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)

Receptor sites can be visualized by labelled ligands as an alternative to receptor-specific antibodies, as substantiated for two different receptor classes. Recombinant tumour necrosis factor alpha (TNF) was biotinylated via amino-groups and the resultant probe was applied to formalin-fixed, paraffin-embedded tissue sections of 94 primary bronchial carcinomas and to normal peripheral lung parenchyma. In addition, monoclonal antibodies specific for neuron-specific enolase (NSE) and TNF itself were used. The biotinylated beta-galactoside-specific mistletoe lectin, which exhibits dose-dependent immunomodulatory and toxic potency, and two probes that specifically detect certain types of sugar receptors were employed to illustrate further the feasibility of using ligands for receptor localisation. The tumours comprised 62 small cell lung carcinomas, 10 epidermoid carcinomas, 11 adenocarcinomas and 11 large cell anaplastic carcinomas. Expression of TNF-binding sites was found in 39 of the small cell lung carcinomas and in 13 of the non-small cell lung carcinomas. Binding capacity for the TNF-specific antibody was seen in similar proportions of small cell lung carcinomas and of non-small cell lung carcinomas. None of the normal lung parenchymas revealed significant staining. Binding capacities to mistletoe lectin were seen in all normal lung parenchymas and in nearly all cases of adenocarcinoma (10/11). A correlation between the expression of NSE and the binding capacities to TNF was detected. Endogenous lectins, specific for lactose or beta-GalNAc, were displayed in nearly one half of the small cell lung carcinoma cases (44% or 45% respectively) and in about 25% of the non-small cell lung carcinoma cases.
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PMID:Analysis of tumour necrosis factor alpha-specific, lactose-specific and mistletoe lectin-specific binding sites in human lung carcinomas by labelled ligands. 132 10

Lectin binding to tumor cells in tissue sections of nonmetastatic and metastatic murine Lewis lung carcinoma (LLC) was assessed by light and electron microscopy using a lectin-gold technique. Ulex europaeus agglutinin-I (UEA-I) and peanut agglutinin (PNA) showed no binding, whereas concanavalin A (Con A), soybean agglutinin (SBA), Dolichos biflorus agglutinin (DBA), Maclura pomifera agglutinin (MPA), and Ricinus communis agglutinin-I (RCA-I) bound equally to the transplanted sites and metastases. However, wheat germ agglutinin (WGA) bound to metastases more highly than to the transplanted sites and there was a statistically significant difference (P less than 0.01) between the transplanted sites and metastases with regard to pre-embedding method. The tumor cells binding to WGA clearly decreased in number after sialic acid pretreatment and were rich in more well-differentiated organelle. In the bromodeoxyuridine (BrdUrd) labeling in vivo, cell proliferation was greater in the metastatic sites than in the transplanted sites. The above findings suggest that glycoconjugates on the tumor cell surface are altered in the process of metastasis and correlate with metastatic potential and cell proliferation.
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PMID:A light and electron microscopic histochemical study on lectin binding to cells with high metastatic potential in Lewis lung carcinoma. 162 36

We have purified a novel member of the integrin gene family from placenta that serves as a vitronectin receptor. This integrin is composed of the alpha v subunit and a beta subunit that we designate beta 5. Purification was accomplished by immunodepleting a placental extract of integrin alpha v beta 3, allowing us to purify alpha v beta 5 from the remaining extract by monoclonal antibody affinity chromatography on LM 142-Sepharose, which binds to the alpha v subunit. Purification to homogeneity was subsequently achieved by affinity chromatography on wheat germ lectin-Sepharose. Western blot analysis with antibodies raised against alpha v beta 5 and alpha v beta 3 demonstrated that beta 3 and beta 5 were distinct but confirmed that the alpha subunit of the two integrins were immunologically identical. Similarly, antibodies that bind beta 3 proximal to the ligand-binding site failed to react with beta 5, indicating an architectural difference at the ligand-binding site of these related integrins. This structural difference apparently results in a functional distinction, since purified alpha v beta 3 bound to vitronectin, fibrinogen, von Willebrand factor, and fibronectin, whereas integrin alpha v beta 5 bound preferentially to vitronectin. Finally, we demonstrate by three criteria that beta 5 and beta x, the latter of which was identified in lung carcinoma cells (Cheresh, D. A., Smith, J. W., Cooper, H. M., and Quaranta, V. (1989) Cell 57, 59-69), are identical. First, peptide maps of beta x and beta 5 are identical. Secondly, polyclonal antibodies raised against alpha v beta 5 immunoprecipitate both beta 5 and beta x, and finally, the amino-terminal amino acid sequences of beta x and beta 5 are identical.
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PMID:Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin. 169 73

Data are reported to demonstrate the usefulness of a monoclonal anti-polysialic acid antibody for (i) the visualization of immature and mature neural elements in human teratomas, and (ii) the distinction of small cell lung carcinoma from bronchial carcinoids as well as squamous cell and adenocarcinomas of the lung. Lectins which discriminate between the various types of sialylated sequences, such as the Sambucus nigra L. I lectin specific for Neu5Ac alpha 2,6 Gal/GalNAc and the leukoagglutinin from Maackia amurensis (MAL) specific for Neu5Ac alpha 2,3 Gal beta 1,4 GlcNAc have been applied to the study of human colonic mucosa. The Neu5Ac alpha 2,3 Gal beta 1,4 GlcNAc sequence was detectable in normal and transitional mucosa and carcinomas, whereas the Neu5Ac alpha 2,6 Gal/GalNAc sequence was found in carcinomas. The lectin Amaranthin reacts with Gal beta 1,3 GalNAc-alpha (the T antigen) and NeuAc alpha 2,3 Gal beta 1,3 GalNAc-alpha (the cryptic T antigen). It stained normal and transitional colonic mucosa as well as carcinoma. The reactivity was solely due to the cryptic T antigen and indicates that the T antigen may not represent a general carcinoma autoantigen.
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PMID:[Properties of the cell surface of normal and malignant cells: investigations on polysialic acid and terminal sialic acid residues in specific linkages]. 170 80

Examination of the in vitro effects of PA-I and PA-II lectins of Pseudomonas aeruginosa on Lewis lung carcinoma cells revealed that these lectins differ in their effects. PA-I, the galactophilic lectin, exhibited both cytotoxic and cytostatic activities on these cells (tested by [3H]thymidine incorporation and by crystal violet vital staining). The two activities were dose and time dependent and inhibitable by the addition of methyl-alpha-D-galactoside to the culture medium. PA-II, the L-fucose and D-mannose binding lectin of the same Pseudomonas strain did not exhibit such a direct toxic effect on the tumor cells but affected them in the presence of splenocytes. Its addition to the tumor cells cocultured with murine (C57B1) splenocytes led to a profound cytolysis of the tumor cells, an effect which was inhibited by L-fucose.
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PMID:Antitumoral effects of Pseudomonas aeruginosa lectins on Lewis lung carcinoma cells cultured in vitro without and with murine splenocytes. 181 6

Tumor infiltrating (TIL) and peripheral blood lymphocytes (PBL) were isolated from 18 patients with non-small cell lung cancer undergoing radical surgery. Surface marker analysis revealed that TILs and PBLs mainly consisted of CD3+ T cells and that TILs generally displayed a lower CD4/CD8 ratio. Differences were found in the expression of CD25 (IL-2 receptor) and DR (MHC class II) antigens, which were increased in TILs, and in the percentage of CD16+ natural killer (NK) cells, which was reduced in TILs as compared to PBLs. Accordingly, the NK activity of TILs was lower than that of PBLs, whereas neither TILs nor PBLs expressed spontaneous cytolytic activity against fresh autologous tumor cells, melanoma cells and the "NK-resistant" A549 lung carcinoma cell line. After 4 days of culture in medium with recombinant-interleukin-2 (rIL-2), TILs and PBLs acquired cytolytic activity against all cell targets, but TILs expressed higher levels of cytotoxicity than autologous PBLs only in 3 patients out of 16 tested. More importantly, both TILs and PBLs displayed similar levels of cytotoxic activity against autologous tumor cells. TILs and PBLs from 8 patients were also analyzed by a limiting dilution microculture system. Cloning efficiency was remarkably lower in TILs, and surface marker analysis of T cell clones confirmed that an accumulation of CD8+ lymphocytes, which displayed cytolytic activity in a lectin-dependent assay, occurred at the tumor site. The non-MHC-restricted cytolytic activity of TIL- and PBL-derived T cell clones against K562, A549, and allogeneic melanoma cells and the cytolytic activity against autologous tumor cells showed no significant differences. Only 53% of TIL clones released IL-2 in response to PHA + TPA stimulation, whereas 68% of PBL-derived clones were IL-2 producers. Moreover, most PBL- and TIL-derived clones released tumor necrosis factor alpha in response to mitogen stimulation.
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PMID:Peripheral blood and tumor infiltrating lymphocytes in non-small cell lung cancer: analysis at the population and clonal level. 217 60

The availability of lectin-resistant cell lines with altered carbohydrate moieties in cell surface glycoproteins and glycolipids has greatly facilitated study of the involvement of cellular glycoconjugates in tumor growth and metastasis. We present here a new animal model for metastasis study based on mouse Lewis lung carcinoma LL2 in vitro cell line. From this line, five lectin-resistant variant sublines were selected with the following lectins: wheat germ agglutinin (WGAR), Ricinus communis agglutinin II (RCA IIR) and Aleuria aurantia agglutinin (AAAR). The correlation of the lectin resistance with their in vitro and in vivo growth properties, and especially lung colonizing ability, were investigated. Three WGAR variants with well-preserved tumorigenicity revealed reduced metastatic ability, both spontaneous, after subcutaneous (s.c.) administration and experimental, after intravenous (i.v.) administration. The RCA IIR variant also possessed reduced spontaneous and experimental metastatic ability, but exhibited higher growth rate of local s.c. tumors. The AAAR variant possessed reduced spontaneous metastatic ability but its ability to colonize the lungs after i.v. administration was five-fold higher than that of the parent LL2 line, whereas its tumorigenicity remained unchanged. The relative differences among WGAR variants and parent LL2 line, concerning their experimental metastatic ability, remained similar in cyclophosphamide-modified mice to those in normal recipients.
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PMID:Lectin-resistant variants of mouse Lewis lung carcinoma cells. I. Selection and in vivo properties. 232 48

Lectin-resistant variants of mouse Lewis lung carcinoma LL2 cell line, selected with wheat germ agglutinin (WGAR), Ricinus communis agglutinin II (RCA IIR) and Aleuria aurantia agglutinin (AAAR) were studied. Total cellular glycopeptides of the parent LL2 line and of the five lectin-resistant variants were analyzed by gel filtration and affinity chromatography on immobilized concanavalin A and Lens culinaris agglutinin. The results revealed that low-metastatic WGAR and RCA IIR variants possessed less highly branched tri- and tetra-antennary N-acetyllactosaminic type glycans with a simultaneous increase in biantennary N-acetyllactosaminic type, oligomannosidic type or hybrid type glycans, as compared to the parent metastasizing LL2 cell line. These findings imply that cell surface carbohydrate changes may possibly be relevant for metastasis. However, the AAAR variant, which possessed reduced spontaneous metastatic ability after s.c. administration, but increased experimental metastatic ability after i.v. inoculation, exhibited apparently the same glycan pattern than the parent LL2 line. This particular variant is under investigation in order to find specific modification(s) of glycan(s) which could play a specific role in the metastatic process.
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PMID:Lectin-resistant variants of mouse Lewis lung carcinoma cells. II. Altered glycosylation of membrane glycoproteins. 232 49

Ninety-three cases of various types of human primary lung carcinomas have been studied by immunohistochemical technique and 5 cases of human primary lung adenocarcinomas by immunoelectron microscopic method with biotinized peanut lectin (PNA). The results showed that PNA staining was weak positive or negative in the normal bronchial epithelial cells which are adjacent to the carcinoma studied but strong or moderate positive in the carcinoma proper (P less than 0.05). The total positive rate of the lung carcinoma in this series is 81%. About 85% of the positive adenocarcinoma the PNA receptors were distributed along the luminal border, which corresponded with the linear electron-dense deposits on the luminal surface of the adenocarcinoma cell's membrane by immunoelectron microscopy. Squamous cell carcinoma, large cell carcinoma and small cell carcinoma, large cell carcinoma and small cell carcinoma were dominant in PNA cytoplasmic positive, while clear cell carcinoma in whole cell membrane positive. Some of the squamous cell carcinoma, large and small cell carcinoma showed microlumen by PNA staining that could not be found easily by conventional HE staining. It is suggested that these carcinomas mentioned above were poorly-differentiated adenocarcinoma or other types of carcinomas combined with adenocarcinoma. The results also assumed that the increasing of PNA receptor may be proportional to the differentiation of lung carcinoma cell. Therefore PNA receptor may be considered as a marker of carcinoma cell differentiation. It could be helpful in early diagnosis of lung carcinoma and prediction of the prognosis.
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PMID:[Immunohistochemical and immunoelectron microscopic observation of human lung carcinomas using biotinized peanut lectin (PNA)]. 239 36

This article documents a patient with lung carcinoma that produced three oncofetal antigens including alpha-fetoprotein (AFP), carcinoembryonic antigen (CEA), and human chorionic gonadotropin (hCG). Serum AFP, CEA, and hCG-beta-subunit were extremely high--118,000 ng/ml, 133 ng/ml and 0.9 ng/ml, respectively. Immunohistochemical staining of these tumor markers revealed that these proteins were present in different cells. The pattern of lectin affinity electrophoresis of AFP resembled that of hepatocellular carcinoma. Also investigated was the reactivity of serum CEA to monoclonal antibodies against peptide or sugar moieties. Serum CEA values measured by antipeptide monoclonal antibodies were higher than those measured by antisugar monoclonal antibodies. The demonstration of AFP, CEA, and hCG in different tumor cells suggests that three genomes were not reactivated together in a cell, and the lung carcinoma probably consisted of at least three clones of cancer cells with different phenotypes.
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PMID:A primary lung carcinoma producing alpha-fetoprotein, carcinoembryonic antigen, and human chorionic gonadotropin. Immunohistochemical and biochemical studies. 244 64


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