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)

Levels of carcinoembryonic antigen (CEA), alpha-fetoprotein (AFP), ferritin and alpha 2-pregency associated glycoprotein (alpha-2-PAG) were determined in patients with confirmed lung cancer at the time of diagnosis and in serial determinations during and after radio- or chemotherapy. Whereas AFP levels were not elevated in patients with lung cancer, increased levels of CEA, ferritin and alpha-2-PAG were found in more than 50% of the patients. The results suggest that determination of CEA, ferritin and alpha-2-PAG in the serum of patients with lung cancer may be useful to detect metastases or recurrences and to monitor the results of treatment. Furthermore, in this study CEA and ferritin could be demonstrated in extracts of lung tumor tissues by specific antisera.
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PMID:Carcinoembryonic antigen, alpha 1-fetoprotein, ferritin, and alpha 2-pregnancy associated glycoprotein in the serum of lung cancer patients and its demonstration in lung tumor tissues. 7 56

A case of lung cancer with elevated amylase activity in serum, urine, and tumor tissue was studied electron microscopically and biochemically. Ultrastructurally, there were numerous electron-dense granules in the cytoplasm of most tumor cells. These granules were located in the apical region of tumor cells and had a single limiting membrane, associated with a clear zone just beneath it. Furthermore, circular, lamellar and annulate structures, which closely resembled those observed within zymogen granules of the salivary glands in postnatal mice and rats, were sometimes recognized within these granules. These observations suggested that these granules were identical to a postnatal or immature form of zymogen granules in salivary glands. Biochemical analysis confirmed that the amylases obtained from the tumor tissue were composed of the sialic acid-containing glycoprotein, which was not found in normal amylases. A possible histogenesis of the amylase-producing lung cancer was briefly discussed.
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PMID:Amylase-producing lung cancer: ultrastructural and biochemical studies. 89 Jun 57

Thrombospondin (TSP), a large glycoprotein present in platelets, and various normal and tumor tissues, has recently been shown to promote cell adhesion and platelet aggregation. Most importantly because TSP has been shown to promote metastasis of melanoma tumor cells to the lung in a murine model (1) and since thromboembolic events commonly occur in patients afflicted with metastatic tumors, we explored the role of TSP in human cancer by measuring TSP blood levels in patients with various malignant neoplasms. Blood TSP levels were measured by indirect enzyme-linked immunoadsorbent assay (ELISA) from 20 control subjects, 22 patients with gastrointestinal (GI) cancer, 18 patients with breast cancer, and 17 patients with lung cancer. Control subjects consisted both of healthy subjects and acutely ill patients with no malignancies. TSP levels of both healthy and acutely ill controls were found to range between 245-440 ng/ml with a mean of 365 ng/ml. In contrast, elevated levels of TSP greater than the mean value of 400 ng/ml for controls ranging between 590-3,650 ng/ml were found in 20/22 (91%) patients with GI malignancies, 13/18 (72%) patients with breast cancer, and 15/17 (88%) with lung cancer. Mean TSP levels of GI, breast, and lung cancer patients were 3, 2, and 3 fold greater than controls, respectively. Increased blood TSP levels in patients were not due to increased levels of platelets since both control and patient groups had platelet counts within the normal range. These results suggest that TSP may play a role in tumor cell metastasis in man and could serve as a blood marker for metastasis.
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PMID:Thrombospondin levels in patients with malignancy. 150

Lung carcinomas represent a heterogeneous group of tumours with large variations in the biochemical, clinical, morphological and pathological manifestations. Despite the neuroendocrine features of small cell lung cancer (SCLC), it is today generally accepted that all types of lung cancer emanate from a common endodermally derived multipotent stem cell of the bronchial epithelium. NCAM (neutral cell adhesion molecule) has been shown to be a sensitive marker of SCLC. The presence of NCAM, with the alpha (2,8) polysialic acid units characteristic of embryonal NCAM, in SCLC and in a portion of NSCLC, seems to correlate with the malignant behaviour and prognosis of the tumours, suggesting that NCAM may have a functional role in the clinicopathological manifestations of lung cancer. Fuc-GM1 with 2-hydroxy fatty acids as a characteristic component of the ceramide has been found to be a unique ganglioside of SCLC, detected in the tissues as well as in serum from SCLC patients using specific monoclonal antibodies. Accumulation of sialylated and fucosylated polylactosamine type 2 carbohydrate glycolipid and glycoprotein antigens was found in serum and tissues of lung tumours in accordance with what is described in gastrointestinal carcinomas, and these antigens may be regarded as general carcinoma antigens irrespective of organ. Sialylated and fucosylated type 1 antigens, and gangliosides with NeuAc alpha (2,6)Gal linkage were also accumulated in lung cancer. The human immune system has been found to recognize lung cancer carbohydrate antigens, which might be human lung cancer autoantigens.
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PMID:Carbohydrate antigens in human lung carcinomas. 152 May 24

Pulmonary surfactant protein A (SP-A) is known to be a major phospholipid-associated glycoprotein in pulmonary surfactant, which is specific to the lung. Immunohistochemically, expression of SP-A in tumor tissues is found in approximately 50% of patients with lung adenocarcinoma but not in the other histologic types of lung cancer of metastatic lung tumors. In this study, the SP-A content of pleural effusions was determined using an enzyme-linked immunosorbent assay. These results showed that approximately 40% of patients with lung adenocarcinomas (27 of 67) had high levels of SP-A (greater than 500 ng/ml) in their pleural effusions. By contrast, patients with other histologic types of lung cancers, adenocarcinomas of different primary sites, and tuberculosis had low levels of SP-A in their pleural effusions. The determination of SP-A in malignant effusions will contribute to distinguishing primary lung adenocarcinoma from adenocarcinomas of miscellaneous origin.
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PMID:Pulmonary surfactant protein A in pleural effusions. 159 82

McAb LC-1 was derived from fusion of myeloma cells and murine spleen cells immunized with human lung adenocarcinoma SPC-A-1 cells. The immunoglobulin isotype of LC-1 belonged to IgM. LC-1 was direct against the common epitope of lung cancer. It not only reacted with small cell lung cancer but also with non small cell lung cancer. LC-1 was purified from ascitic fluid by euglobulin precipitation and Sephadex G-200 filtration chromatography, and was iodinated with Iodogen, the specific reactivity of 125I-labeled LC-1 was determined by comparing standard curve with self-displacement curve. The immunoreactive fraction of 125I-LC-1 was determined by its binding to excess of antigen. The RIA data were plotted in Scatchard-form as binding of SPC-A-1 cells to LC-1. The binding constant of LC-1 binding to SPC-A-1 was 4.8 x 10(8) M-1. The LC-1 binding sites on SPC-A-1 were 7.2 x 10(4) per cell. The RIA inhibition test showed that LC-1 and LAC-122 (another IgM isotype McAb reacted only with non small cell lung cancer) had no cross-reactivity. The treatment of SPC-A-1 cells by proteinase and sodium periodate inhibited LC-1 binding to these treated target cells by 39% and 66% respectively. These results suggested that the biochemical nature of antigen recognized by LC-1 was glycoprotein.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Study on binding characteristics of 125I-labeled McAb LC-1 to lung adenocarcinoma cells in vitro and in vivo]. 159 1

Murine IgG1 monoclonal antibodies (mAbs), ITK-2 and ITK-3, were generated against a small-cell lung cancer (SCLC) cell line. Enzyme-linked immunosorbent assay using a variety of established cell lines as substrates, immunoperoxidase staining of freshly frozen tissue sections, and fluorescence-activated cell sorter analysis of peripheral blood leukocytes showed that these mAbs recognize a part of the SCLC-associated cluster 1 antigen. In immunoprecipitation studies, both ITK-2 and ITK-3 bound to a 145-kDa glycoprotein of SCLC cell membrane extracts, as did MOC-1 and NKH-1, which both recognize the cluster 1 antigen. However, because the binding of 125I-labeled ITK-2 to SCLC cells was not inhibited by MOC-1 or NKH-1, the binding site of ITK-2 on SCLC cells appeared to be different from that of either MOC-1 or NKH-1. Unexpectedly, binding of 125I-labeled ITK-2 to SCLC cells increased in the presence of ITK-3. This ITK-3-induced increase in ITK-2 binding was due partly to an increase in the number of binding sites for ITK-2 on SCLC cells. Addition of ITK-3 may, therefore, improve the effectiveness of ITK-2-based tumor detection or therapy.
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PMID:Two monoclonal antibodies against small-cell lung cancer show existence of synergism in binding. 164 75

Twenty-five non-small cell lung cancer (NSCLC), 42 small cell lung carcinoma (SCLC), one extrapulmonary small cell carcinoma, 4 carcinoid, and 13 non-lung cancer cell lines were analyzed for human chorionic gonadotropin (HCG) and related glycoprotein hormones. HCG or its subunits were present in 72% of NSCLC, 10% of SCLC, one extrapulmonary small cell carcinoma, 3/4 carcinoids and 2/13 non-lung cancer cell lines. Related glycoprotein hormones were undetectable. These data indicate a frequent production of HCG or its subunits by NSCLC cell lines and cell lines from tumors with carcinoid features. They confirm the clinical inclusion of carcinoids under the broad category of NSCLC rather than SCLC despite their neuroendocrine features. Clinicians should not assume that undifferentiated NSCLC with HCG production represent germ cell tumors.
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PMID:Human chorionic gonadotropin and related glycoprotein hormones in lung cancer cell lines. 164 86

The in vivo localization of a polyclonal antibody (pAb) against a glycoprotein with a molecular mass of 68 kDa (GP68), which was found in developing mouse brain, was studied in murine tumor models to evaluate potential applications of this antibody for in vivo radioimmunodetection and/or therapy of cancer. The tissue distribution of 125I-labeled GP68 pAb 3 days after i.v. injection into mice bearing four different kinds of solid tumor revealed a high uptake ratio by adenocarcinoma 755 and Lewis 3LL lung cancer. In contrast, the uptake ratio was low in mice bearing Ehrlich solid tumor and sarcoma-180 (S-180). These uptake ratios accorded well with the in vitro binding activity of this antibody with the tumor cells. In an immunoscintigraphic study, adenocarcinoma 755 was successfully visualized with 67Ga-labeled GP68 pAb. The results of these biodistribution and in vivo radioimmunoscintigraphic studies suggest that GP68 antibody may be applicable to the diagnosis and/or therapy of cancer.
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PMID:Radioimmunoimaging of tumors with radioactive antibody against a glycoprotein (GP68) found in developing mouse brain. 169 92

The Leu-19 (CD56) antigen, which is recognized by anti-Leu-19 and NKH-1 monoclonal antibody, is a 200,000-220,000 molecular weight (MW) glycoprotein that is expressed predominantly on human natural killer (NK) cells that mediate major histocompatibility complex (MHC)-unrestricted cytotoxicity. However, cross-reactivity of this antibody has been observed in lung cancer, and in muscle and neural tissues. In the present study, we used the immunoperoxidase technique to examine the expression of Leu-19 antigen in human thyroid epithelial cells. In normal thyroid tissues (n = 4), thyroid tissues from Graves' patients (n = 7) and benign thyroid tumours (n = 7), thyroid epithelial cells expressed Leu-19 antigen in all cases. In thyroid papillary carcinoma (n = 6) there was no expression in four cases. This staining pattern of anti-Leu-19 antibody is similar to that of anti-thyroid peroxidase antibody. These findings implicate that the expression of Leu-19 antigen is closely related to the differentiation of thyroid epithelial cells.
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PMID:Detection of Leu-19 (CD56) antigen on human thyroid epithelial cells by an immunohistochemical method. 170 51


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