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)

Human cancers express organ-specific neoantigens (OSNs) that elicit immune responses in the tumor host. Leukocyte adherence inhibition, an in vitro assay that detects the antitumor immunity, was used to monitor the purification of the OSN from serum-free spent medium of tissue-cultured colon cancer cell lines (HCT-15 and SW-620). A monoclonal antibody (anti-p40) directed to a cross-reactive framework determinant of Mr 40,000 (p40) cell surface polypeptide, which was a principal component of the enriched isolate with OSN activity, was used to monitor the purification of p40 by enzyme-linked immunosorbant assay. About 50 liters of spent medium were generated from 20 m2 of cells, collected, concentrated, and then separated by anion exchange, molecular-sieve, and blue-Sepharose affinity chromatography. OSN and p40 activity coisolated. p40 was then purified by monoclonal antibody anti-p40 affinity chromatography. The affinity-purified fraction was enriched for both p40 and leukocyte adherence inhibition activity that was specific for leukocytes from colon cancer patients in blind leukocyte adherence inhibition assays. When affinity-purified p40 from colon and lung cancers was tested blind in a criss-cross fashion with leukocytes from colon and lung cancer patients, the positive responses were to the appropriate p40. The homologous colon cancer p40 molecule showed size and considerable charge microheterogeneity (pI 6.3 to 7.6). Affinity-purified p40 and OSN coisolated on hydrophobic interaction and hydroxylapatite high-pressure liquid chromatography. Note that not all colon cancer OSN activity was bound by the anti-p40 affinity column. However, unbound OSN activity also eluted from hydrophobic interaction high-pressure liquid chromatography at the same time as affinity-purified p40, and residual p40 activity was detected by enzyme-linked immunosorbant assay. The results indicate that a p40 glycoprotein from the cell membrane of colon cancer cells coisolates with fractions having OSN activity. Impurities do not seem to account for the OSN activity. The OSN epitope on the Mr 40,000 molecule is recognized by leukocytes from colon cancer patients and is distinct from the cross-reactive framework determinant recognized by mouse monoclonal antibody anti-p40.
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PMID:Identification of a Mr 40,000 polypeptide from colorectal cancer which expresses organ-specific cancer neoantigen activity as determined by leukocyte adherence inhibition. 241 55

Concentration of orosomucoid, pregnancy associated alpha 2-glycoprotein (alpha 2-PAG), Schwangerschaftsprotein 1 (SP1), placental specific-tissue protein 10 (PP10), placental specific-tissue protein 12 (PP12), alpha 1-Fetoprotein (AFP) were estimated in serum samples of 83 patients with lung cancer of stages II-IV. The proteins were determined by means of the single radial immunodiffusion, the rocket immunoelectrophoresis, the radioimmunoassay and the enzymeimmunoassay. Orosomucoid, PP12 and AFP serum concentrations of the cancer group compared with those of the control group, were increased significantly. Orosomucoid (control group: means = 0.828 g/l; s = 0.301; tumour group: mean = 2.16 g/l; s = 0.862); PP12 (control group: mean = 54.08 micrograms/l; s = 61.70; tumour group: mean = 122.52 micrograms/l; s = 131.16); AFP (control group: mean = 3.05 micrograms/l; s = 3.76; Tumour group: means = 8.29 micrograms/l; s = 17.75). alpha 2-PAG was found only in 37 cases of the tumour group; SP1 in 22 cases. PP10 (control group: mean = 2.25 micrograms/l; s = 0.866; tumour group: mean = 2.503 micrograms/l, s = 1.508). On condition that 2 tested parameters at least were estimated in the pathological range the sensitivity amounted to 0.64 and the specificity to 0.92.
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PMID:[Levels of tumor markers (orosomucoid, pregnancy-associated alpha 2-glycoprotein, pregnancy protein-1, placental specific-tissue protein 10, placental specific-tissue protein 12, alpha 1-fetoprotein) in the serum of patients with bronchial carcinoma]. 242 81

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

CA-549 is a circulating breast cancer-associated antigen that reacts with monoclonal antibody BC4E 549. Biochemical characterization of CA-549 revealed that it is an acidic (isoelectric point 5.2) glycoprotein that exhibits two bands by sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions of apparent molecular weights of 400,000 and 512,000. Immunohistochemical staining of unfixed frozen tissue sections of human breast tumors and a variety of benign tissues with BC4E 549 revealed no preferential staining of tumor over benign breast tissue and cross-reactivity with a wide range of other benign tissues including kidney, liver, lung, colon, pancreas, ovary, and spleen. Serum levels of CA-549 were initially tested by an enzyme-linked immunosorbent assay inhibition using BC4E 549. This assay showed that CA-549 concentrations were elevated in 19 of 27 sera from patients with advanced breast cancer compared to 0 of 22 and 0 of 129 sera from benign breast disease patients and healthy females, respectively. These preliminary data suggested that CA-549 was a useful breast tumor marker; thus BC4E 549 was adapted to a sandwich immunoradiometric assay format suitable for routine use in the clinical laboratory and its performance was evaluated on a panel of 668 serum samples. The test detected significant concentrations of CA-549 in the sera of 40 of 80 patients with advanced breast cancer, 1 of 30 with early breast cancer, 4 of 19 with advanced lung cancer, 2 of 40 with advanced colon cancer, and 5 of 29 with advanced prostate cancer. The test showed a high degree of specificity, producing false-positives in only 3 of 79 benign breast patients, 2 of 25 benign liver patients, 2 of 70 benign colon patients, 2 of 19 benign lung patients, 0 of 20 benign prostate patients, and 3 of 257 healthy individuals. These data represent an overall 50% sensitivity and 98% specificity as a test for advanced breast cancer. These data indicate that this immunoradiometric assay is a useful test for the detection of circulating CA-549 in advanced breast cancer patients and suggest that it may prove useful as a monitor in the management of that disease.
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PMID:Serum levels and biochemical characteristics of cancer-associated antigen CA-549, a circulating breast cancer marker. 244 35

Lymphocytes from mediastinal lymph nodes of 9 patients with primary lung cancer were fused with murine myeloma cells (P3U1). One of the clones (4G12) was stable for secretion (10 micrograms/ml) of human IgM lambda for 24 months. The antigen detected by 4G12 was sensitive to both trypsin and periodic acid-Schiff treatment. It immunoprecipitated a glycoprotein with an Mr of 65,000 upon analysis in sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reduced conditions. Immunohistochemical staining demonstrated that 4G12 possessed a high reactivity to squamous cell carcinomas of the lung (29 of 29) and also reacted with other lung carcinomas [adenocarcinomas (14 of 20) and large cell carcinomas (3 of 8)] and with some nonpulmonary malignant tumors (15 of 56). However, it did not react with small cell carcinomas of the lung. No benign tumors (0 of 26) so far tested have been positive. 4G12 did not react with most of the normal tissues; an exception was that it was weakly reactive on the glandular cells of the trachea and bronchi and on the proximal tubular cells of the kidneys. Thus 4G12 showed a broad reactivity to malignant tumors (68% of lung carcinomas, 27% of nonpulmonary carcinomas, and 0% of benign tumors). The reactivity of 4G12 on tissues from squamous cell carcinomas of the lung indicated that the expression of the antigenic determinant was much more in the well-differentiated grade than in the poorly differentiated grade. Thus the antigen detected by 4G12 appears to be related to tumor differentiation. Moreover, fluorescence-activated cell sorter analysis demonstrated that the expression of the antigen epitope depended on the cell cycle (G2-M). These data suggest that the 4G12 monoclonal antibody detects a new tumor-associated antigen that is recognized by the human immune system.
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PMID:Characterization of a human monoclonal antibody with broad reactivity to malignant tumor cells. 245 61

Oligoclonal T-cells have been generated by sensitization of peripheral blood mononuclear cells from lung cancer patients to a lung cancer tumor-associated antigen (TAA). A factor similar to the antigen-specific glycoprotein factor in the serum of these cancer patients was found in the supernatant of the oligoclonal T-cells. The factor from the T-cell supernatant had specificity for lung cancer TAA and induced stimulation of normal lymphocytes of the CD8 phenotype when mixed with lung cancer TAA. Furthermore, the factor blocked the ability of lymphocytes from lung cancer patients to recognize lung cancer TAA. Both the factor from lung cancer serum and from the oligoclonal T-cells were absorbed on a lung cancer-associated antigen-coupled immunosorbent column. On FPLC-gel filtration the desorbed fractions from the immunosorbent column from both sources showed activity in the same molecular weight range, 70-90 kD. Heteroantisera raised against the factor from serum and against the factor from the oligoclonal T-cell supernatant bound about the same portion of lymphocytes from lung cancer patients as measured by immunofluorescence, while only a minor fraction of cells from patients with unrelated cancers and from healthy persons were labelled on incubation with the antisera. These results support the hypothesis that an antigen-specific factor found in serum of cancer patients is produced by antigen-stimulated T-cells, possibly of the CD8 phenotype. This putative antigen-specific suppressor factor and the tumor antigen-reactive lymphocytes of the patient seem to share similar idiotopes.
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PMID:Role of T-lymphocytes in production of a cancer-associated protein factor in serum from lung cancer patients. 246 70

Authors have studied AFP serum levels in 289 lung cancer. Only 2 cases (0.7%) showed little increase of this glycoprotein and liver pathologies were present in both patients, authors believe immunohistochemical study is necessary in lung cancers that show AFP increase.
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PMID:Alpha-fetoprotein as tumor marker in lung cancer diagnosis. 248 Apr 34

CA130 is a glycoprotein which is recognized by monoclonal antibodies-(130-22 and 145-9) produced by immunization with human lung adenocarcinoma cell line (PC-9). CA130 is considered to be a new tumor marker, different from CA125, since it has a separate antigenic determinant. We used the D-7111 kit (Daiichi Radioisotope Laboratories, Ltd.) to measure the serum level of CA130 in 290 patients with lung cancer, 171 patients with noncancerous lung disease (N-CLD) and 93 healthy adults. In addition, CEA, CA19-9, CA125 and sialyl SSEA-1 antigen (SLX) were also measured for the same serum samples when possible. The cutoff level for CA130 was 35 U/ml. The overall positive rates for CA130 were 32% in the lung cancer patients, 23% in the N-CLD patients and 0% in the healthy adults. The positive rate in the lung cancer patients was significantly higher than in the N-CLD patients (p less than 0.05). As a function of the histological type of lung cancer, the positive rates for CA130 were 44% in 120 patients with adenocarcinoma, 17% in 115 patients with squamous cell carcinoma, 33% in 36 patients with small cell carcinoma, 42% in 12 patients with large cell carcinoma and 29% in 7 patients with miscellaneous cell type. The positive rate in the patients with adenocarcinoma was significantly higher than in the patients with squamous cell carcinoma (p less than 0.001).(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Clinical evaluation of serum CA130 in patients with lung cancer]. 257 55

Small cell lung cancer is distinguished from other lung cancer histologic types by possessing a variety of neuroendocrine properties. Anti-Leu-7 is a monoclonal antibody that recognizes a 110,000-dalton molecular weight glycoprotein initially described on natural killer cells and subsequently reported on a variety of normal and malignant neural and neuroendocrine cell types. We have found intense anti-Leu-7 binding to a large number of small cell lung cancers, while other lung cancer types were negative or showed only weak and focal binding. Other antigens expressed by natural killer cells, lymphocytes, and monocytes were never or less often expressed on small cell lung cancer cells. In addition, we report for the first time anti-Leu-7 binding by carcinoids, carotid body tumors, pheochromocytomas, endocrine cells of the fetal bronchus and the adult intestine, and select pancreatic islet cells. Anti-Leu-7 binding by small cell lung cancer is consistent with a derivation from pulmonary precursor cells, and anti-Leu-7 staining is clinically useful for the identification of human neuroendocrine tumors of the amine precursor uptake and decarboxylation ("APUD") type.
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PMID:Small cell lung cancer, endocrine cells of the fetal bronchus, and other neuroendocrine cells express the Leu-7 antigenic determinant present on natural killer cells. 257 40

The nature of the antigen recognized by the murine monoclonal antibody A7 (Mab A7) against human colorectal carcinoma was investigated using immunochemical and biochemical techniques. Binding activity of 125I-labeled Mab A7 was examined using various human cancer cell lines. Mab A7 gave the highly specific binding to colon cancer cell lines, SW1116 and WiDr, and gave only a very weak or no reactivity to gastric cancer cell lines, pancreas cell lines or lung cancer cell lines. SDS-polyacrylamide gel electrophoresis (SDS-PAGE) and immunoblotting of the extractable antigen from SW1116 showed a single band at approximately 45,000 dalton formed by 125I-labeled Mab A7. Treatment of SW1116 with sodium periodate, pronase and ficin resulted in the loss of antigenic activity. These data strongly suggest that the antigen recognized by Mab A7 is composed of glycoprotein. Competitive binding analysis to the surface of the colon cancer cell line using polyclonal anti-CEA and Mab A7 as well as immunoblotting analysis using monoclonal anti-CEA and Mab A7 suggested that the antigen recognized by Mab A7 was different from CEA. Moreover, this antigen was also found in surgical specimens of colorectal cancer patients and its molecular property was identical to the antigen extracted from SW1116.
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PMID:Immunochemical characterization of the antigen recognized by the murine monoclonal antibody A7 against human colorectal cancer. 271 85


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