Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0242379 (lung cancer)
 71,905 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Lectins, which are well known to have an ability to bind with specific carbohydrate residues of glycoprotein, have been used to examine cellular changes associated with malignant transformation. For the analysis of mucus glycoprotein of goblet cells in the tracheobronchial epithelium, 192 paraffin-embedded sections from 54 autopsy cases including the cases with a history of mustard-gas (MG) exposure were stained with seven plant lectins using PAP method. PNA binding with no neuraminidase treatment as well as BSA-1 binding was observed most frequently in MG-exposed lung cancer cases. The proportion of cases positive for SBA binding in MG-exposed and/or lung cancer cases had a statistical difference from non-MG-exposed non-lung cancer cases. These observations may indicate a large heterogeneity in oligosaccharide chains of mucus glycoprotein and suggest its incomplete or abnormal synthesis, which is most likely to be due to previous exposure to carcinogen, such as MG.
 ...
PMID:An altered lectin binding to mucus glycoprotein in goblet cells of human tracheobronchial epithelium among former mustard-gas workers. 330 28

In studies aimed at developing monoclonal antibodies against lung adenocarcinomas, we produced a murine monoclonal antibody designated 130-22 by immunizing mice with lung cancer cells. Since in immunoperoxidase staining experiments this antibody was reactive not only with lung adenocarcinomas but also with ovarian carcinomas, we examined its relationship to the ovarian cancer marker CA125, an antigen recognized by monoclonal antibody OC125 produced by immunization of mice with ovarian carcinoma cells. Although CA125 antigen was adsorbed by 130-22 antibody, 125I-labeled 130-22 did not compete with OC125, indicating that although these two antibodies recognized CA125 antigen, they reacted with separate antigenic determinants. The antigen defined by both antibodies was thought to be heat-labile glycoprotein with a molecular weight of over 1,000,000. A series of immunoradiometric assays was developed using combinations of two monoclonal antibodies in a simultaneous forward sandwich mode. Mixed monoclonal antibodies may provide a more sensitive assay for the detection of CA125 than the homologous assay, in which OC125 was used both as a tracer and as a catcher. These results indicate that CA125 is an antigen with two separate epitopes present in both ovarian and lung adenocarcinomas and that combination use of monoclonal antibodies reactive with different antigenic determinants will give certain advantages to the immunoradiometric assay of cancer markers.
 ...
PMID:Recognition of ovarian cancer antigen CA125 by murine monoclonal antibody produced by immunization of lung cancer cells. 331 84

A hybridoma producing monoclonal antibody (H11) directed to lactoneotetraosylceramide (paragloboside) has been established from spleen cells of a mouse immunized with paragloboside. The monoclonal antibody H11 (immunoglobulin M type) was selected from five clones showing different reactivities with paragloboside. The monoclonal antibody was highly specific to paragloboside and lacked reactivity with other glycolipids including glucosylceramide, lactosylceramide, globotriaosylceramide, globotetraosylceramide, gangliotriaosylceramide, gangliotetraosylceramide, and GalNAc beta 1-4[NeuAc alpha 2-3]Gal beta 1-4Glc beta 1-1Cer. However, the monoclonal antibody (H11) was found to bind to lactosamine-containing glycolipids at their terminals, such as i- and I-type glycolipids as well as paragloboside. A two-step sandwich radioimmunoassay method for paragloboside antigen in serum was established by using the monoclonal antibody. The mean paragloboside antigen concentration in the sera from 20 normal individuals was 25.3 ng/ml. If the cutoff value was set at 80.9 ng/ml [25.3 + 2 x 27.8 (SD)], only 1 of 20 healthy controls had an elevated paragloboside value in the serum, whereas sera from 9 of 12 (75.0%) hepatoma, 4 of 10 (40%) pancreatic cancer, 16 of 40 (40.0%) stomach cancer, and 6 of 10 (60%) lung cancer patients had elevated paragloboside values. Sera from 3 of 8 hepatitis patients and 7 of 10 liver cirrhosis patients were estimated to be positive but sera from 16 patients with benign disease had paragloboside levels lower than the cutoff value. A larger amount of the antigen was found in liver metastases from colorectal carcinoma compared to the normal counterpart. The antigen was also detected in the medium of various human cancer cells and meconium. However, the antigen in the sera, medium, meconium, and cancer tissue seemed to be associated with glycoprotein or lipoprotein, because most of the antigen activity was eluted in the void volume fraction on high-performance liquid chromatography with a gel filtration column.
 ...
PMID:Detection of patients with cancer by monoclonal antibody directed to lactoneotetraosylceramide (paragloboside). 334 24

Monoclonal antibody 5E8 which is specific for a Mr 160,000 glycoprotein (gp160) on the surface of human lung cancer was radiolabeled with 125I. Radiolabeled 5E8 antibody is shown here to suppress the growth of gp160 positive human lung tumor cell lines in a dose-dependent fashion, but this same radiolabeled antibody does not alter the growth of gp160 negative lung tumor cell lines. Neither the unlabeled 5E8 nor a control radiolabeled monoclonal antibody has any effect upon the growth of gp160 positive tumors. The specificity of radiolabeled antibody mediated tumor killing is further demonstrated by the ability of unlabeled 5E8 to inhibit tumor killing by 125I-5E8. The efficiency with which the labeled tumor specific antibody suppressed tumor colony formation is enhanced by increasing the molar ratio of 125I to 5E8. This ratio could be increased to a level of two without affecting the capacity of the antibody to bind to the cell surface antigen. An attempt to increase the efficiency of tumor killing by the addition of a second antibody subsequent to incubation with 125I-5E8 was unsuccessful. These results indicate that 125I is a viable isotope and gp160 represents an appropriate target for radioimmunotherapy of human lung cancer.
 ...
PMID:Selective growth inhibition of human lung cancer cell lines bearing a surface glycoprotein gp160 by 125I-labeled anti-gp160 monoclonal antibody. 279 Jul 90

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.
 ...
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

A monoclonal antibody (5E8) has been used to identify and structurally characterize a previously unreported macromolecule present on the surface of human lung tumors. This antibody was derived from a hybrid clone that was produced using spleen cells of mice immunized with a surgically excised squamous cell carcinoma. Using immunofluorescence, the 5E8 antibody was observed to stain many different human lung tumor cell lines and surgically excised human lung tumors including squamous cell carcinomas, adenocarcinomas, alveolar carcinomas, and a portion of the large cell tumors tested. With few exceptions, notably the basal layer of the skin, little or no detectable staining of 5E8 to normal human tissues (lung, brain, kidney, heart, stomach, breast, erythrocytes, or lymphocytes) was observed. The 5E8 antibody was used to immunoprecipitate detergent lysates of biosynthetically labeled or surface radioiodinated lung tumors. Analysis of the immunoprecipitates by sodium dodecyl sulfate gel electrophoresis revealed a major band and a faster migrating second minor band. The molecular weights of these two proteins were estimated to be 160,000 and 120,000, respectively. The addition of a reducing agent to the gels did not alter the migration pattern of the immunoprecipitated macromolecules. The removal of a terminal carbohydrate, sialic acid, did not restrict the binding of 5E8 to the tumor-associated antigen. However, labeling studies using galactose oxidase and tritiated borohydride revealed the presence of galactose on the immunoprecipitated protein. This major Mr 160,000 glycoprotein that was identified on two different human lung tumor cell lines was also found on a human large cell tumor tissue obtained by surgical biopsy. The 5E8 antibody and the Mr 160,000 glycoprotein that it recognizes represent two very useful components with which to test several new antibody-mediated drug delivery systems in the treatment of human lung tumors. The tumor-associated glycoprotein also represents a potential analyte for a diagnostic or prognostic immunoassay for lung cancer.
 ...
PMID:Membrane-associated glycoprotein (gp 160) identified on human lung tumors by a monoclonal antibody. 353 80

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.
 ...
PMID:Generation of monoclonal antibodies against human lung squamous cell carcinoma and adenocarcinoma using mice rendered tolerant to normal human lung. 373 Nov

We have measured the following ten serum proteins in a sample of 290 patients presenting with possible lung cancer: carcinoembryonic antigen (CEA), alpha 1-acid glycoprotein (AGP), C-reactive protein (CRP), ferritin (FER), prealbumin (PAB), third component of complement (C3), immunoglobin E (IgE), alpha 2-pregnancy-associated glycoprotein (PAG), beta 2-microglobulin (beta 2-m) and retinol binding protein (RBP). It is found that, with the exception of PAG, C3 and IgE, there are significant differences between protein concentrations in the subsequently diagnosed cancer and non-cancer patients. However, protein concentrations in the cancer patients who were suitable for surgery do not differ significantly from the concentrations in inoperable patients. The prognostic significance of the proteins in the inoperable and operable cancer patients is also envisaged. In the operable group C3 appears to be useful, whilst AGP and RBP are prognostic indicators in the inoperable group.
 ...
PMID:The role of serum tumour markers to aid the selection of lung cancer patients for surgery and the assessment of prognosis. 383 Jul 27

A relatively simple, specific and sensitive radioimmunoassay system has been developed for the detection of heterophile Hanganutziu-Deicher (H-D) antigen(s) and antibodies. The 125I-labeled H-D antigen-active molecule used for the assay is a bovine erythrocyte major glycoprotein previously found to have a strong H-D antigen potency. The antigen-antibody complex was precipitated with normal human serum as the carrier protein, followed by the addition of rabbit anti-human IgG F(ab')2 serum. With this method, different H-D antigen-active molecules were compared for heterophile H-D antigen potency with reasonable sensitivity detecting about 0.3 ng of cold glycoprotein. 8 different lung cancer tissues were assayed for H-D antigen. The sera from the 8 lung cancer patients were also screened by ELISA and RIA in an attempt to correlate expression of H-D antigen on tissues with elevation of H-D antibodies. The results showed that all patients' tissues expressed the antigen(s) but only 3 of them had abnormal levels of H-D antibodies. This could have been due to excess antigens in circulation or immune complexes.
 ...
PMID:A potential radioimmunoassay system for detection of Hanganutziu-Deicher type heterophile antigen(s) and antibodies in tissues and fluids. 387 40

Recent attempts implicating glycoproteins have been focused on the study of fibronectin. This glycoprotein was observed especially in cellular adhesivity processes. Some works were direct to detect the fibronectin concentration in plasma and in other biological fluids to relate increased or decreased levels in pathological features. In this paper we describe a study on plasma fibronectin in lung cancer patients during the course of the disease.
 ...
PMID:[Immuno-oncologic monitoring of patients with bronchial carcinoma. II. Plasma fibronectin determination]. 397 25


<< Previous 1 2 3 4 5 6 7 8 9 10 Next >>