Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0027651 (tumor)
 685,946 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Combinations of carcinoembryonic antigen (CEA), gamma glutamyl transpeptidase (GGT), pregnancy-associated macroglobulin (PAM) and placenta-like alkaline phosphatase (PLAP) were studied in groups of patients with ovarian and cervical cancer. In ovarian cancer, only CEA and PLAP levels appeared to reflect tumor burden and were complementary in detecting active disease. In cervical cancer, CEA and GGT reflected tumor burden, while PLAP showed just the reverse--the highest degree of positivity being present in minimal disease. PLAP positivity was even more pronounced in patients with cervical dysplasia and carcinoma in situ while CEA and GGT were negative. The data indicate that the use of marker combinations can improve our capacity to detect minimal disease and provide information regarding tumor biology that may not be available by studying individual markers or by other means. It remains to be determined whether the use of tumor markers can influence existing therapy sufficiently to alter the outcome in cancers which are notoriously difficult to treat.
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PMID:Carcinoembryonic antigen (CEA) and other tumor markers in ovarian and cervical cancer. 3 May 36

Rabbits were immunized with extracts of primary or grafted intestinal adeno-carcinomas induced by carcinogenic drugs in inbred rats. After absorption with normal tissue extracts, the antisera were able to recognize three tumor-associated antigens. Two of them were glycoproteins, present in cancer cells but also, in trace amounts, in mucous cells of the normal digestive tract. The third antigen is not detectable in the normal digestive system, but present in normal spleen; on im-unofluorescence, it is not located in the cancer cells, but in polymorphonuclear cells infiltrating the tumor. None of the three antigens cross-reacts with human carcinoembryonic antigen, or human or rat alphafetoprotein. On the other hand, one of the glycoprotein antigens is immunologically related to the human blood group A substance.
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PMID:Antigens associated with chemically induced intestinal carcinomas of rats. 4 40

The carbohydrate moiety of carcinoembryonic antigen could be sequentially degraded by repeated cycles of periodate oxidation, reduction, and mild acid hydrolysis (Smith degradation). After three complete degradations, all fucose and sialic acid, 80% of the galactose, 65% of the mannose, and about 40% of the N-acetylglucosamine were eliminated without impairing the ability of degraded carcinoembryonic antigen to react with specific antisera against the antigen. Inhibition studies in a carcinoembryonic antigen/rabbit anti-carcinoembryonic antigen precipitating system with oligosaccharides covering previously known internal structures of glycoproteins and presumably corresponding to the internal carbohydrate region of the antigen, demonstrated that none of the compounds tested was inhibitory. Nor could any inhibitory effect on the binding of carcinoembryonic antigen to antibody against the antigen in a radioimmunoassay system be domonstrated for the carbohydrate moiety prepared by hydrazinolysis or the glyco peptide fraction isolated after papain degradation of the antigen. However, if carcinoembryonic antigen is completely reduced and alkylated, with three intrachain disulfide bonds cleaved per 10-5 g, the immunological activity is reduced to 3-5% of untreated antigen. Furthermore, treatment of the antigen with 0.5 NaOH at 20 degrees for 2 hr completely abolished its ability to react with antiserum, whereas its ability to precipitate with a series of lectins was unchanged. No release of low-molecular-weight carbohydrate orchange in sugar composition of alkali-treated antigen was observed. Our tentative conclusion is that the carbohydrate moiety of carcinoembryonic antigen does not contain the tumor-associated determinant(s).
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PMID:Nature of the tumor-associated determinant(s) of carcinoembryonic antigen. 4 56

Plasma and prostatic fluid from man, dog, and baboon were measured for carcinoembryonic antigen (CEA) by a radioimmunoassay technique. No CEA was detected in plasma, prostatic fluid, or seminal fluid in 12 dogs and three baboons. Elevated CEA (less than 2.5 ng/ml) was found in 13 of 20 human prostatic fluids. It was inferred that there was no immunologic cross-reactivity of CEA among man, dog, and baboon. CEA has been isolated and purified from liver tumors. Biochemical studies reveal that CEA consists of 60 percent carbohydrate and 40 percent protein. It contains the following carbohydrates: fucose, mannose, galactose, sialic acid, N-acetylglucosamine, and a small amount of N-acetylgalactosamine. The following amino acids were found in CEA: lysine, histidine, arginine, aspartic acid, threonine, serine, glutamic acid, proline, glycine, alanine, valine, emthionine, isoleucine, leucine, tyrosine, phenylalanine, and cysteine. The amino acid sequence (first 30 amino acids) of the N-terminal has been determined. The N-terminal amino acid was lysine. Using this study as a model, other tumor antigens from prostatic tumor tissues are being investigated. The acid phosphatase isoenzyme from prostatic tissue was also studied. After a series of purifications, two chromatographic fractions were obtained. Treatment with neuraminidase removed the sialic acid content of the molecule, changed the isoelectric focusing patterns, and abolished the chromatographic heterogeneity. Sedimentation studies indicated a molecular weight of about 100,000. Biochemical studies showed that prostatic acid phosphatase isoenzyme is a glycoprotein which consists of 7 percent carbohydrate and 93 percent protein. It contains fucose, galactose, mannose, sialic acid, N-acetylglucosamine, and the following amino acids: aspartic acid, threonine, serine, glutamic acid, proline, glycine, alanine, valine, methionine, isoleucine, leucine, tyrosine, phenylalanine, lysine, histidine, arginine, tryptophan, and cysteine. An antiserum to this purified prostatic acid phosphatase isoenzyme is being prepared in animals.
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PMID:Tumor antigen and acid phosphatase isoenzyme in prostatic cancer. 4 19

We have measured serial carcinoembryonic antigen (CEA) titers in 122 radiotherapy and 52 chemotherapy patients, randomly selected from the patient population of a Radiotherapeutic and a Cancer Chemotherapy Clinic, and correlated with the clinical and follow-up evaluation. Seventy-eight the radiotherapeutic patients had detectable CEA levels which represents the majority of these proven cancer patients. In this group, 57 patients (73 per cent) showed correlation between the curves of CEA response and clinical evaluation diseases activity in the radiotherapy group. Thirty-one of 52, or 60 per cent of patients of the chemotherapy group showed correlation between CEA and clinical response. These data indicate that CEA serum levels parallel, in general, clinical tumor reponse.
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PMID:Carcinoembryonic antigen (CEA) monitoring in the management of radiotherapeutic and chemotherapeutic patients. 5 93

The carcinoembryonic antigen (CEA) active glycoproteins from perchloric acid extract of liver-metastasized primary colon tumor have been separated by concanavalin A Sepharose (Con A Sepharose) chromatography. The CEA activities separated by Con A Sepharose chromatography were designated as loosely bound and tightly bound which, respectively, eluted on the Con A Sepharose column between 0.12 and 0.15 M and 0.3 M alpha-methylmannose in a linear gradient of alpha-methylmannose. Further purification of these activities by Sephadex G-200, Bio-Gels A-1.5m and P-300 yielded two variants of glycoproteins (B1 and C2) with CEA activity. Both purified preparations of CEA had similar immunochemical properties. Their A280/A260 ratios were 1.30 and 1.56, respectively. The purified loosely bound CEA (B1) had immunological, chromatographic, and electrophoretic properties similar to those of 125I-CEA, whereas the tightly bound CEA (C2) had a lower molecular weight (120,000 to 140,000). Further, specificity to these two CEA's was established by their reactions in immunoelectrophoresis with preparations of specific goat anti-CEA anti-serum obtained from other investigators. The results indicate the practical use of Con A Sepharose affinity chromatography for the separation and characterization of glycoprotein tumor antigens.
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PMID:Demonstration of two molecular variants of carcinoembryonic antigen by concanavalin A sepharose affinity chromatography. 5 2

Two different types of immunological reaction are of assistance in the diagnosis of cancer: The first is detection of a weak immunological response of the patient toward his own tumor cells. Unfortunately the currently available techniques for the demonstration of humoral or cellular immunological reaction against autologous tumor cells are not reproducible enough to be recommended as routine clinical tests. Secondly, it is possible to use antisera, obtained by immunization of animals with human tumor extracts, for the detection of substances released into the blood by the tumor cells. The two major antigens associated with human cancer that can be measured in the blood by very sensitive immunological methods are the alphafetoprotein (AFP) and the carcinoembryonic antigen (CEA). It is very important for the physician to be fully alive to the usefulness and limitations of such tests in order to interpret them correctly. Clinical situations in which the measurement of AFP and CEA can provide useful information are reviewed.
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PMID:[Immunological diagnosis of cancer]. 5 32

Several radiopharmaceuticals have recently been shown to have a considerable affinity for malignant tissue. All the tumor-seeking radiopharmaceuticals in current use are nonspecific and may also be picked up by benign tumors and infectious processes, including abscess and granuloma. The sensitivity of the tumor-imaging procedure depends on the radiopharmaceutical employed, the type of tumor, its size and location, and previous or current treatment. Gallium-67 citrate (67Ga), the most widely used tumor-seeking radiopharmaceutical, seems to have its greatest value in detecting bronchogenic carcinomas irrespective of cell type. The sensitivity for lung cancer in 489 studies was 93 per cent. Gallium-67 is also of great value in the staging of Hodgkin's disease, in which its sensitivity is 87 per cent. Non-Hdgkin's lymphomas are detected with only slightly lower sensitivity. There is, in fact, evidence that 67Ga is at least complemenatry, if not more sensitive than lymphangiography, in the staging of lymphoma. However, adenocarcinomas originating in the gastrointestinal tract are detected by 67Ga with a sensitivity of only about 40 per cent, whereas various chelates of bleomycin (including 111In-Bleo, 99mTc-Bleo and 57Co-Bleo) detect adenocarcinoma of the gastrointestinal tract with considerably higher sensitivity. In the few studies available comparing bleomycin chelates, 57Co-Bleo and 99mTc-Bleo appear to be more sensitive in detecting tumor than 111In-Bleo. Other tumor-seeking radiopharmaceuticasl which have been employed with somewhat less success include selenium compounds, labeled pyrimidines, several inorganic cations, lanthanide chelates and labeled proteins. Yet to be evaulated clinically is the efficacy of radiolabeled antibodies which are specific for tumor antigens, such as 131I-anti-CEA (carcinoembryonic antigen).
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PMID:Cancer diagnosis. The role of tumor-imaging radiopharmaceuticals. 5 31

Three species of carcinoembryonic antigen (CEA)-like macromolecules, called the biliary glycoprotein I, II and III (BGP I, II and III) were identified in human bile. BGP I was found in normal gall-bladder bile and hepatic bile but not in bile subjected to inflammation ("white bile"). It was immunologically related to CEA and NGP (the "normal CEA-like glycoprotein". Synonyms: NCA, CCEA-2, etc.). BGP I differed immunologically from CEA in that it lacked the tumor-associated determinants of CEA. It was different from NGP (and CEA) in that it contained BGP I specific determinants as revealed by anti-BGP I antibodies. In bile from gallbladders with obstructed outlet and subjected to cholecystitis, a non-malignant inflammatory process, BGP I was replaced by BGP II and BGP III. Immunologically and physicochemically, BGP II and BGP III appeared to be closely similar to NGP and CEA, respectively.
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PMID:Carcinoembryonic antigen-like substances of human bile. Isolation and partial characterization. 5 33

"Fingerprints" of 0.9% NaCl solution extracts obtained from fetal guts and individual adenocarcinoma of the colon show a randomized pattern of expression of carcinoembryonic antigen (CEA) determinants by CEA radioimmunoassay and isoelectric focusing. All CEA-containing antigens found in a pool of 20 primary adenomas were found at some stage in fetal development. No single CEA-reacting peak was typical of any one period of fetal development. When fetal gut profiles were grouped according to trimester in utero, however, an expanded gene pool was found in the second trimester which correlates well with maximum gastrointestinal growth and differentiation. Isoelectric focusing-CEA radioimmunoassay profiles of individual primary adenomas were similar to but never identical with individual fetal gut profiles. "Fingerprints" of metastatic adenomas of entodermal origin showed quantitative and qualitative increases in molecules with CEA determinants unlike these latter categories. Such data suggest that both integrator and controller gene activities may be lost in metastatic disease. Rather than "phase-specific gene sets" on different chromosomes being activated by various oncogenic modalities, it is more probable that individual chromosomes are involved in oncogenesis. While more data are needed to confirm this idea, it is safe to say that the expression of molecules with CEA determinants need not be caused by either derepressive or reexpressive gene activation. These data point to the individuality of gene expression of molecules with CEA determinants both in fetal development and in early neoplasia. Since CEA-reacting molecules were not found in tumors of ectodermal or mesodermal origin by these methods, such products should be termed carcino-developmental antigens of entodermal or colonic origin.
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PMID:Gene activation of molecules with carcinoembryonic antigen determinants in fetal development and in adenocarcinoma of the colon. 6 12


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