Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0006142 (breast cancer)
 160,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Serum levels of mucin-like carcinoma associated antigen (MCA) were measured in 80 healthy women, 109 patients with breast cancer at presentation and in samples taken from 45 patients with active metastatic breast cancer. The MCA levels in controls had an upper limit of normal of 19.6 U ml-1 in post-menopausal and 16.4 U ml-1 in premenopausal women. The levels at presentation in stages I and II and III were not significantly different from the post-menopausal controls. Longitudinal studies over 5-9 years in 20 patients with stage I and II disease who had remained tumour-free showed a narrow MCA range for each individual patient, but the mean and range of a single measurement in a further 63 of these patients were similar to those of the normal controls. Rising MCA levels occurred in 12/14 patients who developed metastases in 2-8 years after surgery, but local recurrence was not associated with a rise of MCA. Eighty per cent of patients with active metastatic disease had MCA levels greater than 15 U ml-1. MCA levels fell during clinical responses to therapy in metastatic cancer. In the context of follow-up serum MCA levels appear to be a sensitive indicator of metastatic disease; caution is required in the interpretation of isolated measurements.
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PMID:An evaluation of mucin-like carcinoma associated antigen (MCA) in breast cancer. 273 16

The diagnostic value of mucin-like carcinoma-associated antigen (MCA) was compared to that of carcinoembryonic antigen (CEA) and/or CA 15.3 in patients with breast cancer. A total of 368 patients with breast cancer were studied, of whom 253 were free of metastases, whereas 94 had either skeletal or visceral metastases or diffuse metastatic disease. The diagnostic sensitivity of MCA proved to be comparable to that of CA 15.3 and superior to that of CEA in patients with metastatic breast cancer. In contrast, the specificity of MCA was superior to that of CA 15.3. Finally, the diagnostic sensitivity of each of the tested tumour markers, i.e. MCA, CEA and CA 15.3, could be improved by their combined use. We conclude that MCA, either alone or in combination with CA 15.3 and CEA, can improve the monitoring of disease progression in patients with metastatic breast cancer.
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PMID:Diagnostic value of mucin-like carcinoma-associated antigen (MCA) in breast cancer. 275 62

A mucin-like carcinoma associated antigen (MCA), which is recognized by the monoclonal antibody b-12, was found to be elevated in sera of breast cancer patients. Since an immunohistochemical reaction of the monoclonal antibody b-12 was found in epithelial tumors of the ovary we investigated MCA serum levels in 50 patients with ovarian cancer (mean age 59 years, range 31-81 years). In addition, CA 125, CA 19-9 and CEA were determined to compare sensitivity, specificity and the predictive value of the positive test of each parameter used in this study. Blood samples were obtained in 20 patients with progressive disease and in 30 patients during disease free intervals. The MCA serum levels of patients with progressive ovarian cancer (mean +/- SD: 14.7 +/- 14.6 U/ml) did not differ significantly from those of patients in remission (mean +/- SD: 8.2 +/- 5.3 U/ml) or from values of a healthy control group (mean +/- SD: 7.7 +/- 3.8 U/ml, n = 70). Women with progressive disease displayed significantly higher CA 125 (p less than 0.0001) and CEA (p less than 0.0063) serum levels than patients in remission. No significant difference was found for CA 19-9 in patients with ovarian cancer, irrespective of the clinical status. Considering marker surge and tumor progression, the highest sensitivity was found for CA 125 (75%). Sensitivities of the other markers were significantly lower and reached only 25-35%. The predictive value of elevated marker levels as well as specificity of the marker substances were similar. Sensitivity could be extended to 90% if elevation of CA 125, CA 19-9, CEA and MCA were taken into consideration, however specificity was lowered by using this marker combination.
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PMID:A comparative study of mucin-like carcinoma-associated antigen (MCA), CA 125, CA 19-9 and CEA in patients with ovarian cancer. 277 Sep 33

A mucin-like carcinoma-associated antigen (MCA) was recently identified on the surface of established breast cancer cell lines by several monoclonal antibodies. The antibody b-12 was used in a sandwich enzyme immunoassay to measure MCA concentrations in serum samples and other biological fluids. The upper limit for noncancerous women and men was 14 U/ml. MCA levels were independent of estrogen or prolaction secretion, 63% of patients with metastatic breast cancer had elevated serum concentrations of MCA. Elevated MCA levels were also associated with cervical, ovarian or endometrial cancer and carcinoma of the prostate. In metastatic breast cancer, MCA and CA 15.3 showed similar sensitivity. Carcinoembryonic antigen levels did not correlate with MCA. Serum concentrations of MCA increased during pregnancy and remained elevated in nursing mothers. Amniotic fluid was found to be rich in MCA. In contrast, CA 15.3 showed only small changes during pregnancy and was low in amniotic fluid. From binding tests with antibodies used in the MCA and CA 15.3 assays, we conclude that the monoclonal antibodies b-12 as well as 115-D8 and DF3 (CA 15.3 assay) recognize coexisting epitopes on mucin-like antigens, which belong to a polymorphic family of glycoproteins suitable for tumor monitoring. Differences in the behavior of MCA and CA 15.3 may emerge from the complexity and heterogeneity of these mucin-like antigens.
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PMID:MCA, a monoclonal-antibody-defined breast-tumor-associated antigen and its relation to CA 15.3. 281 32

A clinicopathological study was performed on characteristics of mammary mucinous carcinoma and its 3 pathological subgroups: "gelatinous type"--with predominant mucin component, "epithelial type"--with predominant epithelial component, and "combined type"--with a small part of infiltrating ductal carcinoma and mucinous pattern. Among 4,653 primary breast cancers mastectomized at the C.I.H. between 1946 and 1981, 160 or 3.4% was mucinous carcinoma. They were divided into 106 gelatinous type, 20 epithelial type and 34 combined type. 10-year survival rate of mucinous carcinoma (75.3%) was better than whole breast cancer (65.6%). And it was 90.7%, 82.4% and 67.6% in gelatinous, epithelial and combined type, respectively.
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PMID:[A clinicopathological study of 160 cases of mucinous carcinoma of the breast]. 299 63

A family of mucin-type glycoproteins, present in human urine, is coded by a single highly polymorphic gene locus PUM. We have previously shown that these glycoproteins carry epitopes recognized by a series of monoclonal antibodies, many of which were raised to the human milk-fat globule membrane, and which bind to a wide variety of carcinomas and certain normal epithelia. Here we show that in the normal human mammary gland, and in breast cancers the epitopes are present on the same family of molecules as that found in urine. Thus the genetically determined variation at the PUM locus accounts for much of the electrophoretic heterogeneity of the mucin-type glycoproteins present in breast cancer and serum from breast cancer patients that has been reported previously. Knowledge of this normal inherited polymorphism is essential to the interpretation of possible changes to these molecules in malignancy.
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PMID:The breast tumour-associated epithelial mucins and the peanut lectin binding urinary mucins are coded by a single highly polymorphic gene locus 'PUM'. 316 99

MAM-6 is a major epithelial sialomucin which is abundantly present at the apical surface of ductal and alveolar cells of normal tissues and on many different carcinoma cells. MAM-6, as defined by monoclonal antibodies, consists of one or two sialylated glycoproteins with apparent molecular masses of over 400 kDa under reducing as well as nonreducing conditions. The mobility and number of glycoproteins immunoprecipitated vary depending on the cell line of origin. We have employed immunoprecipitation techniques to study the biosynthesis and glycosylation of this mucin. The biosynthesis of MAM-6 was studied in the ZR-75-1 breast cancer cell line. Two glycoproteins with apparent molecular masses of approximately 450 and 650 kDa, representing the mature form, were immunoprecipitated. By pulse-chase analysis, we show that the biosynthesis of the 450-kDa glycoprotein proceeded through intermediates of 220, 200, and 500 kDa which became perceptible after 1, 4, and 30 min, respectively. The biosynthesis of the 650-kDa glycoprotein followed a similar course through 380, 350, and 700-kDa intermediates. The processing of the 220- and 350-kDa precursors involves a rare proteolytic cleavage step which occurs in the endoplasmic reticulum. The late precursors of 500/700 kDa, observed after 30 min chase, and the mature glycoproteins were generated by extensive O-linked glycosylation. The formation of the 500/700-kDa precursors was not affected by monensin. However, the final step of maturation, sialylation of the 500/700-kDa precursors, could be inhibited by monensin. The extensive O-linked glycosylation causes the apparent high molecular weight as observed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Our data on the biosynthesis show that the early MAM-6 precursors contain N-linked glycans, suggesting the presence of N-linked glycans on the mature MAM-6 molecule. Although the copresence of N- and O-linked glycans has been found on many molecules, no N-linked glycans have been reported on mucus glycoproteins previously.
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PMID:Biosynthesis of MAM-6, an epithelial sialomucin. Evidence for involvement of a rare proteolytic cleavage step in the endoplasmic reticulum. 334 46

Plasma carcinoembryonic antigen (CEA) concentrations in 128 patients with breast cancer were measured preoperatively. The data were related to the histologic features of the primary breast carcinoma and to the clinical follow-up data. Analysis of the plasma CEA values did not show a significant correlation with the histologic type and the histologic and nuclear grade of the primary tumor (n = 73) as well as to the presence or absence of keratin, necrosis, desmoplasia, tubule formation and mucin production. Furthermore, the results indicated that high CEA values (more than 10 ng/ml) may be associated with distant metastasis and not with the metastatic spread to lymph nodes. High CEA levels were also associated with reduced survival of the patients. This study confirms our previous report suggesting that high CEA levels are correlated with tumors of endodermal origin, whereas the CEA levels were within the normal range in the tumors of ectodermal origin. In agreement with other studies, however, it was found that the predictive value of plasma CEA concentrations in general is weak, so that the use of CEA measurement for prognosis is of limited value.
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PMID:Prognosis in breast carcinoma utilizing plasma carcinoembryonic antigen and histologic characteristics of the primary tumor. 344 70

Thomsen-Friedenreich (TF) antibodies were prepared from human serum by different enrichment procedures. This resulted in three antibody preparations all of which agglutinated neuraminidase-treated erythrocytes. On the other hand, each of the three antibody populations showed a distinct specificity pattern. Anti-TF1 antibodies could be inhibited in the hemagglutination inhibition assay by asialofetuin, asialotransferrin, asialoglycophorin and asialomucin. The sialylated form of these glycoproteins showed no inhibition. No significant inhibition could be achieved with several mono- or disaccharides. This suggests that anti-TF1 recognizes common structures on glycoproteins normally hidden by sialic acid. Anti-TF2 antibodies showed specificity for asialofetuin, bovine submaxillary mucin, asialomucin, asialoglycophorin, the disaccharide gal-beta (1-3)N-acetyl-galactosamine (galNAc) and nitrophenyl-beta-galactoside. Because asialotransferrin or unbound lactosamine were not inhibitory, we suppose that the residual common structure of the inhibitors is (gal)-galNAc-O-Ser/Thr, which is present in high amounts in submaxillary mucin. Anti-TF3 antibodies were inhibited by asialoglycophorin but not by asialomucin or asialofetuin. Strong saccharide inhibitors were gal-beta (1-3)galNAc, nitrophenyl-beta-galactoside, as well as galactose. Therefore, both of the antibody preparations, anti-TF2 and anti-TF3, could be inhibited by gal-beta-(1-3)galNAc, but showed preference to one or the other sugar component of the disaccharide resulting in a differential recognition of glycoconjugate inhibitors. Anti-TF2 and anti-TF3 seem to recognize the carbohydrates in the context of a protein backbone, because gal-beta-(1-3)galNAc in connection with a ceramide backbone (GM1) was not inhibitory. When tested on three human breast cancer cell lines, only anti-TF2 recognized epitopes exposed on the cell surface. We, therefore, conclude that human serum contains at least three subpopulations of TF antibodies with distinct specificities. Only anti-TF2 can detect cryptic erythrocyte epitopes which are also exposed on human breast cancer cell lines.
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PMID:Characterization of Thomsen-Friedenreich antibody subpopulations from normal human serum. 344 72

A quantitative immunoassay procedure has been constructed to evaluate levels of ductal carcinoma antigen recognized by murine McAb F36/22. Using this method, 3% of 64 apparently healthy individuals and 13% of 40 patients with benign breast disease expressed serum antigen levels above 70 units/ml. Greater than 50% of 116 patients with clinical evidence of breast cancer demonstrated circulating ductal carcinoma antigen levels above 70 units/ml. Patients with ductal carcinomas of other sites, including prostate and gastrointestinal tumors, also demonstrated elevated levels of antigen (11 and 27%, respectively). The incidence of elevated serum ductal carcinoma antigen levels correlated significantly with the incidence of intratumoral antigen expression. Lectin binding, molecular weight, and density measurements indicated that circulating antigen occurs as a high-molecular-weight glycoprotein with mucin-like characteristics.
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PMID:Expression of ductal carcinoma antigen in breast cancer sera as defined using monoclonal antibody F36/22. 608 42


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