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PubMed1979

Distribution, frequency, and quantitative analysis of estrogen, progesterone, androgen, and glucocorticoid receptors in human breast cancer.

The distribution and frequency of steroid hormone receptors are described 329 patients with breast cancer. The distribution of each of the steroid hormone receptors is unimodal with a progressive increase in the proportion of patients positive at lower receptor values. Receptor values expressed as fmol/mg cytoplasmic protein are well correlated with values expressed as fmol/mg breast tumor. Estrogen receptor was positive in 53% of the patients; progesterone receptor was positive in 38% of the patients; glucocorticoid receptor was positive in 52% of the patients; and androgen receptor was positive in 31% of the patients. The type of tissue assayed did not affect steroid hormone receptor positivity. For primary tumors, there was no correlation between steroid hormone receptor positivity and location of the tumor in the breast, size of the tumor, or extent of the disease. Each of the steroid hormone receptors was positively associated with each of the other steroid hormone receptors. Estrogen receptor was correlated with menopausal status and axillary nodal status, but these correlations did not exist for the other steroid hormone receptors. Estrogen receptor was not correlated with age after adjustment for menopausal status. The other steroid hormone receptors were not correlated with age.

Adult↗
PubMedDate not supplied

[Sex hormone regulation of progesterone and estradiol receptors in the cytosol of human endometrium in normal and pathologic pregnancy].

Hormonal control of progesterone and estradiol receptors was studied in the cytozol of short-lived culture of human endometrium in normal and undeveloping pregnancy. Endometrium was cultivated in the presence of estradiol or progesterone for 16 hours. In cultivation of normal endometrium with estradiol the content of estradiol receptors increased 4-fold in comparison with unstimulated tissue, and of progesteron receptors--3-fold. In cultivation of normal endometrium with progesterone the content of estradiol receptors rose 4--5-fold, and of progesterone receptors--3-fold. In cultivation of pathological endometrium with estradiol or progesterone the number of estradiol receptors was only doubled, and of progesterone receptors--increased only 1 1/2 times, this pointing to a diminished sensitivity of pathological endometrium to the regulating action of sex hormones.

Cells, Cultured↗
PubMed1979

A correlation between estrogen sulfotransferase levels and estrogen receptor status in human primary breast carcinoma.

Estrogen sulfotransferase (EC 2.8.2.4) activity and estrogen receptor levels were measured in 32 human primary breast cancer cytosol preparations. Two types of tumors were identified: type 1, in which estrogen sulfotransferase levels were low (less than 40 pmol 17 beta-estradiol 3-sulfate formed per mg protein per 2 hr) and were independent of [35S]adenosine 3'-phosphate 5'-phosphosulfate production from [35S]sulfate and adenosine triphosphate, and type 2, in which estrogen sulfotransferase levels ranged from 50 to 200 pmol 17 beta-estradiol 3-sulfate per mg protein per 2 hr and were correlated with [35S]adenosine 3'-phosphate 5'-phosphosulfate formation (r = 0.70; p less than 0.005). In type 1 tumors, 11 of 16 were estrogen receptor negative; in type 2 tumors, 2 of 16 were receptor negative. Estrogen sulfotransferase levels in receptor-negative tumors were significantly lower than the levels in receptor-positive tumors (p = 0.025).

Breast Neoplasms↗
PubMed1979

Characteristics of the dextran-coated charcoal assay for estradiol receptor in breast cancer preparations.

The measurement of E2 receptor (E2R) in human breast cancer cytosol is significantly influenced by conditions usually employed in the dextran-coated charcoal assay. The incubation time and temperature have an influence on the rate of binding and stability of the receptor. Since lower temperatures preserve the integrity of the receptor, a 2 hr incubation at 4 degrees was selected as the standard incubation procedure. These conditions allow for the detection of at least 80% of the E2R. With supernatants from high-speed centrifugation of HBT biopsies or the human breast cancer cell line MCF-7, reducing agents increased the apparent E2R binding in the order: DTT greater than G-SH greater than MTG. The maximum enhancement of specific E2R binding by a given thiol agent was dependent on its concentration in the incubation medium. The optimum DTT level (7.5 mM) for MCF-7 cell homogenization and cytosol equilibration with tritiated E2 increased E2R to two times control (no DTT). For the HBT 150,000 g supernatant, 1 mM DTT was required to optimize the E2R quantitation. The duration of the dextran-coated charcoal extraction of the cytosol-[3H]E2 incubation had no effect on the level of E2R up to 21 hr. Minimum levels of nonspecific binding of [3H]E2 could be obtained after 4 hr extraction. Maximum depletion of specific [3H]E2 binding could be obtained by adding between 200- and 1000-fold molar excess of unlabeled E2. Greater amounts of unlabeled steroid displaced the radioactive E2 from the dextran-coated charcoal, thereby artifactually increasing the apparent nonspecific binding. This phenomenon may be overcome by utilizing more dextran-coated charcoal in the extraction. However, there was a 9% loss of specifically bound [3H]E2 per milligram of dextran-coated charcoal (1:10 dextran to charcoal by weight) when the cytosol protein was below 90 microgram per incubation. Supplementation with 200 microgram or more albumin per incubation prevented this loss. The dextran:charcoal ratio also prevented E2R loss in the order: 1:1 greater than 1:10 greater than 1:100. One milligram of dextran-coated charcoal (1:10) has the capacity to adsorb 0.3 to 0.4 microgram of free E2. Other unlabeled competitors are capable of displacing [3H]E2 on the receptor. Although DES was as effective as E2, U11,100A and estrone were inefficient competitors. It appeared that the levels of these two estrogen analogues required to maximally displace [3H]E2 on receptor also eluted labeled E2 from the dextran-coated charcoal. DES, however, was unable to displace significant quantities of the [3H] E2 from dextran-coated charcoal even at a molar excess of 50,000:1.

Biopsy↗
PubMed1979

The immunoendocrinology of estrophilin.

Immunoglobulin from the serum of rabbits immunized with highly purified estradiol-receptor complex from calf uterine nuclei has been shown to contain specific antibodies to estrophilin by five criteria. Antibodies to calf nuclear estrophilin cross react with nuclear estradiol-receptor complexes of rat, rabbit and sheep uterus, rat endometrial and pituitary tumor, and MCF-7 human breast cancer cell line. They also react with extranuclear receptor of calf, rat, mouse, rabbit, guinea pig, monkey and sheep uterus, rat mammary, endometrial and pituitary tumor, and human breast cancer. There is no interaction of the antibody with estradiol itself. The nuclear form of estrophilin appears to bind more immunoglobulin molecules than does the cytosol form. The antibodies do not react with either the nuclear or extranuclear dihydrotestosterone-receptor complexes of rat prostate, with the extranuclear progesterone-receptor complexes of rabbit uterus, chick oviduct or rat endometrial tumor, or with rat and mouse alpha-fetoprotein. These findings indicate an immunochemical similarity among estrophilins from several mammalian species, as well as between nuclear and extranuclear forms of the receptor, but not among receptor proteins for different steroid hormones. Immunoglobulin from the serum of a goat immunized with similar antigen shows a considerably higher titer of antibodies to estrophilin. These react with nuclear and extranuclear estradiol-receptor complexes of calf uterus to produce somewhat larger entities than those formed with the rabbit antibody. Unlike the rabbit antibody, interaction with the goat antibody causes a noticeable decrease in estradiol-binding affinity of the extranuclear estrophilin as well as an apparent decrease in the total hormone-binding capacity. Specific antibodies to estrophilin offer promise as valuable reagents for receptor analysis and purification, as well as for the elucidation of many still unresolved questions concerning receptor synthesis, localization and function.

Animals↗
PubMed1978

Correlation between clinical response to hormone therapy and steroid receptor content in prostatic cancer.

Hormonal therapy is the dominating form of treatment for prostatic carcinoma. The majority of cases (80%) are well controlled for varying times with this regimen. However, thus far there have been no adequate methods to predict in which cases hormonal therapy is of less benefit. Measurement of cancer tissue content of intracellular hormone receptors constitutes progress toward a more individualized therapy in prostatic carcinoma. In this study biopsies from 16 cancer patients were taken before therapy was given, and the specimens were analyzed with regard to content of specific methyltrienolone-binding sites. A correlation has been made between receptor content and clinical response to hormonal therapy in each case. Twelve specimens contained measurable amounts of steroid receptors. Of these, one patient died during irradiation therapy before onset of hormonal treatment. However, of the remaining 11 patients, 9 responded well to hormones (9/11 approximately 82%). The two receptor-positive nonresponders had the lowest measurable receptor levels in the series. Four specimens contained no detectable amounts of receptors. Three of these patients showed no response to therapy (3/4 = 75%) but one was "false negative." Our data indicate that steroid receptor analysis may become a valuable diagnostic tool in individualizing the therapy for prostatic cancer.

Aged↗
PubMed1979

Steroid receptor content in human prostatic carcinoma and response to endocrine therapy.

Biopsy material from primary prostatic carcinoma from 25 patients was analyzed with regard to cytosol content of methyltrienolone (a synthetic androgen) binding sites and the receptor content has been correlated to the clinical response to endocrine therapy. A dextran-coated charcoal technique was used and binding data were calculated from Scatchard plots. In 20 of the tumors detectable levels of methyltrienolone receptor were noted. One of the receptor-positive patients died during radiation therapy before onset of hormonal treatment, and a second patient, who had a highly differentiated carcinoma, so far has not received any endocrine therapy. Of the remaining 18 patients 15 responded well to castration, treatment with estrogens, or Estracyt (approximately 80%). The biopsies from two of the three receptor-positive non-responders contained the lowest measurable receptor levels. Five specimens lacked detectable amounts of methyltrienolone receptor. Four of these patients did not respond to therapy (approximately 80%), but one was "false" negative. Our data indicate that steroid receptor analysis may become an important tool in predicting the value of endocrine therapy in human prostatic carcinoma.

Aged↗
PubMed1978

Estradiol receptor analysis in human breast cancer tissue by isoelectric focusing in polyacrylamide gel.

Isoelectric focusing in polyacrylamide gel combined with limited proteolysis is a simple and specific method for quantitation of estradiol receptors in breast cancer tissue. At least eight different samples can be analyzed simultaneously on one gel, and the whole procedure, including sample preparation, takes less than 7 hr. In comparison with sucrose gradient centrifugation, isoelectric focusing is more sensitive, possibly due to the short time (1.5 to 2 hr) needed for the analysis. Furthermore, only one incubation with tritium-labeled estradiol is needed for an analysis, which means that a smaller amount of tumor tissue is needed than for most other methods. This fact allows analysis of the estrogen receptor content in tumor material obtained from fine-needle biopsy.

Breast Neoplasms↗
PubMed1975

The NSILA-s receptor in liver plasma membranes. Characterization and comparison with the insulin receptor.

NSILA-s (nonsuppressible insulin-like activity, soluble in acid ethanol) is a serum peptide that has insulin-like and growth-promoting activities. We have demonstrated previously that liver plasma membranes possess separate receptors for NSILA-s and insulin and have characterized the insulin receptor in detail. In the present study we have characterized the properties and specificity of the NSILA-s receptor and compared them to those of the insulin receptor in the same tissue. Both 125I-NSILA-s and 125I-insulin bind rapidly and reversibly to their receptors in liver membranes; maximal NSILA-s binding occurs at 20 degrees while maximal insulin binding is seen at 1-4 degrees. The pH optimum for NSILA-s binding is broad (6.0 to 8.0), in contrast to the very sharp pH optimum (7.5 to 8.0) for insulin binding. Both receptors exhibit a high degree of specificity. With the insulin receptor, NSILA-s and insulin analogues compete for binding in proportion to their insulin-like potency: insulin greater than proinsulin greater than NSILA-s. With the NSILA-s receptor, NSILA-s is most potent and the order is reversed: NSILA-s greater than proinsulin greater than insulin. Furthermore, six preparations of NSILA-s which varied 70-fold in biological activity competed for 125I-NSILA-s binding in order of their potencies. NSILA-s which had been inactivated biologically by reduction and aminoethylation and growth hormone were less than 1/100,000 as potent as the most purified NSILA-s preparation. Purified preparations of fibroblast growth factor, epidermal growth factor, nerve growth factor, and somatomedins B and C were less than 1% as effective as NSILA-s in competing for the 125I-NSILA-s suggesting that these factors act through other receptors. In contrast, somatomedin A was 10% as active as NSILA-s and multiplication-stimulating activity was fully as active as NSILA-s in competing for the NSILA-s receptor. Analysis of the data suggests that there are approximately 50 times more insulin receptors than NSILA-s receptors per liver cell, while the apparent affinity of NSILA-s receptors is somewhat higher than that of the insulin receptor.

Animals↗