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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 184 patients were analyzed for estrogen binding by two different histochemical techniques using conjugates of estradiol, bovine serum albumin, and fluorescein. In one conjugate estradiol was bound at position 6, in the other at position 17. Results were in agreement in 64% (p less than .001), but obvious differences in ligand distribution were noted. Results were also correlated with estrogen receptor (ER) analysis by dextran-coated charcoal assay (DCC) and were in accord in 65% and 67% of specimens respectively (p less than .001). In 114 cases, the tissue samples were also studied with the estrogen receptor immunocytochemical assay (ERICA) of Greene and his colleagues, which employs monoclonal antibodies to ER protein. Results were in accord with DCC in 86% (p less than .001). The pattern of staining with ERICA differed from that of either histochemical method. In 43 cases assay results were correlated with clinical endocrine response. Overall, the best statistical prognostic parameters were obtained with ERICA. Analysis of combined assay results revealed that patients with assays positive by all techniques were the most likely to respond to hormonal treatment (p less than .001), whereas if one or more assays were negative the chances for a good response were significantly less favorable. These data suggest that DCC and ERICA are both a measure of the same estrogen binding site (type I) while the histochemical methods apparently identify two other separate and distinct sites (putative type II sites). A degree of positive interaction may exist between these multiple estrogen binding sites.
Breast Cancer Res Treat 1985
PMID:Heterogeneity of estrogen binding sites in breast cancer: morphologic demonstration and relationship to endocrine response. 389 73

The influence of total parenteral nutrition (TPN) on nutritional assessment of patients with recurrent cancer was studied. One hundred forty-six patients with recurrent gastric, colorectal and breast cancer who have been admitted to our hospital during the past five years were surveyed. Serum albumin and cholinesterase levels on admission in the gastric and breast cancer patients who died in the hospital were considerably lower than those of the patients who recovered sufficiently to be discharged from the hospital. The patients with recurrent gastric cancer who received TPN for more than a week were also analyzed. It was shown that those whose levels of serum total protein and albumin did not respond favorably to TPN were the patients with shortest survival. Therefore, by checking the response to the administration of TPN, it seems to be possible to predict the patient's prognosis.
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PMID:[Influence of total parenteral nutrition (TPN) on nutritional incidences in patients with recurrent cancer]. 393 22

Cox's proportional hazards regression model was used to analyze the prognostic significance of multiple variables affecting recurrence and survival in patients with Stage II breast cancer. Among the variables were biochemical estrogen (ER) and progesterone receptor (PgR) values and results of a histochemical estrogen-binding assay using a fluoresceinated bovine serum albumin-estradiol conjugate where carrier and label were bound at position 17. In 190 cases ER and PgR were not found to be significantly associated with either disease recurrence or patient survival. On the other hand, patients with tumors that were demonstrably "rich" in estradiol ligand conjugate binding by histochemistry experienced both a longer disease-free interval (P less than 0.03) and survival (P less than 0.02) than did patients whose tumors were "poor" in conjugate binding or showed a heterogeneous population of positively and negatively stained cells. A patient with a tumor rich in estrogen binding was five times more likely to survive than a patient with a neoplasm that was poor in estrogen binding by histochemistry. These results indicate that the histochemical technique used provides new and independent parameters for determination of prognosis in Stage II breast cancer.
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PMID:Histochemical estrogen binding. An independent predictor of recurrence and survival in stage II breast cancer. 394 24

Estrogen, prolactin, and other tissue-derived factors are implicated in the etiology and pathophysiology of human breast cancer (HBC). In a previous study, we demonstrated that a factor(s) secreted by rat pituitary tumor cells (GH3) synergizes with estrogen to induce growth of HBC cells (T-47D) transplanted into athymic nude mice. The present studies were carried out to characterize further this pituitary growth factor. Pituitary tumor cell lines (GH3, GH1, 235-1, and AtT-20) and normal rat pituitaries were transplanted s.c. into estrogen-treated (estradiol valerate injection, 500 micrograms/14 days) athymic nude mice which also received T-47D cells. The influence of the presence of these normal and tumorous pituitary cells on growth (size and weight) of T-47D tumors was monitored for 49 to 56 days. The results indicate that factor(s) from normal rat pituitary glands as well as from the GH1 and GH3 but not 235-1 and AtT-20 pituitary tumor cells were able to potentiate the growth of T-47D tumors in estrogenized mice. To ascertain whether or not prolactin and/or growth hormone are responsible for the growth-promoting activity, purified human and ovine growth hormone and ovine prolactin were administered to estrogenized athymic nude mice either by daily s.c. injection (100 micrograms/day) or by constant infusion using Alzat osmotic minipumps (1.25 and 5.0 micrograms/h) for 29 to 56 days. None of these treatments stimulated the growth of the T-47D tumors, suggesting that prolactin, growth hormone, and their intermediates may not be directly involved. We further determined whether the factor from pituitary tumor cells was present in serum-free conditioned medium and could stimulate the growth of HBC cells in vitro. Conditioned medium from GH3 and GH1 but not from 235-1 and AtT-20 pituitary cells significantly stimulated growth of T-47D cells in the presence of estradiol (10(-10) M) after 12 days of culture in a serum-free medium (Dulbecco's modified Eagle's medium containing bovine serum albumin, 0.5 mg/ml). Optimal serum-free growth of T-47D cells (2-fold above control) was observed in the presence of estradiol (10(-10) M) and conditioned medium (30% v/v) from 48-h cultures of GH3 cells. The bovine serum albumin concentration of the serum-free medium (Dulbecco's modified Eagle's medium) was also important: optimal T-47D cell proliferation was observed with BSA between 0.5 and 2.0 mg/ml. Conditioned medium preparations from serum-pretreated flasks (without cells) from GH3 cell monolayers for zero time and from actinomycin D plus cycloheximide-inhibited GH3 cells were inactive.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Evidence for a novel pituitary factor that potentiates the mitogenic effect of estrogen in human breast cancer cells. 400 46

In human tumor cells freshly obtained from patients with breast cancer, ovarian cancer, or adenocarcinoma of unknown etiology and in normal human bone marrow cells, the cell-to-medium ratio (intracellular/extracellular concentration) in vitro of 5.42 microM melphalan rose rapidly to levels of 6-17 after 35 min at 37 degrees C in Dulbecco's phosphate-buffered saline containing bovine serum albumin and glucose. Only patient C (breast cancer) had received chemotherapy. In all cells studied, L amino acids (1 mM) such as leucine, glutamine, tyrosine, and methionine reduced the cell-to-medium ratio of melphalan at 3 and 35 min. There was a good correlation between the reduction of melphalan transport at 35 min in the heterogeneous nucleated bone marrow cell population by amino acids and their effect on melphalan cytotoxicity in the CFU-C system. Aminoisobutyric acid (A1B), a specific substrate of the A system of amino acid transport, at a concentration between 1 and 50 mM had no significant effect on melphalan uptake at 3 min in any of the human cells studied except those of patient C. At 35 min A1B (10 or 50 mM) significantly reduced the intracellular melphalan concentration in normal bone marrow cells and tumor cells from patients B and C. At 2 mM, 2-aminobicyclo-(2, 2,1)-heptane-2-carboxylic acid (BCH), a specific substrate of the L system of amino acid transport, reduced the cell-to-medium ratio to 70% of control at 3 and 35 min in human bone marrow cells. In tumor cells from patients A, B, D, and F, 2 mM BCH had no significant effect on melphalan uptake at 3 min; it slightly decreased uptake in tumor cells from patient C. At 35 min, 2 mM BCH significantly reduced melphalan transport in tumor cells from patients C and F only. The lack of a BCH-suppressible component to melphalan uptake into human tumor cells freshly obtained from previously untreated patients contrasts with the presence of this component in murine L1210 leukemia cells, murine P388 leukemia cells, and human tumor cell lines. This suggests that minor differences in melphalan transport may exist amongst species and also between human tumor cells which are freshly obtained and cell lines maintained in culture.
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PMID:Effects of amino acids on the transport and cytotoxicity of melphalan by human bone marrow cells and human tumor cells. 401 61

Evidence is presented for the existence of specific receptors for alpha-fetoprotein on the surface of MCF-7 human breast cancer cells. At 4 degrees C, the binding of alpha-fetoprotein to these cells displayed a biphasic saturation curve. Scatchard analysis revealed the presence of at least two binding sites with dissociation constants of 4.5 X 10(-9) M (2,000 sites/cell) and 1.3 X 10(-8) M (135,000 sites/cell), respectively. Binding was inhibited by 85% in the presence of a 5,000-fold excess of unlabeled alpha-fetoprotein and by 50% with the same excess of serum albumin. Competition by other serum proteins was not significant. At 37 degrees C, alpha-fetoprotein was endocytosed and the uptake curve reached a plateau after 3-4 hours of incubation.
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PMID:Alpha-fetoprotein receptors in a human breast cancer cell line. 620 54

The ability to internalize alpha-fetoprotein (AFP) and serum albumin, which is characteristic of embryonic and fetal elements undergoing differentiation, may reappear in some cultured neoplastic cells (i.e., the MCF-7 human breast cancer cell line). The in vivo uptake of AFP by spontaneous carcinomas of the CH3/Bi mouse was investigated. Nineteen mice were given i.v. injections of approximately 10 muCi of mouse 125I-AFP (0.6 to 4 micrograms of AFP according to the specific ratio of the preparation used). Four to 7 days later, the animals were sacrificed. The radioactivity concentration in the tumor was the highest among all solid tissues examined. Tumor:liver radioactivity ratios were clearly positive [3.6 +/- 0.3 (S.E.)] in 27 of 31 specimens studied. Microscopy examination of autoradiograms from various tissue sections confirmed the selective accumulation of radioactive AFP in the tumors. In order to assess the specificity of AFP uptake by mammary tumors, 4 mice were given simultaneous injections of 125I-AFP and 131I-ovalbumin, respectively. Compared to AFP, the retention of ovalbumin was very low in all tissues studied, including the tumor. The possibility of tumor localization of radiolabeled AFP by external photoscanning was also explored. Two mice were given injections of 131I-AFP, one mouse received 131I-serum albumin, and one was given 131I-ovalbumin. Images were obtained 6 days after with a standard gamma-camera linked to a computer with data display. About 50% of the total radioactivity retained was concentrated in the tumor areas of mice given injections of iodinated AFP, while it was only 15% in the mouse that received 131I-serum albumin. No tumor image could be detected in the mouse given ovalbumin. These results show that the ability to internalize AFP, common to many tissues during ontogenesis, may also be shared by neoplastic cells which develop later in life. They also prove the preferential uptake of AFP by the tumors compared to normal tissues and the usefulness of AFP as a radiotracer for mammary carcinomas. The latter represents a novel approach to tumor detection.
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PMID:Uptake of radiolabeled alpha-fetoprotein by mouse mammary carcinomas and its usefulness in tumor scintigraphy. 620 15

We tested the ability of hormones and growth factors to enhance the colony formation in soft agarose of breast carcinoma using two human breast carcinoma cell lines, MCF-7 and MDA-MB231, MCF-7 could clone in a basal medium supplemented only by insulin, transferrin, prostaglandin F2 alpha, and fibronectin. Combining oestradiol, dexamethasone, insulin, transferrin, and triiodothyronine with a basal medium supplemented with 5% (v/v) foetal bovine serum (FBS) increased colony forming efficiency (CFE) two-to three-fold over the best obtained in serum supplemented medium without hormones. While optimal CFE was seen in the hormonally supplemented medium plus 5% FBS, clonal anchorage independent growth could also be obtained without serum for both cell lines by substituting 0.5-1% (v/v) bovine serum albumin (BSA) for FBS. Although CFE was enhanced with the addition of hormones, they did not substantially alter the in vitro chemosensitivity patterns of the cell lines to 8 cytotoxic drugs. Hormonally-supplemented medium with 5% FBS increased the CFE of a small number of fresh specimens of human breast cancer compared with medium supplemented with serum alone. The systematic study of requirements for the in vitro growth of human breast cancer may improve drug sensitivity testing by increasing our ability to grow this neoplasm in culture.
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PMID:Hormone supplemented media for cloning human breast cancer: increased colony formation without alteration of chemosensitivity. 635 59

Lyophilized receptor-positive tissue powders and cytosols, prepared from calf uterus and human breast tumor tissue, are used to assess the validity of routine dextran-coated charcoal estrogen receptor assays. Since 1978 lyophilized reference preparations have been analyzed twice yearly by 18 laboratories in the Netherlands. During 8 consecutive trials 20 different lyophilized samples were studied. The inter-laboratory variability of estrogen receptor results decreased with time. Most laboratories found receptor values around the median value of all groups together, though some participants consistently reported estrogen receptor values that were higher or lower than the median. The variability of estrogen receptor results between labs seemed to be associated with cytosol dilution, determination of non-specific binding, concentration and volume of dextran-coated charcoal, and the use of single dose assays or Scatchard analysis. The agreement on the presence or absence of estrogen receptors was more than 98% for lyophilized reference samples with high receptor content. For samples with low receptor content 85% agreement was observed, while 12% of the assays performed on receptor-negative material were reported to be estrogen receptor-positive. The use of the same protein determination (Coomassie Brilliant Blue) and human serum albumin standard has decreased the interlaboratory variation coefficient of the protein results to 7.5%.
Breast Cancer Res Treat 1983
PMID:Quality control of estrogen receptor assays in The Netherlands. 636 54

We tested the ability of a serum-free medium containing insulin, transferrin, 17 beta-estradiol, dexamethasone, triiodothyronine, prostaglandin F2 alpha, and fibronectin (HBCA medium) to support the continuous growth and passage of five human breast carcinoma cell lines on a collagen matrix. Doubling times of the cell lines (20 to 44 hr) were similar in HBCA and serum-supplemented media. The gross morphology of the cell lines was not altered in the serum-free medium. Insulin, transferrin, and the collagen matrix were the most essential factors required for optimal growth of the cell lines. Estradiol appeared to stimulate the growth of cell lines, both with and without estrogen receptors. HBCA medium supplemented with low concentrations of bovine serum albumin, Fraction V (0.5%, v/v), supported the clonal growth of three cell lines in soft agarose with colony-forming efficiencies superior to that observed with standard serum-supplemented medium. Deleting estradiol from HBCA medium reduced the colony-forming efficiency of the three cell lines. HBCA medium may be useful in studying hormonal regulation and improving the in vitro growth of human breast cancer.
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PMID:Continuous culture and soft agarose cloning of multiple human breast carcinoma cell lines in serum-free medium. 646 10


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