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Query: UMLS:C0006142 (breast cancer)
 160,383 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Monoclonal antibodies 323/A3 and Ca1 have been suggested as markers of breast cancer risk in benign breast disease. We have studied the staining profiles in benign biopsies of 323/A3 and Ca1 in 146 patients. We then compared the staining patterns grouped according to whether the patients were at "high or low" risk of breast cancer by conventional epidemiological or radiological criteria. The results show that the staining profiles are similar between risk groups and that on the risk criteria used in this study 323/A3 and Ca1 will not distinguish patients at risk of developing breast cancer.
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PMID:Immunohistochemical staining patterns of benign breast biopsies by 323/A3 and Ca1 monoclonal antibodies related to epidemiological and radiological risk criteria. 137 68

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

It has been predicted that low affinity antibodies (Abs) should penetrate into tumors more readily than high affinity Abs. However, the absolute uptake and residence time of a high affinity Ab may be better. It is, therefore, not clear whether a high affinity Ab would have a therapeutic advantage. This is particularly relevant with 125I radioimmunotherapy, where targeting of every cell is important. This study compared the uptake kinetics and toxicity in multicell spheroids of two murine monoclonal Abs labeled with 125I. 17-1A was produced by immunization with a human colon cancer cell line and has an affinity of 5.15 x 10(7) M-1. 323/A3 was produced by immunization with a human breast cancer cell line and has an affinity of 1.87 x 10(9) M-1. Binding of both Abs to LS174T spheroids was similar at 4 degrees C, but binding of 17-1A was 8-10-fold less than that of 323/A3 at 37 degrees C. Despite this difference, the toxicity of 125I-17-1A in spheroids after 7 days of incubation was similar to that of 125I-323/A3. Autoradiography showed that 17-1A penetrated the spheroids much more deeply and evenly than did 323/A3. It appears that much of the radiation dose to spheroids treated with 125I-323/A3 was wasted because of the uneven Ab distribution. This study demonstrates the potential advantage of using Abs of lower affinity for 125I radioimmunotherapy, because of their more even distribution. It also suggests that a large number of binding sites per cell may be a disadvantage if more 125I is bound than is necessary to kill the cell, because this may slow Ab penetration.
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PMID:Comparisons between two monoclonal antibodies that bind to the same antigen but have differing affinities: uptake kinetics and 125I-antibody therapy efficacy in multicell spheroids. 151 38

The 323/A23 monoclonal antibody (MAb) is expressed with increasing breast atypia, whilst Ca1 has been suggested as a marker of cancer risk in benign breast disease. To establish whether they would be useful as markers of malignancy the staining characteristics in benign tissue components associated with malignant biopsies have been compared with the staining patterns of benign biopsies from patients with no known malignancy. Staining with 323/A3 and Ca1 MAb was carried out on formalin-fixed paraffin-embedded tissue sections using ABC Vectastain Reagents (Vector Laboratories) and diaminobenzidine as the chromogen. All biopsies contained ductolobular tissues. Apocrine metaplasia was present in 35 of 79 malignant biopsies, in 42 of 77 selected and 20 of 50 prospective unselected benign biopsies. The 323/A3 MAb stained strongly the cytoplasm of apocrine metaplasia in breast carcinoma biopsies in 18 of 35 cases, in the selected benign group this was two out of 42 (P less than 0.001) and in the prospective benign group one of 19 (P less than 0.01). No differences in staining were noted for ductolobular tissue. The Ca1 MAb showed strong apical staining in ductolobular tissue in 66 of 79 invasive carcinoma biopsies, in 20 of 50 prospective benign biopsies and 53 of 77 selected biopsies. The prospective and selected benign group staining was significantly different from that of the invasive carcinomas (P less than 0.005 and less than 0.05 respectively). These data suggest that 323/A3 staining of apocrine metaplasia and Ca1 staining of ductolobular tissue is affected by a paracrine function of breast cancer.
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PMID:Monoclonal antibodies 323/A3 and Ca1 identify a paracrine function of breast carcinoma on adjacent benign histological components. 169 92

The monoclonal antibody 323/A3 has been suggested as a marker of cancer risk in benign breast disease. Patients who have had both a benign biopsy and a later biopsy for breast carcinoma were studied. The staining patterns in the biopsies were analysed using a semi-quantitative recording system adapted from Mariani-Costantini et al. Immunohistochemical (IHC) staining was carried out on formalin fixed paraffin embedded tissue sections. In apocrine metaplasia the cytoplasm of benign tissue did not stain with 323/A3 whereas in the biopsies with associated breast cancer 5 of 7 biopsies stained, a statistically significant difference. A positive predictive value of 100% was noted for strong cytoplasmic staining to indicate the presence of carcinoma and this phenomenon may be useful as a means of demonstrating patients who have malignant breast disease in which a biopsy has inadequately sampled the breast tissue.
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PMID:Monoclonal antibody 323/A3: a marker for the presence of breast carcinoma. 202 84

Monoclonal antibody (MAb) MUSE11 detects an adenocarcinoma-associated antigen and is useful for the serodiagnosis of pancreas cancer. We established a sandwich enzyme immunoassay using MAb MUSE11 and MAb DF3 against a breast cancer-associated mucin core protein as a catcher and a tracer, respectively. With this assay system, the binding of the tracer MAb DF3 to an antigen in the human kidney tissue lysate was clearly inhibited by MAb MUSE11. In addition, MAb MUSE11 showed a significant binding activity to the synthetic peptide corresponding to the tandem repeat of a human epithelial mucin core protein. These data suggest that MAb MUSE11 could detect the polypeptide core of a mucin, and may be of use for studying mucin as a gene product.
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PMID:Recognition of the polypeptide core of mucin by monoclonal antibody MUSE11 against an adenocarcinoma-associated antigen. 212 88

We have earlier described a monoclonal antibody (323/A3) against a Mr 43,000 surface glycoprotein of MCF-7 human breast cancer cells which shows considerable specificity for primary and metastatic breast tumors (Cancer Res., 46: 1306-1317, 1986). Here we report the occurrence of the 323/A3 antigen in a large cohort of primary breast tumors (m = 384) and its interrelationship with several clinically important variables. Frozen, stored tumor tissues were examined by a Western blot procedure, and the level of 323/A3 protein in individual tumors was calculated in arbitrary units based on the integrated Mr 43,000 signal in tumors compared with an MCF-7 internal standard. Thirty-six % (139 of 384) of tumors were found to be positive for 323/A3. Higher frequencies of 323/A3 protein were found in tumors larger than 2 cm (P = 0.03), tumors with infiltrated lymph nodes (P = 0.01), and tumors without estrogen receptor (P = 0.006). No significant relationship was found with patient age, menopausal status, or progesterone receptor status. Of the newer clinical determinants proliferative rate (% S phase), DNA ploidy, and the lysosomal protease cathepsin D, but not the HER-2/neu oncogene protein, were significantly correlated with 323/A3. The presence of 323/A3 protein was also related to increased recurrence (P = 0.003) and mortality (P = 0.036) after primary treatment. As an exposed surface antigen, this glycoprotein might be a useful target in radioimaging and immunotherapy of some human breast tumors, especially those having large size, infiltrated lymph nodes, deficient estrogen receptor, high proliferative rate, abnormal DNA content, and high levels of cathepsin D, all of which are ominous indicators of tumor behavior.
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PMID:Association of the 323/A3 surface glycoprotein with tumor characteristics and behavior in human breast cancer. 233 24

The detection of early micrometastasis or disseminated single tumor cells poses a problem for conventional diagnosis procedures. Using a panel of monoclonal antibodies against cytokeratin and the 17-1A epithelial antigen we identified immunocytochemically tumor cells in bone marrow of patients with breast cancer (n = 155) and colorectal cancer (n = 57) at the time of surgery of the primary tumor. Monoclonal antibody CK2, recognizing the human cytokeratin component 18 in simple epithelia, appeared to be the most suitable reagent because of its negative reaction with bone marrow samples of the noncarcinoma patients (n = 75). Its specificity was further demonstrated in a double-marker staining procedure using an anti-leukocyte common antigen monoclonal antibody (T200) as counterstain. A comparative analysis showed that immunocytology was clearly superior to conventional cytology (n = 212) and histology (n = 39). In 9.5-20.5% of patients without distant metastasis, tumor cells could be detected in bone marrow. We found a significant correlation between tumor cells in bone marrow and conventional risk factors, such as distant metastasis or lymph node involvement. In a first approach toward immunotherapy we demonstrated in 3 patients that infused monoclonal antibody 17-1A can label single tumor cells in bone marrow in vivo. We then used this approach to follow up 7 patients undergoing 17-1A therapy in an adjuvant clinical trial.
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PMID:Micrometastatic cancer cells in bone marrow: in vitro detection with anti-cytokeratin and in vivo labeling with anti-17-1A monoclonal antibodies. 244 26

A monoclonal antibody (323/A3) with a high degree of selectivity for binding to breast cancer cells was produced by immunization of mice with MCF-7 human breast cancer cells. The antigen recognized by 323/A3 on MCF-7 appears to be surface localized, and by enzyme-linked immunosorbent assay, the antibody was found to bind strongly with four of six breast cancer cell lines examined while no binding was detectable with nonbreast cancer cell lines. In vivo distribution of the 323/A3 antigen was screened by immunoperoxidase staining of formalin-fixed paraffin sections of normal human tissues and tumors. Among breast tissues, positive staining was detected with 75% (6 of 8) of metastatic lymph nodes, 59% (76 of 128) of primary breast tumors, 20% (13 of 63) of benign breast lesions, and 0% (0 of 10) of normal breast. No immunostaining was detected with a large variety and number of other normal human tissues with the exception of staining observed with epithelium of normal colon. Antigen distribution appears not to be disease specific, since positive staining was also observed with adenocarcinomas other than breast. The antigen recognized by the 323/A3 antibody was identified by Western blot analysis as a Mr 43,000 protein. The glycoprotein nature of the antigen was demonstrated by its binding to concanavalin A, specific elution with sugar, and immunoprecipitation of a Mr 43,000 radiolabeled protein from extracts of MCF-7 cells after pulse labeling with [3H]glucosamine. The 323/A3 antigen appears to be the same Mr 43,000 protein in cell lines as in breast tumors in vivo. Based on a comparison with the molecular weights of other known tumor-associated antigens and with their immunocytochemical tissue distribution, the Mr 43,000 glycoprotein described here represents a tumor-associated antigen previously undescribed in breast cancer or in other tumors. Since the Mr 43,000 glycoprotein is present on the surface of most breast cancer cells and is either absent or expressed at very low levels in most normal tissues including normal breast, the monoclonal antibody described here may have potential applications in diagnosis and management of breast cancer.
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PMID:Monoclonal antibody identification and characterization of a Mr 43,000 membrane glycoprotein associated with human breast cancer. 351 Jul 21

The importance of contrast agents in enhancing diagnoses from magnetic resonance images has been established in numerous cases. However, the development of a potent tissue-specific contrast agent, as a sensitive probe for early detection and investigation of the physiological characteristics of a tumor, has not yet been realized in MR imaging (MRI). In nuclear scintigraphy the technique has been demonstrated; however, the poor spacial resolution inherent to the modality and the substantial dose of radioactivity administered to the patient has hindered its widespread use. This article will review the different classes of contrast agents in MRI, with special focus on the strategies involved in the development of targeted tissue-specific MRI contrast agents for the early detection of breast cancer. The features of a new class of contrast agents for targeted MR imaging will be described. Gadolinium-containing melanin polymers (GMP's) have been synthesized as MR contrast agents in our laboratory. These GMP's demonstrate significantly higher relaxivities than any other paramagnetic contrast agents reported; consequently, they are extremely effective contrast enhancing, imaging agents by themselves. The successful coupling of these potent GMP's to a monoclonal antibody specific for breast carcinoma, the 323/A3 monoclonal antibody, suggests that in vivo tissue-specific MR imaging, at the receptor level, will become feasible in the near future.
Breast Cancer Res Treat 1994
PMID:New magnetic resonance imaging techniques for the detection of breast cancer. 781 81


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