Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0001418 (adenocarcinoma)
 68,496 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The literature on tumor distinctive markers in ovarian cancer has been reviewed. Various immunological and biochemical approaches have been attempted for the diagnosis and management of patients with ovarian cancer. The complex spectrum of antigens that can be detected in human ovarian cancer consists of several tumor-associated antigens, fetal or carcinoembryonic antigens, carcinoplacental markers, and normal tissue antigens. We have described and partially characterized two ovarian tumor-associated antigens designated as OCAA and OCAA-1, which seem to have potential for the immunodiagnosis of ovarian cancer. Several other investigators have carried out similar studies, but in general their serological characterization of these antigens has been limited. The well-defined embryonic proteins that have been examined in the ovarian cancer include carcinoembryonic antigen (CEA), alpha-fetoprotein (alpha-fp), beta-oncofetal antigen (BOFA), Regan and Nagao isoenzymes and human chorionic gonadotropin (HCG). The presence of pregnancy-zone protein (PZP) has also been reported in ovarian cancer. In addition, several normal tissue components include fibrin-fibrinogen degradation products (FDP), alpha 1-globulin, and urokinase have been found associated with ovarian cancer. Both humoral antibodies and cell-mediated immune responses against tumor-associated antigens can be measured in ovarian cancer patients. In addition, serum factors, which block cellular immune reactions, have been identified. However, progress in this area has been hampered by the complexity of the antigens associated with ovarian tumors and the lack of standardized, well-characterized sources of antigens or target cells. Enzymes, especially those involved in glycoprotein biosynthesis, (eg, glycoprotein:glycosyltransferases and glycosidase) have been explored as possible early biochemical indicators of ovarian neoplasia. A serum specific deficiency of alpha-L-fucosidase has been found in patients with ovarian cancers. Of all the glycoprotein:glycosyltransferases studied, galactosyltransferase has been found to be the best enzyme marker for ovarian adenocarcinoma. The determination of serum levels of this enzyme reflected the clinical status of the patient with respect of tumor progression as well as tumor burden. Recently, assay of a phosphodiesterase, which specifically hydrolyzes cytidine 5'-monophospho-N-acetylneuraminic acid, has been found promising in the detection and management of patients with ovarian cancer.
 ...
PMID:Tumor markers for ovarian cancer. 9 53

The process of glycocalyx formation by the trilaminar membrane was investigated at the subcellular level by use of cultivated cancer cells derived from a human stomach adenocarcinoma. Glycocalyx was apparently synthesized on the characteristic trilaminar membrane of Golgi-derived vesicles which gave rise to cytoplasmic vacuoles which, in turn, fused to form an intracytoplasmic cyst. Characteristic microvilli similar to those of intestinal epithelium extended from the membrane lining the intracytoplasmic cyst. These ultrastructural features agree with earlier histochemical findings in suggesting intestinal metaplasia in the origin of the gastric tumor. The morphologic features of the cancer cells clearly indicated that glycoprotein is first synthesized in the Golgi complex and fully formed mucoprotein then emerges as membrane-bound glycocalyx in the vesicles budding from the Golgi stacks. The glycocalyx layer is an integral part of the external leaflet of the characteristic trilaminar membrane. Abundant deposits of glycocalyx in the intracytoplasmic cyst constituted the ultrastructural basis for a distinctive type of signet ring cell that differed from mucous signet ring cells derived from goblet cells.
 ...
PMID:Deviated formation of intestinal glycocalyx in human stomach cancer cells. Another type of signet ring cell. 20 29

A new non-strain-specific ascites subline of the TA3 mammary adenocarcinoma TA3-MM, which arose in vivo from the strain-specific TA3-St subline during an acute respiratory illness of the syngeneic mouse strain A/HeHa hosts, possessed at its surface a glycoprotein not found on the parent TA3-St cell. This glycoprotein, termed TA3-MM epiglycanin, was characterized by a high molecular weight (500,000), by potent inhibition of hemagglutination by the Vicia gramines lectin, and by carbohydrate and amino acid compositions nearly identical to those of the glycoprotein epiglycanin present at the surface of the allotransplantable TA3-Ha ascites cell. By electron microscopic examination, TA3-MM epiglycanin appeared as long extended rods with widths (2.5 nm) and lengths (450--500 nm) similar to those of TA3-Ha epiglycanin. Incubation of each of two sublines of the TA3-MM ascites cell, TA3-MM/1 and TA3-MM/2, with a modified trypsin followed by column chromatography produced approximately 1.0- and 0.2-fold as much epiglycanin-like material, respectively, as was obtained from the TA3--a ascites cell. Continuous growth of the TA3-MM cell in suspension culture resulted in an almost complete disappearance of epiglycanin in a manner demonstrated earlier for the TA3-Ha cell grown under similar conditions. Allotransplantability in the TA3-MM cell may be due, at least in part, to masking a histocompatibility antigens by epiglycanin-like molecules.
 ...
PMID:Isolation and partial characterization of an epiglycanin-like glycoprotein from a new non-strain-specific subline of TA3 murine mammary adenocarcinoma. 28 25

Alterations in cell surface glycoproteins have been implicated in malignancy. We examined surface membrane proteins of a cultured cell line, SKCO-1, which had been derived from a human colonic adenocarcinoma. Cell surface labeling of SKCO-1 cells with galactose oxidase, followed by reduction with sodium borotritide, revealed five major labeled glycoproteins upon sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis. At least three additional labeled glycoproteins could be detected if galactose oxidase treatment was preceded by neuraminidase treatment. Some, but not all, of the glycoproteins could be iodinated by lactoperoxidase. The predominantly labeled glycoprotein (GPI) had a molecular weight of 200,000 and co-migrated in SDS gel with carcinoembryonic antigen (CEA). GPI was not removed from the cell surface by EDTA, hypertonic saline, or sonication but was released from the membrane by detergents. This glycoprotein was subsequently purified using lectin-agarose columns and gel filtration. GPI was judged homogenous by protein- and carbohydrate-stained SDS-polyacrylamide gels and had an amino acid composition similar to that of CEA. The carbohydrate composition of GPI was qualitatively similar to CEA but quantitatively distinct. GPI had a greater proportion of sialic acid and galactosamine and less fucose and glucosamine than CEA. Immunological studies, however, demonstrated identity between GPI and CEA. A study of the turnover rate of GPI showed it to have a half-life of 5 days.
 ...
PMID:Glycoproteins from human colonic adenocarcinoma. Isolation and characterization of cell surface carcinoembryonic antigen from a cultured tumor cell line. 41 28

A human lung tumor-associated antigen was purified to homogeneity from a crude cell-free extract of a human lung adenocarcinoma using standard biochemical procedures. In order to facilitate monitoring the recovery of antigen, trace amounts of previously purified and radioiodinated antigen from another lung tumor were added to the crude extract. The purified antigen was a glycoprotein and contained sialic acid. The antigen had a molecular weight of 76,000 and appeared to contain three subunits, each with a molecular weight of 25,000. The antigen had the following physical properties: Stokes radius, 39.4 A; S20,w, 4.24 S; D20,w, 5.15 x 10(-7) cm2 S-1; and a frictional ratio of 1.40. In addition, the purified, radioiodinated antigen retained complete immune reactivity since it could be quantitatively precipitated with specific immune serum. All of these properties were in close agreement with the properties of another antigen which was purified from a separate human lung tumor. Thus, it appeared from the biochemical and immunochemical criteria presented in this report that a common and identical antigen was isolated from two distinct human lung tumor extracts.
 ...
PMID:Further studies on a human lung tumor-associated antigen. Comparison of antigens from different tumors. 42 69

A partially purified glycoprotein fraction (the G-200 II fraction) obtained from sera of CD-1 mice sensitized with Corynebacterium parvum and treated with endotoxin was designated as tumor necrosis factor (TNF). Human melanoma cells exposed to this factor in vitro had decreased tumorigenicity when injected into nude mice. Human melanoma, embryonal adenocarcinoma of the testis and colon carcinoma heterotransplanted in nude mice exhibited regressions in size following intraperitoneal injections of TNF. The responses were related to dose and duration of exposure.
 ...
PMID:Effects of murine tumor necrosis factor on heterotransplanted human tumors. 43 45

In order to elucidate the mechanism of appearance of abnormal glycoproteins in cancer, activities of glycoprotein glycosyltransferases and glycosidases were determined in the homogenates prepared from normal ovaries and ovarian epithelial adenocarcinoma. Significantly high activities (more than normal mean + 2 S.D.) of these enzymes were found as follows: galactosyltransferase and sialytransferase in 100%; fucosyltransferase 1 (exogenous acceptor, fetuin minus sialic acid and galactose) in 86%; fucosyltransferase 2 (fetuin minus sialic acid, acceptor) in 45%; N-acetylglucosaminyltransferase 1 (ovalbumin acceptor) in 53%; N-acetylglucosaminyltransferase 2 (ribonuclease A as acceptor) in 10% of the samples analyzed. Among the glycosidases, substantially elevated activities above normal controls were found as follows: N-acetyl-beta-D-glucosaminidase in 85%; N-acetyl-beta-D-galactosaminidase in 63%; N-acetyl-beta-D-galactosidase in 50%, and those of alpha-L-fucosidase in 35% of the tumors. In serum of these cancer patients, only levels of galactosyltransferase were consistently elevated compared to controls. Increases in serum levels for other transferases were as follows: fucosyl-1, 10%; fucosyl-2, 60%; sialyl-, 20%; N-acetylglucosaminyl-1, 90%; N-acetylglycosaminyl-2, in 80% of the serum samples from ovarian carcinoma patients. Galactosyltransferase thus appears to be an excellent marker for ovarian carcinoma.
 ...
PMID:Glycosyltransferase and glycosidase activities in ovarian cancer patients. 44 94

Adenocarcinoma of the human colon produce carcinoembryonic antigen (CEA), one of a family of glycoprotein molecules that may be produced by various human cancers and, occasionally, by other abnormal tissues. The physicochemical nature and tissue distribution of CEA have been well established and a variety of radioimmunoassays have been developed for the detection of this material in the circulation of patients with CEA-producing tumours. Although the assay should not be used as a screening test for cancer of the bowel, it may serve as a helpful adjunct in the diagnosis of digestive system tumours in conjunction with other routine investigations. More important is the utilization of the radioimmunoassay for CEA under the following circumstances: 1. Preoperatively as an indicator of tumour dissemination based upon the quantitative concentrations of CEA in the circulation. 2. As an indicator of potentially curative resection manifested by a decrease in circulating concentrations of CEA to below detectable limits. 3. As an early warning of recurrent tumour growth, by detecting the reappearance of CEA in the circulation of a patient rendered CEA-negative after tumour resection, 3 months to 2 years or more before any other presently available technology can detect clinical evidence of recurrence. This last observation is now under investigation for its potential value as an indicator for second-look surgery in patients who have undergone potentially curative surgery for colorectal cancers.
 ...
PMID:Immunology and immunotherapy of colorectal cancer. 64 9

Why do tumors continue to grow in the presence of cell-mediated immune reactions? When inoculated subcutaneously, 10(5) viable spontaneous mammary adenocarcinoma cells produced solid tumors that progressively proliferated and eventually killed all the recipient mice. During the first 10 days after inoculation, the mice developed antibody titers, and the serum acquired toxic activity against the tumor cells. As the tumor gained in size these two activities ceased. Serum of normal mice had no effect on the tumor; the serum of mice immunized with an adenocarcinoma-associated antigen (a glycoprotein) inhibited growth, but that of mice with progressive tumors enhanced proliferation of the tumors.
 ...
PMID:Adenocarcinoma-associated antigen: enhancement of tumor growth with serum from animals bearing adenocarcinoma. 99 4

Cell surface structures of two mouse ascites tumors were studied using lectins. The tumors are sublines of the spontaneous mammary adenocarcinoma TA3 in strain A, differing in two main characteristics. Subline TA3-St grows only in syngeneic mice and has high expression of H-2 antigens. Subline TA3-Ha, in contrast, proliferates in all mouse strains, and has low amounts of exposed H-2 antigens. Concanavalin A (Con A), phytohemagglutinin (PHA) and Helix pomatia anti A hemagglutinin (HP) were used in agglutination tests, in binding experiments with 125I-labelled lectins and also in fluorescence studies with FITC-labelled lectins. Con A and PHA agglutinated the TA3-St cells but not the TA3-Ha cells. However, fluorescein-labelled Con A and PHA were bound to all cells (greater than 90%) of both sublines. Moreover both cell types contained an identical number of Con A receptors. The same result was obtained when the number of PHA receptors on the two sublines was compared. HP agglutinated TA3-Ha cells but not TA3-St cells. However, in this case, the difference in agglutinability between the lines was due to the presence or absence of HP receptors. All TA3-Ha cells contained large numbers of HP receptors. In contrast the majority (greater than 90%) of the TA3-St cells lacked HP receptors. (See article.) Trypsin released the HP receptors from TA3-Ha cells, at the same time making these cells agglutinable by both Con A and PHA. We conclude that the Ta3-Ha cells have a trypsin sensitive surface glycoprotein (or glycoproteins) detectable by HP, which is absent on most TA3-St cells. It is possible that this glycoprotein interferes with the agglutinability of TA3-Ha cells by Con A and PHA; whether it is also responsible for the low expression of H-2 alloantigen on this cell remains to be seen.
 ...
PMID:Concanavalin A and other lectins in the study of tumor cell surface organization. 109 13


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