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)

Slides from ten cases of infiltrating lobular and ten of in situ lobular breast cancer were studied with mucicarmine stain to determine the incidence of intracellular mucin in such cases. Nine of the ten infiltrating carcinomas and six of the ten in situ tumors contained such cells. None of the cases contained infiltrating duct or "colloid" carcinoma and none had in situ carcinoma of major ducts.
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PMID:Intracellular mucin production by lobular breast carcinoma cells. 99 72

In order to develop reagents that can detect the exposed core carbohydrate antigens of mucins, we have prepared monoclonal antibodies against partially deglycosylated LS174T human colon cancer mucin. The three monoclonal antibodies, 10F4, 15D3a, and 91S8, stained cancers of the colon, pancreas, stomach, breast, prostate, and lung to a greater extent than corresponding normal tissues. There was no staining of normal pancreas or breast, suggesting that these antibodies may be particularly useful for detecting cancers in these two organs. In homogenates of cultured cancer cells, antigen was detectable in three colon cancer cell lines, but not in a variety of other epithelial cancers. The epitope specificity of all three monoclonal antibodies appears to be for Tn antigen, i.e. GalNAc-alpha-Ser/Thr, based on their recognition of alpha-linked GalNAc, but not T antigen, sialyl Tn, or a range of other structures. However, the three anti-Tn antibodies differed in tissue staining specificity and in relative binding to different mucins. These monoclonal antibodies, prepared against deglycosylated colon cancer mucin, appear to be useful reagents for the immunohistochemical detection of epithelial cancers, especially pancreatic cancer and breast cancer.
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PMID:Monoclonal antibodies against partially deglycosylated colon cancer mucin that recognize Tn antigen. 128 Oct 60

A panel of three monoclonal antibodies (MoAbs) was tested on 29 benign and 53 malignant effusions with the aim of investigating its usefulness for the discrimination between benign and malignant lesions. The panel consisted of MoAbs directed against epithelial membrane antigen (EMA); MCA-b-12, reacting with a 350 kD glycoprotein with mucin-like characteristics present on human breast cancer cells and various other normal and neoplastic tissues, and Ber-EP4, directed against a 34 and 39 kD glycopeptide on human epithelial cells but not on mesothelium. Fifty-two (98%) of the malignant effusions reacted with EMA, 49 (92%) with MCA-b-12 and 44 (83%) with Ber-EP4. Fourteen per cent of benign effusions reacted with EMA, 17% with MCA-b-12 and 7% with Ber-EP4. All seven effusions obtained from patients with a malignant mesothelioma reacted with EMA, six of the seven cases staining intensively. None of the seven stained with Ber-EP4. MCA-b-12 did not react with the cells in one case of malignant mesothelioma. The results suggest that the combination of EMA and Ber-EP4 may be used to discriminate between benign and malignant cells and possibly also between adenocarcinoma and malignant mesothelioma. MCA-b-12 followed in general the reaction pattern of EMA, although often with a less intense staining reaction, making this antibody unsuitable for inclusion in the panel.
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PMID:Identification of malignant cells in serous effusions using a panel of monoclonal antibodies Ber-EP4, MCA-b-12 and EMA. 128 55

The identification of tumor markers in patients who had undergone operation for breast cancer provides important information in the follow-up in addition to evaluation by clinical and visual methods. The aim of our study was to determine the clinical prospective value of CA 15-3, mucin-like carcinoma-associated antigen and carcinoembryonic antigen in preoperative measurement of serum samples in patients with primary breast cancer, and to determine CA 15-3 and steroid receptors in the cytosol of the tumor. The results show that the most exact correlation occurred between serum CA 15-3 and the different stages of the tumor. However, there is no conclusive evidence for the prognosis and the course of the disease from preoperative findings of tumor markers in serum samples or in the cytosol of the tumor in patients with breast cancer.
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PMID:The significance of determining CA 15-3 in the cytosol of breast cancer. 132 52

Biologic properties of breast cancer in men that might reflect alterations in pathogenesis from the disease in women were examined. We studied 22 tumors from males, 18 invasive carcinomas, three of which were papillary, and three in situ tumors of which one was papillary, and one papilloma. Our data support the previously reported high incidence of papillary carcinoma in men. Estrogen receptor status and the expression of cancer-associated antigens recognized by antibodies DF3, B73.2, SP-1, and c-erbB-2 were compared to matched tumors from females. Immunocytochemistry was performed on formalin-fixed, paraffin-embedded sections using standard avidin-biotin techniques; anti-PSA was used to exclude the possibility of metatastic prostate cancer, and 12 cases of gynecomastia were included as nonmalignant controls. The incidence of estrogen receptor positivity was higher in tumors from males (73%) than from females (54%), as has been reported previously. The range of expression of all breast cancer antigens tested in male tumors was similar to that observed in females, but some interesting differences were noted. With the exception of the anti-mucin DF3, all the antibodies reacted only with neoplastic tissues. Expression of the oncoprotein c-erbB-2 was lower (17%) in males than in females (33%), despite the preponderance in men of the large-cell type carcinomas that have been associated with c-erbB-2 expression. Unexpectedly, the pregnancy-associated hormone detected by SP-1 was expressed in 33% of tumors from males and, in contrast to females, was found in less differentiated tumors.
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PMID:Immunocytochemical characterization of male breast cancer. 136 97

Second generation antibodies to mammary mucins were produced by immunizing mice with a peptide with a sequence deduced from that of the MUC1 complementary DNA sequence (PAHGVTSAPDTRPAPGSTAP). Four monoclonal antibodies (BCP7-10) were produced which gave different reactions. BCP8 was similar in tissue reactivity (by immunoperoxidase staining) to anti-breast cancer or anti-human milk fat globule membranes (HMFG) antibodies and reacted strongly with most breast cancers and a proportion of other adenocarcinomas, whether formalin fixed or fresh, and reacted less strongly with some normal tissues. The three other antibodies (BCP7, BCP9, BCP10) reacted only with fresh tissues or a single cell line (LS174T of colon cancer origin) and gave variable weak reactions. Like many anti-mucin antibodies BCP8 reacted with HMFG, but more strongly with deglycosylated HMFG; analysis with peptides by enzyme-linked immunosorbent assay indicated reactivity with an epitope contained in the amino acid motif PDTR and using the pepscan method, the minimum epitope was DTR. MAbs BCP7, BCP9, and BCP10 did not react with HMFG; substantial reactions were obtained with deglycosylated HMFG for BCP7 and weaker reactions with BCP9 and BCP10. The finding that BCP7 reacted with breast cancer tissues and deglycosylated HMFG suggested that the epitope recognized by BCP7 was masked in native form and exposed in cancer, indicating that BCP7 could be a useful agent for analyzing differences between normal and cancer mucins. The amino acid epitopes for these antibodies were VTSA (BCP7), GSTAP (BCP9), and RPAP (BCP10). For BCP8, amino acid substitution analysis of SAPDTR indicated that substitutions were poorly tolerated (except Q for T and L/Y for R), contrasting with the substitution analysis of anti-mucin antibody reactions where virtually any amino acid can be substituted for T, indicating that in the native state T (threonine) may be O-glycosylated. The use of synthetic peptides to produce antibodies similar to those produced using crude mucins or tumor extracts represents a major advance in the production of antitumor reagents.
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PMID:Second generation anti-MUC1 peptide monoclonal antibodies. 137 8

The antigen MUSE11 detected by a monoclonal antibody (MAb) is an adenocarcinoma-associated antigen, while CA15-3 is a representative breast cancer-associated antigen detected by MAbs 115D8 and DF3. MAb MUSE11 showed higher binding activity to a synthetic peptide corresponding to the tandem repeat motif of the mucin core protein than that of MAb DF3, although MAb DF3 also had a significant binding activity indicating that MAbs MUSE11 and DF3 could recognize an identical polypeptide core. The reactivity of MAb DF3 to a breast cancer cell line MRK-neu-1 was completely abolished by neuraminidase treatment whereas that of MAb MUSE11 was partly conserved. The simultaneous measurement of the antigens MUSE11 and CA15-3 in sera from 35 cancer patients demonstrated that the incidence of abnormal serum level of CA15-3 was lower than that of antigen MUSE11. These data suggest that at least a part of the structural basis for the difference between the serum levels of antigen MUSE11 and CA15-3 could be carbohydrate side chains including sialic acids.
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PMID:Circulating tumor-associated antigens detected by monoclonal antibodies against the polypeptide core of mucin--comparison of antigen MUSE11 with CA15-3. 137 32

Three sandwich enzyme immunoassays were used to evaluate serum from 93 women: 20 normal, 20 with benign breast disease, 22 with primary and 31 with recurrent breast cancer. Using the three assays, breast cancer mucin enzyme immunoassay (BCM-EIA) carcinoma-associated mucin antigen (CAM) 26 and CAM 29, both singly and in combination, we were unable to establish meaningful cut-offs to differentiate between patients with or without breast cancer. The sensitivity and specificity for BCM-EIA were 90% and 40%, for CAM 26, 89% and 42%, and for CAM 29, 91% and 66%, respectively. Serial serum specimens from 29 patients with recurrent breast cancer were assayed. At recurrence, an increase of 25% or more in marker level over the previous value was found in 24/29 (83%) BCM results, 14/29 (48%) CAM 26 results and 12/29 (41%) CAM 29 results. Prior to clinical detection of recurrence, stepwise increases in BCM and CAM 26 marker levels were seen up to 299 days prior to clinical detection of recurrence. We conclude that these markers may help in the early detection of recurrent breast cancer.
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PMID:Serum markers for primary and recurrent breast cancer: BCM-EIA, CAM 26 and CAM 29. 141 Nov 39

A phase I/II study of intraperitoneal (ip) radioimmunotherapy was conducted in ovarian or breast cancer patients with symptomatic chemotherapy-resistant ascites using a novel anti-mucin monoclonal antibody (mAb) 2G3 labeled with 131I. Tracer doses of 2 mCi [131I]2G3 were given by ip injection to 11 patients, followed by increasing therapeutic doses up to 150 mCi (cumulative) in 9 patients. There was no serious toxicity. Temporary palliation of ascites was observed in 3 of 4 patients who received doses greater than 50 mCi. Total body elimination half-life of the radiolabeled antibody assessed by gamma scintigraphy ranged from 95 to 250 hr, longer than data previously reported in patients without ascites treated with ip administered radiolabeled antibodies. However, uptake of radiolabel by tumor nodules was small and variable (2 x 10(-4) - 2 x 10(-2) % ID/g), and preferential uptake by tumor compared to normal peritoneum was observed in only 2 of 5 patients in whom biopsies were obtained. These results suggest that the observed palliation of ascites is due to prolonged retention of radiolabeled antibody in the peritoneal cavity even in the absence of specific targeting.
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PMID:Intraperitoneal therapy of malignant ascites associated with carcinoma of ovary and breast using radioiodinated monoclonal antibody 2G3. 142 88

An antiserum against the carboxy-terminal seventeen amino acids of the human MUC1 mucin has been raised and extensively characterized. This antiserum, CT1, immunoprecipitates two high molecular weight polymorphic bands (greater than 200 kDa) from a metabolically labelled breast cancer cell line corresponding to the two alleles which have previously been shown to contain different numbers of a twenty amino acid repeat. The CT1 antiserum reacted with tissues from many mammalian species and immunoprecipitated large polymorphic proteins, suggesting that the cytoplasmic portion of the molecule is well conserved. The cell and tissue distribution of Muc-1 mucin in the mouse has been studied by immunocytochemistry. This protein is abundant at the apical surfaces of epithelial tissues and is found expressed in the stomach, kidney, mammary gland, pancreas, salivary gland, lung, trachea, uterus, cervix and vagina.
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PMID:Antibodies to the cytoplasmic domain of the MUC1 mucin show conservation throughout mammals. 159 54


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