Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0007097 (carcinoma)
 152,788 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

An antigen has been isolated from a human signet-ring cell carcinoma serially growing in hamsters, GW-39, by saline, PCA, or phenol extraction, and has been found immunologically identical to a similarly extracted substance in normal human or hamster colon. No other hamster or human tissues or cells were found to contain this antigen, for which reason we have termed it colon-specific antigen, or CSA. CSA has been found to be distinct from the major blood group-specific antigens and from othercolon tumor-associated antigens, such as CEA, CCA-II, and CCA-III. It thus seems that a colon organ-specific antigen can be synthesized by this particular human tumor system. Hamsters immunized with CSA could reject cheek pouch grafts of GW-39 tumors, and tumor rejection by these animals correlated with their anti-CSA antibody titers. Preliminary characterization of CSA suggested that it is a glycoprotein on the cell surface having a molecular size of 30,000 to 50,000 daltons. It is proposed that CSA may play a role in the diagnosis of mucin-producing adenocarcinoma of the colon and in ulcerative colitis.
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PMID:Identification of a colon-specific antigen (CSA) in normal and neoplastic tissues. 4 58

A glycoprotein was isolated from 3M KCl extracts of mammary carcinoma. Addition of an optimal amount of the carcinoma associated glycoprotein induces proliferation of both peripheral blood lymphocytes from normal donors and from patients with mammary carcinoma. RNA-dependent DNA-polymerase levels were found to be markedly increased in glycoprotein-untreated lymphocytes from patients with mammary carcinoma and in glycoprotein-treated lymphocytes of both normal donors and tumor-bearing patients. A factor ("Blocking Factor") was eluted at pH 3.1 from the cell membrane of the mammary carcinoma cells. Addition of an optimal amount of this factor inhibits the glycoprotein induced stimulation of the RNA-dependent DNA-polymerase activity in glycoprotein-treated lymphocytes of both normal donors and tumor-bearing patients.
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PMID:Lymphocyte stimualtion by a mammary carcinoma assoicated glycoprotein. 5 27

The distributions of acid alpha1-glycoprotein, alpha1-fetoprotein, beta-galactosidase and gastrin in gastric carcinoma and gastric ulcer as well as in the neighbourhood of these lesions were studied by means of immunohistochemical methods on imprint preparation. We could not find significant differences between gastric carcinoma and the nonneoplastic lesions, except for the acid alpha1-glycoprotein. The results of this first study indicate that the immunochemical and immunohistological assay of acid alpha1-glycoprotein might be of practical value in diagnosing malignant changes of gastric mucosa.
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PMID:[Immunohistochemical studies on non neoplastic and neoplastic gastric mucosa. Determination of embryonic and specific antigens (author's transl)]. 5 51

A periodic acid-chromic acid-silver methenamine techniqe for visualizing glycoproteins at the electron microscope level was applied to colonic mucosa taken from areas adjacent to and remote from carcinoma. Normal control mucosa was obtained by biopsy of patients with no known gastrointestinal disease. Non-oxidized control sections were run in parallel. Quantitative and qualitative differences in glycoproteins were detected in the mucosa adjacent to carcinoma ('transitional' mucosa, as we call it) as compared with the normal. Furthermore, the vesicles in both the 'intermediate' and absorptive cells elaborate a glycoprotein product and it seems that a direct relationship exists between the increased vesiculation and the markedly developed 'fuzzy coat' in the 'transitional' mucosa. It is suggested that these findings may represent one of the features of an early stage of carcinogenesis. Histochemical and ultrastructural techniques of the kind used in this study may thus be of value in identifying or predicting malignancy in the colonic epithelium.
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PMID:An ultrastructural application of silver methenamine to the study of mucin changes in the colonic mucosa adjacent to and remote from carcinoma. 5 55

Prostatic acid phosphatase from human seminal fluid was purified to homogeneity. The enzyme was characterized as to its purity, molecular weight and amino acid composition. Analytical isoelectric focusing of purified enzyme on polyacrylamide gels resolved the enzyme activity into eleven discrete bands, apparently due to various amounts of sialic acid associated with the glycoprotein. Antisera raised against the purified enzyme produced only one precipitan arc on immunoelectrophoresis. A double antibody radioimmune assay was developed and used to evaluate serum prostatic acid phosphatase in 226 patients without prostatic disease, in 186 patients with benign prostatic hyperplasia and in 93 patients with prostatic carcinoma. No statistical difference was noted in serum prostatic acid phosphatase between patients with benign prostatic hyperplasia and in those without prostatic disease Serum prostatic acid phosphatase was elevated in 94% of the patients with metastatic prostatic carcinoma. Significant elevations were also found in carcinoma patients without metastases.
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PMID:A radioimmune assay for human prostatic acid phosphatase-levels in prostatic disease. 8 87

In an attempt to qualitatively identify the membrane antigen (MA) complex induced by Epstein-Barr virus (EBV) infection of lymphoblastoid cells, superinfected Raji cells were surface labelled with 125I by the lactoperoxidase method and solubilized with Triton X-100, then the 125I-labelled membrane proteins were precipitated by sera containing high antibody titers to MA. Analysis of these immune precipitates on sodium dodecyl sulfate polyacrylamide gel eletrophoresis identified four major EBV-specific membrane proteins with molecular weights (mol. wt) of 280,000, 250,000, 170,000 and 90,000. Sera from patients with Burkitt's lymphoma (BL), nasopharyngeal carcinoma (NPC) and infectious mononucleosis (IM) and from EBV-infected disease-free individuals showed differential patterns of reactivity to these antigens with some sera only recognizing three or less of the antigens. The results from invesigations with these sera also indicated that these major proteins were not related to EBV-induced viral capsid antigens (VCA) or the virus-associated early antigen (EA) complexes as defined by immunofluorescence. Metabolic labelling of EBV-infected Raji cells with [14C]glucosamine, followed by Triton X-100 solubilization and radioimmune precipitation, identified the 280,000, 250,000 and 90,000 components as glycoproteins. The lactoperoxidase-labelled 170,000 molecular weight component was not significantly glycosylated and, therefore, could not be categorized as a glycoprotein on the basis of this study. In addition, a glycoprotein with a mol. wt of 130,000 was identified by this approach which also appeared to be specified by EBV. The results from these investigations, therefore, indicated that the EBV-induced MA complex was composed of four major glycoproteins and one nonglycosylated high mol. wt protein.
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PMID:Epstein-Barr virus-induced membrane antigens: immunochemical characterization of Triton X-100 solubilized viral membrane antigens from EBV-superinfected Raji cells. 8 99

The antigen common for continuous epithelial cell lines and gastric mucosa of humans described earlier was studied. This antigen was revealed in one more cell line, namely in that prepared from human mammary carcinoma MDA-MB-231, noncontaminated with HeLa cells. The antigen described can be detected in the exophytely growing adenocarcinomas of the stomach and in the mucosa of the carcinoma affected stomach at a distance of 10--12 cm from the site of affection; no such antigen was revealed in the endophytely growing carcinoma of the stomach and in mucosa areas surrounding gastric ulcer. The antigen is not a glycoprotein since glycoprotein fractions obtained by means of 1.2 M perchloric acid from the normal stomach mucosa homogenate and the E 16b extract were inactive in immunodiffusion with a sensitive serum. The electrophoretic mobility of the antigen was similar to that of globulin alpha1-beta2. This antigen is of interest since its detection or absence would possibly aid in determination of the initial type of cells from which development of carcinoma occurred, and in more precise recognition of the histological form of carcinoma of the stomach.
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PMID:[Study of the "continuous cell antigen" and the human gastric mucosa]. 10 92

In 41 patients with benignant and malignant diseases of the stomach the appearance of alpha 1-acid glycoprotein (alpha1sGP) in the gastric juice was recorded quantitatively by radial immunodiffusion and compared with normal serum alpha1sGP by immunelectrophoretic analyzation and by immunodiffusion after after Ouchterlony. In 80.0% of the patients with carcinoma, in 11.8% of patients with gastric or duodenal ulcer and in 28.6% of the patients with gastritis the presence of alpha1sGP could be evidenced in the gastric juice. The appearance of this glycoprotein significantly differed in benignant and malignant diseases of the stomach. A polymorphism of the stomach alpha1sGP compared with normal serum alpha1sGP could not be established by the applied methods. Therefore it is unprobable that the gastric alpha1sGP is originated by the malignoma.
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PMID:[Significance of alpha 1-acid glycoprotein for the diagnosis of stomach cancer (author's transl)]. 10 78

Alpha-fetoprotein (AFP) is an alpha1-glycoprotein (M.W. about 65000) appearing in the fetal serum of most mammals including man during the early stages of pregnancy; 4 weeks after birth it disappears altogether or exists at very low concentrations as in the normal adult. AFP is formed in the yolk sac, the fetal liver and the gastro-intestinal tract. One of its physiological functions in fetal life is supposed to be the protection of the fetus from maternal oestrogens (oestrophilic property). The clinical significance of AFP is based on the regular and increasing production in primary liver cell carcinoma, less frequently in teratogenetic tumors where it serves as a control of therapy and course of the disease. Less frequent, minor and temporary increases in the AFP serum level occur in several primary tumors with secondary liver involvement, and in inflammatory gastro-intestinal diseases, e.g. of the liver (hepatitis, cirrhosis). AFP has an increasing importance in gynecology (gestational age, fetal distress syndrom, malformations, hydatidiform mole/chorion carcinoma). The physico-chemical properties of AFP are widely known. Both fetal and tumor AFP appear to be immunologically and biochemically identical, as are that of tissue and biological fluids. The differences observed (variants, microheterogeneity) depend mainly on the different content of sialic acid. An antigenetic relationship exists, between the AFP of most species. The immunodiffusion (Ouchterlony) is the most frequently used but relatively insensitive test (1-5 mug/ml) in finding AFP, whereas the radioimmunoassay is the most sensitive one (up to 0,25 ng/ml) and permits the determination of normal serum levels in adults (below 20 ng/ml). The serum concentration in healthy pregnant women lies up to 500 ng/ml, in patients with hepatitis, liver cirrhosis and other liver diseases mostly under 3 mug/ml, whereas in those with primary liver cell carcinoma levels up to and above 600 mg-percent have been found.
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PMID:[Carcinofetal antigens. I. alpha-fetoprotein (author's transl)]. 16 80

Trypsin-like protease with wide spectrum of enzymatic activities have been isolated from cell-free medium from in vivo cultured human mammary carcinoma cells, and from peripheral blood lymphocytes of patients with mammary carcinoma cultured in presence of cell-membrane carcinoma-associated glycoprotein.
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PMID:Isolation of a protease from the cell-free medium of in vitro cultured mammary carcinoma. 18 24


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