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)

Flow cytometric DNA content analysis is a rapid, quantitative method of determining the DNA ploidy status and proliferative index of a given tumor. Abnormal DNA content, or aneuploidy, has been recognized as a marker of malignancy and is present in about 70 per cent of solid tumors. In the majority of solid tumors, the consensus is that the presence of an aneuploid tumor predicts a poorer over-all survival rate and a shorter disease-free interval, indicating that patients with diploid tumors have a more favorable prognosis than those with aneuploid tumors. The prognostic implications of an abnormal DNA content, therefore, suggest either a higher risk of relapse, a worsening of survival rate or a risk for progression of disease in stages I and II carcinoma of the breast, carcinoma of the colon and rectum, superficial carcinoma of the bladder and malignant melanoma. Thus, the assessment of cellular DNA content should be regarded as an additional prognostic determinant and should play an ancillary role in the decisions regarding the management of patients with malignant disease. With the introduction of more sophisticated technology, it will be possible to simultaneously assay for DNA ploidy and cell cycle distribution in addition to a series of tumor markers, such as CEA, and various products of oncogenes, thus providing further understanding of the heterogeneity of solid tumor cells.
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PMID:Flow cytometry and prognostic implications in patients with solid tumors. 220 Oct 96

Spleen cells from inbred Biozzi mice, immunized against the human breast cancer cell line T47D, were fused with murine myeloma SP2O cells to generate monoclonal antibodies. One of these, 1BE12, of IgM isotype, reacted with five of six human breast tumor cell lines, while no binding was detectable with normal lymphocytes, RBC, or fibroblasts. The antigen recognized by monoclonal antibody 1BE12 was localized on the surface of T47D and MCF7 cells and was detected in cell-free supernatants of cultures. The antigen was found also on the surface of milk secretory cells. Immunohistochemical staining of frozen and paraffin-embedded sections of human tissues showed apical polarized reactivity in normal breast glands, while in all breast cancers staining was either cytoplasmic or membranous and heterogeneously distributed. Immunostaining was also observed in some other normal epithelia, including salivary gland, gastroduodenal mucosa, exocrine pancreas, and cervix. The antigen was not detectable in secretory endometrium, whereas proliferative endometrium was strongly stained. Colon carcinoma, and cancers of the bladder and endometrium were strongly reactive. No staining was detected in melanoma, lymphoma, mesothelioma, non-small cell lung carcinoma, and thyroid, renal, and ovarian carcinomas. Lectin absorption of MCF7 membrane extracts reduced 1BE12 binding. A large reduction in 1BE12 reactivity was observed after digestion of T47D and MCF7 membrane extracts with proteases. Treatment with sodium periodate resulted in complete loss of antigenicity, while neuraminidase treatment did not affect 1BE12 binding. These findings suggest that the 1BE12 epitope is expressed on the carbohydrate moiety of a glycoprotein and does not contain sialic acid. Immunoblotting of the perchloric acid-soluble fraction of MCF7 membrane extracts after electrophoresis in 1% agarose detected the antigen as a high molecular weight species (Mr greater than 900,000). The antigen was purified by perchloric acid extraction of MCF7 membrane preparations followed by affinity chromatography on 1BE12 antibody coupled to Sepharose-4B and gel exclusion fast protein liquid chromatography. No reactivity of the purified material was found with monoclonal antibodies directed against human milk fat globule membrane-associated mucins HMFG1 and DF3.
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PMID:Characterization and distribution in human tissues of a glycoproteic antigen defined by monoclonal antibody 1BE12 raised against the human breast cancer cell line T47D. 222 61

Plasmapheresis is being used with considerable frequency in the management of malignant and non-malignant disorders. More recently, staphylococcal Protein A immunoadsorption has been employed in similar clinical situations. In patients with malignancy, plasmapheresis has been shown to produce alterations in plasma proteins, decrease circulating immune complexes, remove "specific" and "non-specific" blocking factors, change immune reactivity, and affect monocyte function. Partial responses have been reported in a small number of patients with carcinoma of lung, colon, and breast following plasmapheresis. In addition, there are reports of favorable responses in patients with melanoma, head and neck tumors, lymphomas, leukemias, and Kaposi's sarcoma in acquired immune deficiency. All these responses were partial and brief, and the treatment did not alter the course of the disease. Plasmapheresis has been useful in the management of hyperviscosity and occasionally of paraneoplastic syndromes. It may also have a role in the treatment of thrombotic thrombocytopenic purpura associated with mitomycin-C therapy. Protein A immunoadsorption, by which circulating immune complexes are selectively removed, can activate the complement system, increase blastogenic responses, and increase the natural killer cell activity. It has been shown to produce partial responses in breast and colon cancer, as well as Kaposi's sarcoma in acquired immune deficiency. It may have a useful role to play in the management of mitomycin-C-associated thrombotic thrombocytopenic purpura. Both plasmapheresis and Protein A immunoadsorption should be considered investigational interventions at this time. Toxicity of plasmapheresis, though uncommon, can be serious and may rarely be fatal. Toxicity of Protein A immunoadsorption is mild, consisting mainly of influenza-like symptoms and rash.
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PMID:Therapeutic plasmapheresis and protein A immunoadsorption in malignancy: a brief review. 222 1

A new immunohistochemical assay was developed for the detection of human monoclonal antibody (HuMAb) bound to human biopsied tumor tissues. A murine anti-idiotype monoclonal antibody, alpha type, 18C6 (IgGl), was raised against an IgM HuMAb, L612, defining a tumor-associated ganglioside antigen (GM3) and used as a probe in a three step cell-binding assay (HuMAb + anti-id + biotinylated anti-mouse Ig). Anti-id 18C6 has an exclusive binding specificity for HuMAb L612, but does not interfere with the binding of L612 to antigen positive melanoma cell lines or to a purified antigen, GM3. The applicability of 18C6 in the three step cell-binding assay was tested first using a melanoma cell line, UCLASO-M12. L612 bound to M12 cells was specifically detected by 18C6 without any background reactivity in ELISA. When this assay was compared with the standard two-step cell-binding assay (HuMAb + peroxidase-conjugated anti-human IgM) using various cultured tumor cell lines, parallel reactivity was observed. The three-step cell-binding assay was then applied to various fresh-frozen human tumor sections. Positive reactivity was demonstrated on various histologic types of human tumor tissues: primary melanoma (10/10), metastatic melanoma (4/4), nevus (10/10), lung cancer (3/6), breast cancer (2/6), and colon cancer (1/1). Adjacent normal tissues were unstained. Control experiments included the cell-binding assay with L612 alone, 18C6 alone. L612 + unrelated mouse IgG, and unrelated IgM HuMAb (L72) + 18C6; but biotinylated anti-mouse IgG did not react with these control preparations. The results indicate that anti-id 18C6 is a highly specific probe to assess the expression of the ganglioside antigenic epitope recognized by the L612 HuMAb on biopsied human tumor tissues.
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PMID:Murine monoclonal anti-idiotype antibody (alpha) as a probe to detect human monoclonal antibody bound to human tumor tissues. 223 Jan 46

Immunohistochemical techniques were used to determine the distribution and cellular location of the mature and precursor forms of a colonic-type mucin in normal and malignant epithelial tissues. The antisera used in this study were prepared against native human colon cancer mucin (LS), partially deglycosylated mucin (HFA or GalNAc-apomucin), and fully deglycosylated mucin (HFB or apomucin). These antisera reacted with most mucin-producing cells of the normal gastrointestinal tract, salivary ductular cells, bronchial epithelial cells, some bronchial mucous glands, and squamous epithelial cells of the esophagus. Breast, endometrium, ovary, prostate, liver, and thyroid were nonreactive. In most normal organs, HFB reactivity was present in the supranuclear and perinuclear cytoplasm and LS and HFA were located primarily in goblet cell vacuoles, apical cytoplasm, and luminal secretions. These findings are consistent with the expected subcellular locations of apomucin and more "mature" mucins. LS, HFA, and HFB were frequently expressed in adenocarcinomas of the colon, stomach, pancreas, and lung. Lymphoma, sarcoma, and melanoma specimens were nonreactive. Alterations in the expression of these mucin antigens in malignant tissues included loss of subcellular compartmentalization, increased intensity of staining, and disappearance of staining. In addition, de novo expression of HFB was observed in one of five breast carcinomas and three of five ovarian mucinous cystadenocarcinomas. These data demonstrate that LS, HFA, and HFB are useful for studying the organ specificities and biosynthetic pathways of one type of mucin in normal and malignant tissues.
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PMID:Expression of native and deglycosylated colon cancer mucin antigens in normal and malignant epithelial tissues. 223 15

22-Hydroxytingenone was reisolated from a new source, Glyptopetalum sclerocarpum M. Laws and, for the first time, its unambiguous 13C-NMR assignments were accomplished through the use of APT, HETCOR, and selective INEPT spectroscopy. Intense, but nonspecific cytotoxic activity was observed when this substance was evaluated with a battery of cell lines comprised of the P-388 lymphocytic leukemia, KB carcinoma of the nasopharynx, and a number of human cancer cell types, i.e. HT-1080 fibrosarcoma, LU-1 lung cancer, COL-2 colon cancer, MEL-2 melanoma, and BC-1 breast cancer.
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PMID:Spectral assignment and cytotoxicity of 22-hydroxytingenone from Glyptopetalum sclerocarpum. 223 93

The actin cytoskeleton is important for cell structure and motility. A disordered actin architecture has been correlated with a high metastatic potential in melanoma, fibrosarcoma, and colon cancer models. Thyrotropin is known to induce growth and differentiation in cultured thyroid cells, whereas the carcinogenic phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA) causes dedifferentiation and malignant transformation in many cell lines. We therefore assessed the effect of thyrotropin and TPA on the actin architecture of FTC-133 human follicular thyroid cancer cells in continuous culture. Staining of filamentous actin with rhodamine phalloidin showed that 1 mU/ml or 30 mU/ml thyrotropin-induced actin polymerization was detectable at 1 hour but more notable at 24 hours. Similarly TPA (0.008 to 10 mumol/L) caused rapid actin fiber disruption and redistribution to the cell periphery. Secondary antibody staining for alpha-actinin, a protein that binds and crosslinks actin, was more prominent after treatment with thyrotropin but decreased after TPA. These findings indicate that the actin cytoskeleton has a dynamic response to trophic factors. Thyrotropin promoted actin polymerization, but TPA caused depolymerization. These effects may correlate with cellular alpha-actinin levels. Actin architecture may therefore reflect the state of differentiation of thyroid tumor cells.
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PMID:Actin architecture of cultured human thyroid cancer cells: predictor of differentiation? 224 45

The aporphine alkaloids, dicentrine, glaucine, corydine, and apomorphine were shown to have inhibitory activity against several mouse tumor cell lines, leukemia P388 and L1210, melanoma B16, bladder cancer MBC2, and colon cancer Colon 26 in culture. These aporphine alkaloids also inhibited the mitogen-induced lymphocyte proliferation as well as the growth of IL-2 dependent CTLL2 line in a dose-dependent way. Of the four alkaloids apomorphine proved to be most potent in the inhibitory action. Apomorphine treatment resulted in some prolongation of survival time of the mice inoculated i.p. with P388, although its activity was not enough to meet the standard criterion for antitumor activity.
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PMID:Suppression of tumor cell growth and mitogen response by aporphine alkaloids, dicentrine, glaucine, corydine, and apomorphine. 229 Jan 26

Because both Rhodamine 123 (R123) and hyperthermia have been shown to be cytotoxic, we examined their effect, independently and in combination, on five different human malignant cell lines in vitro and on cultured melanoma cells grown intradermally in nude mice. The cell lines examined include two human melanomas, UCLA-SO-M14 and UCLA-SO-M21, the colon cancer cell line HT29, the human lung cancer cell line P3, and the human breast cancer cell line B231. R123 and hyperthermia, when used in combination, were found to be cytotoxic for these five different human malignant cell lines in vitro. The two agents together appear to enhance the cytotoxic effect of each alone, as documented by synergistic ratios ranging from 2.31 to 45 for the different cell lines. In the "nude" mouse model, animals were treated with a combination of R123 and hyperthermia (43 degrees C for 90 min). A statistically significant (P = 0.04) decrease in tumor growth rate was observed when compared with the rate of tumor growth in untreated animals. The results suggest a potential role for R123 in combination with hyperthermia in the treatment of malignant cells.
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PMID:In vitro and in vivo cytotoxicity of rhodamine 123 combined with hyperthermia. 229 90

Methods of single-tracer whole-body autoradiography (WBAR) have been developed in our laboratory which allow imaging and measurement of the zonal distribution of radioiodinated antibodies and their fragments within GW-39 colon carcinoma xenografts varying in size from large, cystic masses with necrotic cores to micrometastases. The whole-animal distribution of 90Y-labeled anti-carcinoembryonic antigen monoclonal antibody NP-2 was evaluated by WBAR in nude mice bearing s.c. implants of GW-39 colon cancer and revealed antitumor uptake specifically as well as significant accumulation of 90Y in the bones. Dual-tracer qualitative WBAR methods have also been applied in order to examine the biodistribution of labeled immunoglobulins in the GW-39 animal tumor model as a function of the underlying rapid cell proliferation index ([3H]-thymidine assay) in the same tumor. In addition, extension of the WBAR method was made to permit imaging of the biodistribution of 10B compounds in mice bearing Harding-Passey melanoma implants by using a track-etch procedure to produce alpha-particle WBAR. Further applications of single and multiple radionuclide WBAR are offered and discussed as an effective means of assessing the degree of penetration of immunoglobulins in tumors in which vascular patterns, local glucose metabolism, protein synthesis, and rapid cell proliferation indices may be characterized.
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PMID:Use of whole-body autoradiography in cancer targeting with radiolabeled antibodies. 229 39


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