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

Breast cancer specimens from 114 patients were assayed for the presence of estrogen receptors (ER) utilizing highly specific, monoclonal antiestrophilin antibodies and the peroxidase-antiperoxidase technique. Results were compared with conventional ER determinations by the dextran-coated charcoal method (DCC) and were in agreement as to positivity and negativity in 86%. Semiquantified immunocytologic assay results were in accord with the level of ER as measured by DCC in 66%. The tumors studied included 43 from patients with Stage IV disease where clinical response to hormonal manipulation was known. In the latter group, the immunohistologic method had a sensitivity similar to that of DCC but showed a superior positive predictive value and a significantly better specificity. These results indicate that this new method is a valuable laboratory tool, enabling prediction of hormone responsiveness in advanced mammary carcinoma and capable of performance at the community hospital level.
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PMID:Immunohistologic localization of estrogen receptors in breast cancer with monoclonal antibodies. Correlation with biochemistry and clinical endocrine response. 397 44

Based on previous studies of the properties of moxestrol, we hypothesized that a radiohalogenated analog of moxestrol, [125I]11 beta-methoxy-17 alpha-iodovinyl-estradiol [( 125I] MIVE2), should bind to the estrogen receptor (ER) in some ovarian adenocarcinomas (OVCA), thereby offering the potential for imaging and/or treatment of these cancers. We used monoclonal antibodies (H222, H226, and D547) against human breast cancer ER to identify the [125I]MIVE2-binding moiety in OVCA cytosols that is found on high salt sucrose gradients. After gel electrophoresis and western blotting, exposure of OVCA extracts to the ER antibodies, followed by exposure to goat antirat serum and then rat peroxidase antiperoxidase, demonstrated a moiety in OVCA that migrated indistinguishably from the ER in MCF-7 human breast cancer cells and from that in specimens of breast cancer tissue. Because few studies have demonstrated efficacy of hormone management for OVCA, we also wanted to learn whether ER exists in multiple forms in OVCA, in view of the possibility that some forms may be inactive in regulating growth-dependent cell functions while retaining estrogen-binding capacity. By incubating the monoclonal antibodies H222, H226, and D547, each of which recognizes a different region on the ER protein, with OVCA cytosol fractions, we demonstrated that ER in OVCA can exist in multiple forms, some of which fail to express an H226-recognized site and some of which fail to express a D547-recognized site. This observation indicates that a relationship may exist between the presence or absence of certain forms of ER in ovarian epithelial cancer and a patient's response to hormone therapy.
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PMID:Monoclonal antibody recognition of multiple forms of estrogen receptor tagged with [125I]methoxy-iodovinyl estradiol in ovarian carcinomas. 401 11

The presence of Tissue Polypeptide Antigen (TPA) and Carcino-embryonic Antigen (CEA) in serial sections of 32 breast carcinomas and one case of neurofibrosarcoma was demonstrated by immunocytochemistry using the indirect peroxidase technique. The neurofibrosarcoma was negative for TPA and CEA. All 32 specimens of breast cancer were positive for TPA and/or CEA. In 12 cases the staining was strongly positive for both TPA and CEA. In other cases either TPA or CEA was more abundant in the tumor. The overall concordance of staining was 58%, which is in relative agreement with the correlation between values for TPA and CEA in serum from patients with breast cancer. The finding that in addition to the difference between tumors, there was a difference within tumors was interesting. This indicated that TPA and CEA may be synthesized during partly different phases of the proliferative cycle.
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PMID:Immuno-histochemical localization of tissue polypeptide antigen (TPA) and carcino-embryonic antigen (CEA) in breast cancer. A comparative study. 618 81

Fusion of splenic lymphocytes from Lewis rats, immunized with affinity-purified estrogen receptor from the cytosol of MCF-7 human breast cancer cells, with two different mouse myeloma lines, has provided 13 monoclonal hybridoma lines secreting antiestrophilin antibodies, each of which (with one possible exception) recognizes a different antigenic determinant in the human receptor molecule. Of this library of monoclonal antibodies, some react with estrophilin from all sources tested, some react with mammalian but not avian receptors, whereas one preparation appears specific for estrophilin from primate sources. By proteolytic digestion under controlled conditions with mercury-deactivated papain, chymotrypsin, and trypsin, respectively, it is possible to remove sequentially the determinants recognized by one, two or three of the monoclonal antibodies, leaving the epitopes for the six remaining antibodies investigated on the steroid-binding portion of the receptor. The proteolytic fragment containing the epitope most readily removed (by mercuripapain) also contains the DNA-binding domain of the activated receptor molecule. Immunocytochemical staining, using the peroxidase procedure with various monoclonal antibody preparations, of frozen sections of human breast cancer tissue, fixed in ethanol or in picric acid-formaldehyde reagent, shows clearly that the majority of the native receptor, which appears in the cytosol after tissue homogenization, is actually localized within the nuclear compartment in the intact cell. The immunocytochemical technique also permits the identification of mixed populations of receptor-containing and non-containing cells in human breast cancers.
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PMID:Immunochemical studies of estrogen receptors. 620 Jul

The intracellular uptake of alphafetoprotein (AFP) and its fluorescein conjugates, by cultures of the MCF-7 human breast cancer cell line, has been demonstrated using an indirect immuno-peroxidase technique or by direct visualization under fluorescent lighting. The protein was localized in the cytoplasm. Ultrastructural autoradiographs of MCF-7 cells incubated with human 3H-AFP showed protein accumulation in several cytoplasmic organelles, particularly in lipid droplets. Nuclei were free of AFP. A significant species-specificity of AFP internalization was observed in comparative assays with human, mouse, pig and chicken AFP. The incorporation of the protein was prevented by incubation at 0 degrees C or by previous treatment of the cultures with 10nM sodium azide. Attention is paid to the reappearance in a human breast carcinoma cell line of a property associated during ontogenic development with ectodermal derivatives, including the epidermis.
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PMID:Incorporation of alphafetoprotein by the MCF-7 human breast cancer cell line. 620 95

Human breast carcinoma contains high-affinity receptors for the basement membrane glycoprotein laminin. Plasma membranes isolated from tissue samples of human breast carcinoma exhibit specific, saturable, reversible, and displaceable binding to laminin. Fibronectin, collagen, and serum proteins fail to displace this bound laminin. Scatchard analysis is linear with a Kd of 1.8 X 10(-9) M. The laminin receptor, isolated and purified 1200-fold by laminin-affinity chromatography, exhibits a molecular weight of 67 000 daltons as determined by gel electrophoresis. The receptor was verified to be located on the cell surface of the invading breast carcinoma cells by immunohistologic studies utilizing a peroxidase-conjugated fragment of the laminin molecule which contained the receptor-binding domain.
Breast Cancer Res Treat 1984
PMID:Characterization of a laminin receptor from human breast carcinoma tissue. 623 95

An antigen immunologically related to mouse mammary tumor virus (MuMTV) and the major envelope glycoprotein, gp52 of MuMTV, was identified in tissue sections of human male and female mammary carcinomas using the peroxidase-antiperoxidase technique. The specificity of the reaction was established by absorption studies. Positive reactions with the gp52 antiserum were seen in mouse and human mammary carcinomas, but not in normal mammary tissues, mammary tissues with benign diseases and in other primary malignant neoplasms. Almost all (32/36, 89%) male mammary carcinomas were positive for the gp52 related antigen. A lesser proportion of tumors among female patients (14/50, 28%) were positive. The gp52 positive tumors were significantly larger than the gp52 negative tumors in female patients (P less than 0.05). Gp52 positive tumors were also larger than gp52 negative tumors in male patients, but the difference was not statistically significant. Gp52 reactivity was also detected in metastatic mammary carcinoma in axillary lymph nodes of male and female patients. The presence of gp52 related antigen was not apparently related to tumor grade or lymphocytic infiltrate in the primary tumor. The data do not permit a firm conclusion regarding nodal status in men; no correlation of gp52 activity and nodal status in women was evident. These results indicate that mammary carcinomas in men as well as in women have an antigen related immunologically to MuMTV gp52. Other than tumor size, the antigen seems to be unrelated to major prognostic factors. The significance of the antigen with respect to etiologic features and prognosis in breast cancer remains to be determined.
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PMID:Murine mammary tumor virus related antigen in human male mammary carcinoma. 629 11

Monoclonal antibodies against a 24,000 dalton intracellular estrogen-regulated protein in human breast cancer cells were used to study storage conditions and the effects of monoclonal antibody concentrations on immunohistochemical antigen localization. Both hybridoma supernatants and ascites fluid obtained from mice injected with hybridoma cells were used as sources of monoclonal antibodies; the monoclonal antibodies in the ascites fluid were concentrated and purified. Both antibody preparations were stored at 4, -20, or -70 degrees C and periodically tested for activity at these storage conditions. There was no difference in activity for the antibodies between storage at -20 and -70 degrees C. However, when highly diluted antibody was stored at 4 degrees C, the activity was lost within 2 weeks if carrier proteins were not added. These monoclonal antibodies were applied to immunohistochemical staining of different mouse and human tissues processed for routine paraffin sections, using the avidin-biotin-peroxidase procedure. A monoclonal antibody of unrelated specificity was used as control. When these antibodies were used at high concentrations, all the different tissues examined were immunostained. With reduction of the antibody concentration, an immunohistochemical dissection of the tissues was seen until specific immunostaining was reached. When even more highly diluted monoclonal antibody was used, heterogeneity in the staining pattern became very high. On the basis of these results, certain immunohistochemical criteria are proposed for the selection of the optimum concentration of monoclonal antibodies for specific antigen detection.
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PMID:Monoclonal antibody storage conditions, and concentration effects on immunohistochemical specificity. 634 59

Immunoperoxidase reaction of appropriately fixed tissue with an antiserum to catechol-o-methyl transferase (COMT), as the primary step in the peroxidase-immunoglobulin bridge technique, has been utilized for the localization of COMT in biopsy specimens of human breast neoplasm and its metastases. Our immunocytochemical identification of a strong activity of COMT in all cases studied might have a diagnostic implication in breast cancer.
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PMID:Immunoperoxidase localization of catechol-o-methyl transferase (COMT) in human breast cancer. 634 77

We have used monoclonal antiestrophilin antibodies to develop an improved immunocytochemical method for localizing estrogen receptors in tissue sections with an indirect immunoperoxidase technique. Rat monoclonal antibodies were raised against human estrogen receptor (estrophilin) protein derived from the cytosol of MCF-7 human breast cancer cells. These monoclonal antibodies have been shown to have extensive cross-reactivity with estrogen receptors from various primate and nonprimate tissues. We have used frozen sections of human proliferative phase endometrium and an indirect immunoperoxidase technique to establish conditions for demonstrating estrogen receptor antigenic determinants in frozen tissue sections. The method involves (a) brief fixation with formaldehyde-containing fixatives either prior to freezing or immediately after cutting cryostat sections, (b) bleaching the tissue of endogenous peroxidase activity, (c) application of primary antibody or control immunoglobulin, (d) application of an adsorbed bridging antibody (goat antirat IgG), and (e) application of rat peroxidase-antiperoxidase followed by diaminobenzidine. Specific nuclear staining for estrogen receptor antigenic determinants was observed in the vast majority of epithelial and stromal cells. No specific cytoplasmic staining was identified in cryostat sections of any of the 17 cases studied for this report.
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PMID:An immunocytochemical method for demonstrating estrogen receptor in human uterus using monoclonal antibodies to human estrophilin. 636 73


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