated in certain organs only with a limited population of mucosal epithelial cells. Other organ systems lack any reactive cells. The cells of most human non-small cell lung carcinomas and their released glycoconjugates have large amounts of the 43-9F epitope, while small cell lung carcinomas and the glycoconjugates released by small cell lung cancer cells lack the epitope. The oligosaccharide recognized by the 43-9F antibody may therefore provide a useful marker to distinguish the different lung carcinomas and for investigating the different cells of origin of these tumors.
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PMID:Glycoproteins distinguishing non-small cell from small cell human lung carcinoma recognized by monoclonal antibody 43-9F. 243 33

A rat monoclonal antibody 133-13A to a mouse lung carcinoma cell line was found to react with macrophages in mouse lung [1]. This monoclonal antibody is different from previously described antibodies to macrophages. Immunogold electron-microscopy and immunoperoxidase light microscopy have been used to show that MoAb 133-13A binds specifically to macrophages in normal and in BHT treated mouse lungs. This MoAb recognizes a protein of approximately 100 kDa (P100) on cultured lung carcinoma cells and a 87 kDa protein on macrophages from lung or the peritoneal cavity which is different from other macrophage antigens. The surface glycoprotein has been purified from cultured cells using immunoaffinity chromatography. The purified protein was radioiodinated and MoAb 133-13A was used to develop a competition radioimmunoassay to quantitate P100. Spleen, intestines, lung, skin and uterus all have high levels of P100. P100 on peritoneal macrophages has been determined to be about 94,000 molecules/cell. Analyses of lung lavage and whole lung homogenates from mice treated with BHT, BHT plus 70% O2, and 70% O2 alone show that treated animals have elevated P100 content compared to corn oil treated mice.
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PMID:A new monoclonal antibody to study mouse macrophage antigen during BHT-induced lung injury and repair. 246 38

Interleukin 2 (IL-2) is a secreted glycoprotein which acts as an activation and proliferative signal for lymphocytes expressing membrane-bound glycoprotein IL-2 receptors. We have recently established that swainsonine (SW), an inhibitor of mannosidase II during N-linked glycoprotein processing, augmented mitogen-induced mononuclear leukocyte IL-2 receptor expression and IL-2-induced proliferation. The objective of the present investigation was to examine the effect of SW on lymphokine-activated killer (LAK) cell induction. Human mononuclear leukocytes were treated with various concentrations of SW (0.1-10 micrograms/ml) and IL-2 (1-100 units/ml) for up to 72 h. SW augmented IL-2-induced LAK activity directed against human lung carcinoma, melanoma, and leukemia cells 2-3-fold. LAK activity generated in the presence of SW at suboptimal doses of IL-2 (10 units/ml) was similar to that observed with higher concentrations of IL-2 (100 units/ml) alone. SW treatment alone or in combination with IL-2 increased the percentage of IL-2 receptor-positive cells. Furthermore, pretreatment with SW subsequently enhanced IL-2-induced lymphocyte proliferation. SW-treated mononuclear leukocytes exhibited an increase in high-mannose type glycoproteins based upon [3H]mannose labeling, susceptibility to alpha-mannosidase, and binding to concanavalin A-Sepharose. These results indicate that modulators of glycoprotein processing may be useful in lowering the concentrations of IL-2 required for LAK induction and maintenance.
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PMID:Potentiation of human lymphokine-activated killer cell activity by swainsonine, an inhibitor of glycoprotein processing. 250 Oct 20


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