Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0006826 (cancer)
 1,092,456 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

As part of a more extensive study of the immune response in children with neuroblastoma, serum immunoglobulin and alpha-glycoprotein levels were measured in 58 patients. Twenty-nine children were studied at diagnosis, 18 at some time during the first 2 years of treatment, and 11 who were apparently cured after treatment had been completed. No correlation was found between the levels of IgG, IgA, and IgM and the clinical status of the patient. The acute phase reactants (alpha-1-antitrypsin, haptoglobin, C3 component of complement and orosomucoid) varied with the disease status. Twenty-seven of the 29 patients had elevated levels at the time of diagnosis. Alpha-1-antitrypsin and haptoglobin were the two proteins that most accurately reflection the clinical status; C3 component of complement was not infrequently normal when the disease was active; and orosomucoid was sometimes raised in patients apparently in remission. Serial measurement of alpha-1-antitrypsin and haptoglobin could provide a useful means of detecting early relapse in patients responding to treatment.
Cancer 1977 Oct
PMID:The prognostic value of acute phase reactants in patients with neuroblastoma. 7 Nov 94

Cell membranes of Moloney lymphoma cells (YAC, of strain A origin) were solubilized by NP40. The antigenicity of the solubilized protein fraction was assayed by inhibition of the corresponding cytotoxic reaction against YAC target cells. The Moloney leukemia virus (MLV)-determined cell surface antigen (MCSA) was detected with mouse antisera, produced by the repeated inoculation of heavily irradiated YAC cells into syngeneic mice. Virion proteins gp71, p30, p15, p12 and p10 were identified with goat or rabbit antisera against purified Rauscher and Friend leukemia virus proteins. MCSA was found to bind to Con-A--Sepharose and was eluted by mannoside together with H-2A AND GP71. In contrast, p30, p12, p10 and part of p15 and p15(E), were not retained on the column and could be separated from MCSA. Passage of the glycoprotein fraction through Sephadex G-200 led to the separation of MCSA activity from gp71 and H-2A. MCSA eluted between the immunoglobulin (IgG) and the bovine serum albumin (BSA) size markers. MCSA could be also separated from the known viral proteins and from H-2 by velocity centrifugation in sucrose gradients. It sedimented with approximately 6.6 S ahead of gp71 (4.4 S) and H-2 (3.2 S). It is suggested that MCSA may be a glycoprotein with an approximate molecular weight of 110,000 and distinct from the known viral proteins gp71, p30, p15(E), p12, p10 and from H-2.
Int J Cancer 1977 Jul 15
PMID:Separation of the Moloney leukemia virus-determined cell surface antigen (MCSA) from known virion proteins associated with the cell membrane. 7 Dec 77

A profile of acute phase reactant proteins has been studied in patients with cancer of the prostate as an aid to diagnostic staging and therapy control. A linear discriminant function analysis incorporating serum acid phosphatase, prealbumin, alpha1 antitrypsin, alpha1 acid glycoprotein and haptoglobin allows the correct identification of metastatic disease in 88.6% of patients. The profile may also serve to augment other parameters in the assessment of the physiological effect of oestrogen treatment and show whether the prescribed medication is being taken.
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PMID:Acute phase reactant proteins in prostatic cancer. 7 95

A glycoprotein has been isolated from the colonic lavages of healthy individuals that is immunologically equivalent to carcinoembryonic antigen purified from tumor tissue. The NH2-terminal sequence of the glycoprotein from normal colon lavages is Lys-Leu-Thr-lle-Glu-Ser-Thr-Pro-Phe-(Asn)-Val-Ala-Glu-Gly-Lys-Glu-Val-(Leu,lle)-(Leu,lle)-(Leu,lle)-Val-(His,Arg?)-?-(Leu,lle). This is homologous to the NH2-terminal sequence of 23 of the first 24 amino acids of carcinoembryonic antigen isolated from tumor tissue.
Cancer Res 1978 Mar
PMID:Amino-terminal sequence of a carcinoembryonic antigen-like glycoprotein isolated from the colonic lavages of healthy individuals. 7 56

A radioimmunoassay for a plancental glycoprotein, beta1SP1, capable of detecting 2 microgram/l of the glycoprotein in serum was used to measure concentrations of beta1,SP1 in patients with choriocarcinoma, teratoma, colonic cancer, breast cancer, and ovarian cancer. 12 out of 94 (13%) healthy men and health non-pregnant women had detectable serum-beta1SP1 concentrations. Concentrations up to 50 000 microgram/l were found in the sera of patients with hydatidiform mole, invasive mole, choriocarcinoma, and malignant teratoma. beta1-glycoprotein concentrations were generally much lower than corresponding concentrations of chorionic gonadotrophin which is the most reliable marker for trophoblastic tumours. In a few cases, however, beta1-glycoprotein measurements may be useful in the detection of minimal residual tumour. The slightly raised values found in some patients with carcinoma of the colon, breast, or ovary seem unlikely to be useful for diagnostic purposes of for monitoring the course of these cancers.
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PMID:Serum-SP1-pregnancy-specific-beta-glycoprotein in choriocarcinoma and other neoplastic disease. 7 23

Fucosyltransferase levels in 6 established strains of spontaneously metastasizing rat mammary tumors (STMT-058, MT-449, DMBA-4, SMT-077, TMT-081, and SMT-2A) were compared with 4 nonmetastasizing strains (MT-W9B, MT-W9A, MT-100, and MT-66) as controls. Two acceptors were prepared from fetuin for the assay, one by acid hydrolysis of N-acetylneuraminic acid and the other by the stepwise removal of N-acetylneuraminic acid and penultimate galactose by Smith degradation. The enzyme that transfers fucose to the first acceptor was designated fucosyltransferase A, whereas the one that uses the second acceptor was designated fucosyltransferase B. Both types of fucosyltransferases were found in this rat mammary tumor system. Whereas the levels of fucosyltransferase A in the 2 tumor groups were comparable, those of fucosyltransferase B were sixfold to sevenfold higher in the metastasizing tumors. This difference in the level of fucosyltransferase B was not caused either by differential hydrolysis of GDP-fucose by pyrophosphatase in the 2 groups or by hydrolysis of the product by fucosidases. Presence of any other inhibitor(s) or activator(s) of fucosyltransferase was excluded by mixing experiments. Optimal conditions for the assay of this enzyme were determined in a representative strain from each group. Under all circumstances, the activity of fucosyltransferase B was higher in the metastasizing tumors. The enzyme was inhibited by nucleoside diphosphates and triphosphates, and guanosine nucleotides were the most efficient inhibitors. Subcellular distributions of the two fucosyltransferases were similar, 35-50% of the enzyme activity being present in the crude microsomes. When plasma membrane factions were prepared from the microsomes, the major part (50-70%) of the enzyme was associated with the light and heavy plasma membrane fractions. Increased activity of fucosyltransferase B in the group of metastasizing tumors may have reflected faster synthesis and shedding of fucose-containing glycoprotein antigens. Similar molecules possibly were also synthesized in the nonmetastasizing cells but at a much slower rate, because the antigen is not easily lost from the cell surface. Any alteration of the specificity of this focosyltransferase in the metastasizing tumors, in addition, may have caused antigen modulation.
J Natl Cancer Inst 1978 Jul
PMID:Fucosyltransferase activity in metastasizing and nonmetastasizing rat mammary carcinomas. 7 84

Evidence has been reported for at least two common tumor-associated antigens, or antigenic determinants, in human cystadenocarcinomas of the ovary that are apparently absent in tissues of normal reproductive organs. These antigenic determinants are immunologically distinct from carcinoembryonic antigen, alpha-fetoprotein, ferritins and histocompatibility antigens. One of these two ovarian cystadenocarcinoma-associated antigens (OCAA) is not detectable in any ovarian carcinomas except serous or mucinous types, other gynecologic or nongynecologic malignancies thus far tested, while the second antigen is present in about 90% of all gynecologic tumors and occasionally in breast and colon tumors. OCAA has been purified and partially characterized. It is a high molecular weight glycoprotein which carries the unique ovarian tumor-specific antigenic determinant along with some normal cross-reacting determinants. High levels of this glycoprotein antigen have been detected in the sera of ovarian cancer patients with advanced disease by the radioimmunoassay inhibition technique. The serial determination of circulating OCAA appeared to correlate with tumor volume as well as the clinical status of the patients.
Cancer 1978 Sep
PMID:Ovarian tumor antigens. 8 12

Antigen(s) related to the major external glycoprotein (gp52) of mouse mammary tumor virus was detected in the human breast cancer cell line MCF-7. No such antigenic determinants were detectable in normal human mammary epithelial cells.
J Natl Cancer Inst 1978 Nov
PMID:Presence of a mouse mammary tumor virus-related antigen in human breast carcinoma cells and its absence from normal mammary epithelial cells. 8 81

Depression of lymphocyte transformation and an increase in insulin resistance are common to pregnancy, oral contraceptive use, widespread malignancy, infection, and tissue destruction. We suggest that these abnormalities are caused by a rise in the plasma-glycoprotein level which is also common to these clinical states. There is evidence that glycoproteins can inhibit cell division, lymphocyte transformation, and the action of hormones on target cells. Because of the increase in plasma glycoprotein the cells in many organs and their hormone receptors may have a thicker coating of glycoproteins which blunts their response to variuos stimuli.
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PMID:Do plasma glycoproteins induce lymphocyte hyporesponsiveness and insulin resistance? 8 44

alpha2-PAG is a high-molecular, carbohydrate-containing glycoprotein. It occurs in traces in normal human serum. The variations in serum levels of this protein were studied during treatment of 32 gynecological cancer patients in the course of 2 years. The periodic alpha2-PAG determinations were done with an electro-immuno-assay. A correspondence between alpha2-PAG serum levels and the clinical course could be found in 60%. In 5 of 13 patients who did not respond to therapy alpha2-PAG levels rose, additional 4 had unchanged high levels, whereas 13 of 17 patients had significantly decreased levels on successful treatment. The relevance of periodic alpha2-PAG determinations is discussed.
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PMID:[Pregnancy associated alpha2-glycoprotein (alpha2-PAG) in the serum of patients with gynecologic carcinomas]. 8 57


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