Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0699790 (colon cancer)
 28,837 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We have previously shown that an autocrine factor (CRDGF) of molecular weight 25,000 is produced by the HT29 human colon cancer cell line. Although CRDGF was shown to inhibit the binding of epidermal growth factor (EGF) to its receptor, several lines of evidence suggested that it was distinct from EGF or transforming growth factor-alpha (TGF-alpha). In order to check the possibility that CRDGF represents a new member of the EGF family, a four-step purification protocol involving acid gel filtration, cation-exchange high-performance liquid chromatography (HPLC), C18 reversed-phase HPLC and gel permeation HPLC was used to purify this protein to homogeneity. The purified material exhibited a 22 kDa molecular mass on SDS-PAGE. Partial N-terminal amino acid sequence of CRDGF showed identity to amphiregulin (AR), an EGF-related protein. Western blotting experiments using AR-specific antiserum confirmed that CRDGF and AR are identical proteins. In addition, we showed that AR, like EGF or TGF-alpha stimulated the phosphorylation of the epidermal growth factor receptor (EGF-R) on tyrosine residues. This indicates that the AR intracellular signalling pathway involves the activation of EGF-R kinase.
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PMID:Colorectum cell-derived growth factor (CRDGF) is homologous to amphiregulin, a member of the epidermal growth factor family. 133 77

A biotinamine probe, 5-(biotinamido)pentylamine, was used for biotin-labeling of proteins in HT29 colon cancer cell extracts by endogenous transglutaminase activity. The biotin-labeled protein substrates were isolated and recovered by avidin-affinity chromatography. The proteins were separated using SDS-polyacrylamide gel electrophoresis, electroblotted onto a polyvinylidene difluoride membrane, visualized using Coomassie blue, cut out, and sequenced. Amino acid sequence data identified human fructose-1,6-bisphosphate aldolase A, an intracellular protein, as a substrate for cellular transglutaminase.
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PMID:Identification of transglutaminase substrates in HT29 colon cancer cells: use of 5-(biotinamido)pentylamine as a transglutaminase-specific probe. 135 85

A colorectal antigen (IOR-C2) was characterized by a monoclonal antibody produced against the colon cancer cell line SW1116. By immunohistochemical staining the antigen was abundant and strongly expressed in epithelium of normal colon whereas colorectal carcinomas showed a more variable and heterogenous reactivity to the antibody (IOR-C2). Radioimmunoprecipitates of SW1116 cell homogenates showed a 160-200 kD band in SDS gels. Physicochemical characterization indicate that at least two IOR-C2 reactive sites are present on the antigen tested and that it is mainly an 0-linked glycoprotein carbohydrate chain which can also be N-linked to the protein. The expression of IOR-C2 mimics that of the colon associated antigen (CAA) and NCC-CO-450 antigen but is distinct from these with regard to its expression in carcinomas as well as its physicochemical characteristics.
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PMID:Characterization of the colorectal antigen IOR-C2. 137 20

An antigen, protein X (Px), was purified from immune complexes isolated from malignant pleural effusions from patients with adenocarcinoma of the lung by EDTA treatment, PEG 8000 precipitation, protein A affinity chromatography, and Sephadex G-200 separation in the presence of 3 M NaCl. The purified antigen had a M(r) 17,000 by SDS-PAGE, and consisted of isoelectric species of pI 6.3 and 6.6. Purified Px recombined with Ig isolated from pleural fluids from patients with lung adenocarcinoma, but not with Ig from patients with breast carcinoma. Using an autologous human and heterologous chicken antibody, Px was found, by immunohistology, in the cytoplasm of some of the well-differentiated lung adenocarcinoma cells, but was not seen in normal lung or a variety of other malignant tissues. A liquid-phase competitive-inhibition RIA was developed. Over 30 ng/ml of Px were found in 9 of 15 pleural fluids from patients with lung carcinoma, none of 20 from patients with breast, ovary, stomach or colon cancer, and in 3 of 15 patients with unknown primary tumor. Our data suggest that Px may be a lung-cancer-associated autoantigen which can elicit a host humoral response in vivo.
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PMID:Characterization of a lung-cancer-associated auto-antigen. 139 30

We have compared by SDS-PAGE Western blotting the molecules detected by two human monoclonal antibodies, C-OU1 and 16.88. The antibodies have previously been shown to detect a cytoplasmatic antigen with an Mr of 43 kD present in colon adenocarcinoma cell lines and in colon cancer tissues. We now demonstrate that these antibodies differ significantly in their fine specificity, resulting in a quite dissimilar tumor selectivity. The antibody 16.88, in addition to reactivity with the 43-kD molecule, also recognizes a 190-kD molecule present both in melanoma cells and in cells previously reported as 16.88 antigen positive. The 16.88 antibody does not detect a 43-kD molecule in extracts of melanoma cells. The 190-kD component was not detectable in hepatoma or mamma carcinoma cells, both of which showed presence of the 43-kD molecule. The C-OU1 antibody shows no reactivity with the 190-kD molecule in any of the cells tested or with other proteins in melanoma cells. Radiolabeled 16.88 antibody shows better localization to melanoma cancer than to colon cancer xenograft transplanted onto nude mice. These findings indicate the presence of a tumor-associated antigen not previously described and have obvious implications for potential clinical uses of the antibodies.
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PMID:Antigens recognized by two human monoclonal IgM anticolon cancer antibodies, 16.88 and C-OU1 (B9165). 175 84

A total of 72 human leukemia-lymphoma cell lines were studied for reactivity with the monoclonal antibody (MAb) A7, an anti-human colon-cancer-cell-associated antigen reagent, by indirect membrane immunofluorescence. Nine of the 72 cell lines expressed the antigen recognized by A7 MAb. Five of the 34 T-cell lines, 2 of the 21 B-cell lines, and 2 of the 3 non-lymphoid-non-myeloid cell lines were reactive with A7 MAb. By means of SDS-PAGE and immunoblotting, the antigens isolated from both colon cancer cell lines (WiDr, SW1116 and LoVo) and leukemia cell lines (A3/KAWAKAMI, H9, RPMI 8226 and SPI-801) showed an identical MW of 42-43 kDa. The non-glycosylated antigen recognized by A7 MAb, which was expressed on both the colon cancer line (SW1116) and the leukemia line (H9) in the presence of tunicamycin, also showed an identical MW of 36 kDa. However, the quantity of the antigen in the leukemia cells was significantly lower than in the colon cancer cells. Although expression of this colon-cancer-associated antigen in the non-colon cancer cells is real, the significant expression of this antigen in colon-cancer cells makes it useful for clinical monitoring of colon cancer patients.
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PMID:Identification and characterization of a colon-cancer-associated antigen expressed on leukemia-lymphoma cell lines. 199 51

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

A high molecular weight, mucous glycoprotein (MG) from the pleural fluid of lung adenocarcinoma was purified by the DEAE-cellulose, gel-filtration and wheat germ agglutinin affinity chromatography. Protein portion of the molecule was composed of amino acids rich in serine, threonine and proline, but methionine and tyrosine concentrations were relatively low. About 65% of the weight, was composed of galactose, galactosamine, glucosamine, fucose and sialic acid. The gel-filtration pattern on Sepharose 4B revealed Mr greater than 10(6) Da. The SDS-PAGE pattern revealed a main band at the position of the Mr about 350 kDa under the reducing condition. Rabbit antibody against this molecule recognized mainly the peptide portion, and the radioimmunoassay (RIA) using the double antibody method was developed by this antibody. Serum MG level was low in healthy subjects and in benign diseases (0.8 +/- 0.7 U/ml; mean +/- SD and 1.1 +/- 2.3 U/ml, respectively). Thus, 3 U/ml was used as the cut-off value. The mean of serum MG levels and positive rates in malignant diseases were significantly high; 4.4 U/ml and 32.3% in lung cancer, 20.1 U/ml and 77.5% in pancreas cancer 11.6 U/ml and 64.3% in gastric cancer, 12.9 U/ml and 57.1% in hepatoma, 12.3 U/ml and 77.8 in colon cancer. Other malignancies such as ovarial and uterus cancer showed also high levels. Elevated values in these malignancies were observed frequently in patients with metastasis. On the other hand, the false positive cases were found in 10% of benign diseases. Determination of MG seems to be useful for the detection of several kinds of malignancies, but it is not adequately sensitive as a screening method for early cancer detection.
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PMID:Clinical significance of mucin-like high molecular weight glycoprotein originated from lung cancer as tumor marker. 274 68

Mucin from xenografts of LS174T human colon cancer cells was treated with anhydrous HF for 1 h at 0 degree C to give a product (HFA) with over 80% of the glucosamine and hexose removed, but retaining some galactosamine, and for 3 h at room temperature to give a product (HFB) devoid of carbohydrate. Rabbit antibodies against HFA bound to HFA much more than to HFB, and bound to native mucin to an intermediate extent. Antibodies to HFB bound to HFB more than to HFA, and did not bind to native mucin. Both HFA and native mucin bound a number of lectins, but HFB did not. By SDS/polyacrylamide-gel electrophoresis and size-exclusion h.p.l.c., native mucin and HFA are of apparent molecular mass greater than 400 kDa, whereas HFB is heterogeneous and of low molecular mass. On Western blots, antibody to HFA detected both high-molecular-mass mucin and a 90 kDa protein in homogenates of LS174T cells. Antibody to HFB detected a major 70 kDa band as well as higher-molecular-mass species. In tissue sections of normal colon and colon cancers, antibody to HFA showed both cytoplasmic and extracellular staining, whereas antibody to HFB generally stained only cytoplasmic antigens. These results indicate that anti-HFB antibody is specific for apo-mucin, whereas anti-HFA antibody is specific for GalNAc-apo-mucin.
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PMID:Deglycosylation of mucin from LS174T colon cancer cells by hydrogen fluoride treatment. 277 37

The carcinoembryonic antigen (CEA) in the cyst fluid of ovarian mucinous and serous tumors was investigated. The molecular weight and antigenicity of the CEA from both ovarian tumors were very similar to those of colon cancer CEA as determined by SDS electrophoresis and double immunodiffusion on agar plates. In the cyst fluid of ovarian mucinous tumors, the amount of CEA was generally high and CEA of molecular weight (MW) 200,000 was increased. In contrast, in the cyst fluid of ovarian serous tumors, the CEA amount was low and CEA variants of MW 370,000 and 180,000 were present in addition to the main CEA of MW 200,000. Immunohistochemically, CEA was stained mainly in the intestinal type epithelium of ovarian mucinous tumors, and the CEA revealed a tendency to be stained more frequently and strongly with increasing degree of tumor malignancy. Thus, ovarian mucinous tumors (especially the intestinal type epithelium) produced large amounts of CEA which closely resembled colon cancer CEA, whereas ovarian serous tumors produced small amounts of CEA, including some CEA variants. In the study of ovarian epithelial tumors, CEA may be useful as a marker for the malignant transformation of ovarian mucinous tumors.
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PMID:Biochemical and immunohistochemical studies on carcinoembryonic antigen of ovarian mucinous and serous tumors. 351 90


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