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)

The murine anti-human lung tumor monoclonal antibody L3 recognizes antigens found both in the medium of cultured carcinoma cells and in normal human serum. Sequential immunoprecipitation experiments indicate that the L3 antigen is also recognized by a previously described monoclonal antibody directed against a melanoma-associated antigen [Natali, P. G., Wilson, B. S., Imai, K., Bigotti, A., & Ferrone, S. (1982) Cancer Res. 42, 583-589]. This antibody precipitated a Mr 76000 glycoprotein from metabolically labeled extracts of the lung carcinoma cell line Calu-1 and a Mr 94 000 glycoprotein from labeled culture medium. Pulse-chase experiments suggested a precursor-product relationship between these molecules. Analysis of glycosidase sensitivities of the two forms indicated that maturation of carbohydrate side chains correlated with the apparent increase in molecular weights. L3 antigenic activity, measured in a competitive radiometric cell binding assay, was purified more than 90-fold from serum-free medium of Calu-1 cells and more than 3000-fold from normal human serum. The major immunoreactive components purified from culture medium and serum were identical with respect to apparent molecular weight, electrophoretic mobility, pI, glycosidase sensitivity, and V8 protease fingerprints. In addition, the sequence of the amino-terminal 16 N-terminal amino acid residues of the major immunoreactive species from both sources was identical. The properties of the L3 antigen did not correspond to those of any known protein, suggesting that this serum protein has not been previously characterized.
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PMID:Identification of a novel serum protein secreted by lung carcinoma cells. 352 24

The distribution of a variant of blood group A antigen recognized by a murine monoclonal antibody, KM-32, generated against human squamous cell lung carcinoma was investigated in various tissues and sera. By immunoperoxidase staining, the antibody was found to react with a number of lung carcinoma tissues of squamous cell carcinoma, adenocarcinoma, and small cell carcinoma, and several other tumor tissues. Positive staining was also observed in a small number of cells of some normal tissues, such as bronchiolar epithelium, gastrointestinal glands, and convoluted tubules of the kidney. The antibody could also be used in detecting macromolecular antigens, designated KA-32, in sera of patients with lung cancer. The antigen level in serum was determined by an inhibition assay using purified KM-32. The higher level of inhibition was seen in sera from over half of patients with lung cancer and patients with benign diseases when compared with those in sera from healthy adults. Purification of the antigen in serum was performed by gel filtration chromatography, immunoaffinity chromatography, and polyacrylamide gradient gel electrophoresis. Purified antigen exhibited a glycoprotein nature, and its molecular weight was estimated at more than 500,000.
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PMID:Distribution of a squamous cell lung carcinoma-associated antigen, KA-32, in human tissues and sera defined by monoclonal antibody KM-32. 353 Apr 36

Four murine monoclonal antibodies against human lung carcinoma were generated using a novel immunization procedure. BALB/c mice were rendered neonatally tolerant to normal human lung tissues and subsequently immunized with human lung tumor tissues. The lower level of antibody-reactivity to the tolerogen was seen in the sera of mice rendered neonatally tolerant as compared with the level of reactivity in the sera of nontolerant mice. The mice which maintained a sufficiently tolerant state were selected for hybridoma production. Two monoclonal antibodies, KM-32 and KM-34, were developed from mice immunized with lung squamous cell carcinoma tissues and two other monoclonal antibodies, KM-52 and KM-93, were developed from mice immunized with lung adenocarcinoma tissues. Distribution of antigens detected by the monoclonal antibodies were investigated by enzyme-linked immunosorbent assay using membrane fractions prepared from a number of tumorous and normal tissues and various human normal and tumor cell lines. KM-32 recognized a carbohydrate antigen expressed predominantly on lung squamous cell carcinoma cells and its carbohydrate structure appeared to be associated with blood group A antigen. KM-93 recognized a sialylated carbohydrate epitope on the antigen expressed on lung adeno-carcinoma cells and a few other tumor cells. KM-34 and KM-52 detected protein or glycoprotein antigens and they showed predominant reactivity to lung squamous cell carcinoma and lung adenocarcinoma, respectively. KM-32 and KM-34 antibodies showed complement-dependent cytotoxicity against a lung tumor cell line. These results suggest that the tolerance technique is useful for efficient screening of murine monoclonal antibodies specific to human tumors. The efficacy of these four monoclonal antibodies in diagnosis and therapy of lung cancer will be the subject of a sequential study.
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PMID:Generation of monoclonal antibodies against human lung squamous cell carcinoma and adenocarcinoma using mice rendered tolerant to normal human lung. 373 Nov

Hybridoma cultures producing monoclonal antibodies were derived from fusions of the parent myeloma P3-X63-Ag8-U1 with spleen cells of BALB/c mice which had been immunized with the Lewis lung carcinoma (3LL) of C57BL/6 mice. Four monoclonal antibodies (A8-2.7, C6-1.2, D12-2.7), and G8-1.6) showed high reactivity to 3LL cells but showed no or low reactivity to other tumor cells, cultured cell lines, and normal tissues from C57BL/6 mouse. The C6-1.2 antibody was confirmed to have a binding capacity specific to 3LL cells by absorption assay and inhibition assay. Antigenic analysis indicated that the C6-1.2 antibody bound to 3LL surface glycoprotein (approximately 45,000 daltons), and other antibodies reacted with proteins (less than 10,000 daltons) on the cell surface of 3LL. Administration of C6-1.2 antibody i.v. reduced the metastasis into the lungs of 3LL in C57BL/6 mice.
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PMID:Monoclonal antibodies to Lewis lung carcinoma. 404 23

A previously described defect of in vitro monocyte maturation in patients with squamous-cell carcinoma of the lung (SCC) has been investigated further. The maturation of patients' monocytes in pooled normal human serum was significantly better than in autologous serum. Conversely, the maturation of normal control monocytes was significantly depressed in patients' serum. The defect has been shown to be due to the presence of an inhibitory factor, rather than the lack of a necessary component in the patients' serum. Artificially aggregated gamma-globulin inhibited monocyte maturation in vitro, but the presence of immune complexes in the serum of many patients with SCC did not correlate well with the depression of in vitro maturation of monocytes from the same patient. Similarly, pregnancy-associated alpha 2-glycoprotein, in increased amounts in the serum of patients with SCC, showed no correlation with monocyte maturation. The addition of soluble extracts of tumour, but not of surrounding normal lung tissue significantly inhibited monocyte maturation. The results suggest that the defective monocyte maturation in patients with SCC is at least in part due to serum inhibitory factors, which are likely to be a heterogeneous group.
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PMID:In vitro monocyte maturation in squamous-cell carcinoma of the lung: influence of humoral factors. 617 51

Continuous cell lines have been established from a variety of biopsy and postmortem species of tumor from patients with small-cell carcinoma of the lung (SCCL) and have been maintained over several years. The medium from the cultures has been assayed for peptide, glycoprotein, and steroid hormones. Significant amounts of 14 hormones including calcitonin, adrenocorticotropin (ACTH), parathormone, luteinizing hormone, chorionic gonadotropin, glucagon, growth hormone, somatostatin, prolactin, beta-endorpin, lipotropin, oxytocin-neurophysin, vasopressin-neurophysin, and estradiol have been demonstrated. Up to ten different hormones have been produced by a single cell line. Most produce ACTH and all evaluated so far produce estradiol. These studies indicate that cells from SCCL have a potential for producing a wide variety of hormones and that this characteristic can be maintained for prolonged periods of culture in vitro.
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PMID:Hormone production by cultures of small-cell carcinoma of the lung. 626 22

Monoclonal antibodies KS1/4, KS1/9, and KS1/17 were developed in this laboratory from a fusion of the murine myeloma cell line P3X63Ag8 with spleens of BALB/c mice previously primed with UCLA P3 cells derived from a human adenocarcinoma of the lung. Monoclonal antibodies KS1/4 and KS1/17 seemed to recognize similar glycoprotein antigens on the lung carcinoma cells by indirect immunoprecipitation and sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. However, mapping of [3H]lysine- and [3H]arginine-labeled tryptic peptides of antigens in specific immunoprecipitates of lung carcinoma cells by high-pressure liquid chromatography revealed a one peptide difference. Antibody KS1/9 did not immunoprecipitate any identifiable protein from detergent extracts of the immunizing cell line by routine methods and appears to detect a glycolipid antigen. Immunocytochemical analysis of tissue sections showed this monoclonal antibody to be reactive with adenocarcinomas of the lung and not with the other histological types of lung carcinoma or normal tissue. Monoclonal antibodies KS1/4 and KS1/17, however, reacted with 3 major histological types of lung cancer and minimally with the proximal tubules of normal kidney and the epithelium of bronchioles.
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PMID:Antigens associated with a human lung adenocarcinoma defined by monoclonal antibodies. 636 52

The surface oligosaccharide residues, glycoproteins and sialyl components of CMT64 lung carcinoma cells and high-metastatic sublines CMT167 and CMT181 have been studied in culture. (1) The total cellular sialic acid content did not differ appreciably between the three lines. However, the accessibility of surface sialyl groups, measured by metabolic incorporation of [3H]NAcmannosamine followed by neuraminidase hydrolysis, was decreased from 42% in CMT64 to 25% hydrolyzed in CMT181. (2) The major plasma membrane glycoproteins of the lines were radiolabelled by lactoperoxidase iodination, metabolic incorporation of [3H]fucose or labelling in the terminal sialyl residues by the NaIO4-NaB[3H]4 method and the labelled glycoproteins were analyzed by two-dimensional gel electrophoresis. Each labelling technique identified a complex pattern of glycoproteins including a prominently labelled group of high-molecular-weight acidic sialoglycoproteins: GP200/4.9-5.1 (apparent molecular weight X 10(-3)/pl of iodoprotein); GP150/5.1-5.6; GP130/5.0-5.6; GP110/5.0; GP100/4.8 and GP100/5.0-5.4. (3) The neuraminidase-susceptible glycoproteins on CMT64 and CMT181 were identified in the isoelectric focusing separation of the two-dimensional gel separation by the charge difference caused by desialylation. The glycoproteins most susceptible to neuraminidase were the high-molecular-weight acidic glycoproteins which showed marked charge heterogeneity: GP150/5.1-5.6, GP130/5.0-5.6; GP100/5.0-5.4 and GP100/4.8. (4) Using these procedures we did not detect modifications between CMT181 and CMT64 and we conclude that the cultured cells of the sublines do not display marked surface glycoprotein alterations that reflect their enhanced spontaneous metastatic potential.
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PMID:Cell surface properties of high- and low-metastatic cell lines selected from a spontaneous mouse lung carcinoma. 665 29

The 6B3-Ag recognized by a monoclonal antibody 6B3 to human large cell lung carcinoma cell line (HLC-2) is a high-molecular-weight glycoprotein of 1,000,000. Its serum level is increased in various adenocarcinoma patients. When a patient's serum with a high concentration of 6B3.Ag (54 micrograms/ml) or concentrated 6B3.Ag from normal human serum was analyzed by immunoelectrophoresis, 6B3.Ag showed a long bimodal precipitin line extending from the per-beta to beta globulin region. However, the precipitin line of 6B3.Ag in the HLC-2 culture medium was formed only in the pre-beta globulin region. The 6B3.Ag was purified from pooled patients' serum by salting out, precipitation by acidification at pH 4.5 and Sepharose 4B and immunoaffinity chromatographies. Western blotting indicated that the 6B3.Ag from human serum contained IgG and/or IgM. The 6B3.Ag from human serum showed a dose-dependent reaction in a sandwich enzyme-linked immunosorbent assay with anti-6B3.Ag antibody as a solid-phase antibody and anti-human IgG or anti-human IgM antibody labeled with alkaline phosphatase. The 6B3.Ag was concluded to be partly present as a complex with IgG and/or IgM in human serum, and this complex showed a precipitin line in the beta globulin region on immunoelectrophoresis.
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PMID:A glycoprotein secreted by lung cancer cells is present in human serum as an immunoglobulin-binding protein. 750 5

Merkel cell carcinoma (MCC) is a primary cutaneous neoplasm most commonly involving older adults. The cell of origin is thought to be the Merkel cell, a cutaneous neurosecretory cell. However, other neuroectodermal tumors may present in the skin and may be difficult to distinguish from MCC, including peripheral neuroectodermal tumors (PNET) and metastatic small cell carcinoma. We examined a primary cutaneous tumor of an 18-year-old which was strongly positive for cytokeratin (CK), neuron-specific enolase (NSE), and 12E7, an antibody to the protein determined by the MIC2 gene. Electron microscopy showed paranuclear aggregates of filaments and no cytoplasmic processes. These findings were considered to be consistent with MCC. Cytogenetic analysis demonstrated 46,XX,der(1)t(1;3;22)(1qter-->pa34::3q28-->q11::22q 12--> qter),der(3)t(1;3)(3pter-->q11::1p35-->pter), der(22)t(3;22)(22pter-->q11::?3q29-->qter). This was confirmed by chromosome painting using probes for chromosomes 1, 3, and 22. Peripheral neuroectodermal tumors (PNETs) show a characteristic translocation involving the same breakpoint on chromosome 22 that was present in this tumor. PNETs can also be CK and NSE positive. The MIC2 gene codes for a surface glycoprotein that has been shown to be very strongly and reliably expressed in PNETs, but not in other small round blue cell tumors and not in small cell carcinoma of the lung. However, MIC2 expression has not been studied in MCC. We investigated the use of MIC2 analysis in the distinction of MCC from PNET. Five additional MCCs were stained with the monoclonal 12E7 antibody, and one additional tumor showed the strong membranous positivity reported in PNETs. Our data suggest that MIC2 analysis may be useful in differentiating between MCC and PNET. However, cases will remain for which the distinction is elusive and cytogenetic analysis may be helpful.
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PMID:Primary cutaneous neuroendocrine tumors. Diagnostic use of cytogenetic and MIC2 analysis. 762 31


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