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Will Nolvadex help with Deca gyno?
- Thread starter CyBeRoiDs
- Start date
keep this thread aliveNolvadex will help with progestin induced/prolactin gyno...
Multihormonal regulation of the progesterone receptor in MCF-7 human breast cancer cells: interrelationships among insulin/insulin-like growth factor-I, serum, and estrogen.
Endocrinology 1990 Feb;126(2):891-8 (ISSN: 0013-7227)
Katzenellenbogen BS; Norman MJ [Find other articles with these Authors]
Department of Physiology and Biophysics, University of Illinois, Urbana 61801.
Estrogen (E) is well known to be an important stimulator of progesterone receptor (PR) synthesis in target cells. We have observed that E stimulation of PR in MCF-7 human breast cancer cells (as monitored by progestin binding or Western blotting with anti-PR antibodies) increases as a function of serum concentration in the cell culture medium; PR stimulation by E is greatest in high serum medium (5% or 10% charcoal dextran-treated calf serum) and is not observed when cells are in medium containing serum concentrations below 1%, although estrogen receptor levels are well maintained. This suggests that some serum factor(s) may be essential for E to be able to stimulate PR. To better understand such factors, we have grown cells in serum-free medium and in serum-free medium supplemented with insulin (6.25 micrograms/ml) [corrected], transferrin (6.25 micrograms/ml), selenium (6.25 ng/ml), albumin (1.25 mg/ml) [corrected], and linoleic acid (5.35 micrograms/ml; ITS+). Unexpectedly, we found that addition of ITS+ (without E) increases PR levels in these cells, especially in the absence of serum and under low serum conditions where E stimulation of PR is poor. Analyses of the individual components in ITS+ reveal that insulin is the major active component. Dose-response studies indicate that high superphysiological (greater than 1 microgram/ml) concentrations of insulin are required. In contrast, low physiological levels of insulin-like growth factor-I (IGF-I; 10 or 40 ng/ml) are active, suggesting mediation by the IGF type I receptor system. At all serum concentrations (0-10%), the effects of ITS+ and E in increasing PR are synergistic. The fact that anti-E are able to suppress the insulin/IGF-I stimulation as well as the E stimulation of PR suggests that the anti-E can actively interfere with the action of the growth factor as well as the action of E. These results indicate that regulation of PR is multifactor and raise the possibility that PR may be regulated in vivo by both E and growth factors such as IGF-I that are known to be increased in these breast cancer cells by E.
: Endocrinology 1990 Jan; 126(6):3217
---------------------------------------
Hormones as cancer growth factors.
Lancet 1984 Oct 13;2(8407):843-4 (ISSN: 0140-6736)
Israel L; Band P [Find other articles with these Authors]
It is postulated that some hormones may regulate proliferation of cancer cells in the same way as growth factors produced by cellular oncogenes. The gene coding for the hormone's specific receptor would also act as a cellular oncogene. Normal adult breast cells show few if any oestrogen receptors. In the model put forward the oestrogen receptors in breast cancer cells should not be regarded as a marker of differentiation but as a survival advantage for the tumour when oestrogens are present. Prolactin and somatomedin may also behave as growth factors. In relation to the antitumour effects of hormone antagonists such as tamoxifen, it is postulated that cancer cells are immortalised and prevented from full differentiation by the presence of growth factors and their receptors. If receptor genes are re-expressed through the process of neoplastic transformation, their presence in cancers from unresponsive normal tissues should be regarded as a common event
--------------------------------------------
Insulin-like growth factor 1 receptors in human breast cancer and their relation to estradiol and progesterone receptors.
Cancer Res 1988 Nov 15;48(22):6429-33 (ISSN: 0008-5472)
Peyrat JP; Bonneterre J; Beuscart R; Djiane J; Demaille A [Find other articles with these Authors]
Centre Oscar Lambret, Lille, France.
Insulin-like growth factor 1 (IGF1) binding sites were characterized in breast cancer. We demonstrate the presence of one high affinity binding site. Chemical cross-linking of 125I-IGF1 to breast cancer membranes in reducing condition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed one band with an apparent molecular weight of 130,000. The specificity of the binding was studied. IGF2 was a good competitor whereas insulin competed with a potency lower than 1/100 that of IGF1. This IGF1 binding corresponded to the previously described type 1 IGF receptor (IGF1-R). IGF1-R was determined in 76 human breast cancer biopsies. Ninety-three % of the tumors were positive. The specific binding range was 0-16.4%; the geometric IGF1-R mean level was 3.9%. There was a relation (chi 2 test) between IGF1-R and progesterone receptor positivity rates (P = 0.002). The IGF1-R concentrations were correlated (Spearman test) with those of estradiol receptor (P = 0.0018) and progesterone receptor (P = 0.0011). A positive linear correlation existed between IGF1-R and estradiol receptor (P = 0.006) and between IGF1-R and progesterone receptor (P = 0.003). Our demonstration of the presence of IGF1-R in human breast cancer biopsies suggests that IGF1, acting either via the endocrine, paracrine, or autocrine pathways, could stimulate tumor growth.
If you appreciate the studies, thank 'Ivan Drago' from Anabolic Fitness, he looked up the research, not I.
The bottom line is that increased IGF-1 level is nessecery for gyno to develope, no matter what is it ER, or PR.
Nolvadex lower IGF-1 level very effectively(by 24%)
-X
Multihormonal regulation of the progesterone receptor in MCF-7 human breast cancer cells: interrelationships among insulin/insulin-like growth factor-I, serum, and estrogen.
Endocrinology 1990 Feb;126(2):891-8 (ISSN: 0013-7227)
Katzenellenbogen BS; Norman MJ [Find other articles with these Authors]
Department of Physiology and Biophysics, University of Illinois, Urbana 61801.
Estrogen (E) is well known to be an important stimulator of progesterone receptor (PR) synthesis in target cells. We have observed that E stimulation of PR in MCF-7 human breast cancer cells (as monitored by progestin binding or Western blotting with anti-PR antibodies) increases as a function of serum concentration in the cell culture medium; PR stimulation by E is greatest in high serum medium (5% or 10% charcoal dextran-treated calf serum) and is not observed when cells are in medium containing serum concentrations below 1%, although estrogen receptor levels are well maintained. This suggests that some serum factor(s) may be essential for E to be able to stimulate PR. To better understand such factors, we have grown cells in serum-free medium and in serum-free medium supplemented with insulin (6.25 micrograms/ml) [corrected], transferrin (6.25 micrograms/ml), selenium (6.25 ng/ml), albumin (1.25 mg/ml) [corrected], and linoleic acid (5.35 micrograms/ml; ITS+). Unexpectedly, we found that addition of ITS+ (without E) increases PR levels in these cells, especially in the absence of serum and under low serum conditions where E stimulation of PR is poor. Analyses of the individual components in ITS+ reveal that insulin is the major active component. Dose-response studies indicate that high superphysiological (greater than 1 microgram/ml) concentrations of insulin are required. In contrast, low physiological levels of insulin-like growth factor-I (IGF-I; 10 or 40 ng/ml) are active, suggesting mediation by the IGF type I receptor system. At all serum concentrations (0-10%), the effects of ITS+ and E in increasing PR are synergistic. The fact that anti-E are able to suppress the insulin/IGF-I stimulation as well as the E stimulation of PR suggests that the anti-E can actively interfere with the action of the growth factor as well as the action of E. These results indicate that regulation of PR is multifactor and raise the possibility that PR may be regulated in vivo by both E and growth factors such as IGF-I that are known to be increased in these breast cancer cells by E.
: Endocrinology 1990 Jan; 126(6):3217
---------------------------------------
Hormones as cancer growth factors.
Lancet 1984 Oct 13;2(8407):843-4 (ISSN: 0140-6736)
Israel L; Band P [Find other articles with these Authors]
It is postulated that some hormones may regulate proliferation of cancer cells in the same way as growth factors produced by cellular oncogenes. The gene coding for the hormone's specific receptor would also act as a cellular oncogene. Normal adult breast cells show few if any oestrogen receptors. In the model put forward the oestrogen receptors in breast cancer cells should not be regarded as a marker of differentiation but as a survival advantage for the tumour when oestrogens are present. Prolactin and somatomedin may also behave as growth factors. In relation to the antitumour effects of hormone antagonists such as tamoxifen, it is postulated that cancer cells are immortalised and prevented from full differentiation by the presence of growth factors and their receptors. If receptor genes are re-expressed through the process of neoplastic transformation, their presence in cancers from unresponsive normal tissues should be regarded as a common event
--------------------------------------------
Insulin-like growth factor 1 receptors in human breast cancer and their relation to estradiol and progesterone receptors.
Cancer Res 1988 Nov 15;48(22):6429-33 (ISSN: 0008-5472)
Peyrat JP; Bonneterre J; Beuscart R; Djiane J; Demaille A [Find other articles with these Authors]
Centre Oscar Lambret, Lille, France.
Insulin-like growth factor 1 (IGF1) binding sites were characterized in breast cancer. We demonstrate the presence of one high affinity binding site. Chemical cross-linking of 125I-IGF1 to breast cancer membranes in reducing condition and sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed one band with an apparent molecular weight of 130,000. The specificity of the binding was studied. IGF2 was a good competitor whereas insulin competed with a potency lower than 1/100 that of IGF1. This IGF1 binding corresponded to the previously described type 1 IGF receptor (IGF1-R). IGF1-R was determined in 76 human breast cancer biopsies. Ninety-three % of the tumors were positive. The specific binding range was 0-16.4%; the geometric IGF1-R mean level was 3.9%. There was a relation (chi 2 test) between IGF1-R and progesterone receptor positivity rates (P = 0.002). The IGF1-R concentrations were correlated (Spearman test) with those of estradiol receptor (P = 0.0018) and progesterone receptor (P = 0.0011). A positive linear correlation existed between IGF1-R and estradiol receptor (P = 0.006) and between IGF1-R and progesterone receptor (P = 0.003). Our demonstration of the presence of IGF1-R in human breast cancer biopsies suggests that IGF1, acting either via the endocrine, paracrine, or autocrine pathways, could stimulate tumor growth.
If you appreciate the studies, thank 'Ivan Drago' from Anabolic Fitness, he looked up the research, not I.
The bottom line is that increased IGF-1 level is nessecery for gyno to develope, no matter what is it ER, or PR.
Nolvadex lower IGF-1 level very effectively(by 24%)
-X
Last edited:
Winstrol will help with progestin receptor activity, but to what degree, that's the Q
Ellis AJ, Cawston TE, Mackie EJ.
Rheumatology Research Unit, Addenbrooke's Hospital, Cambridge, UK.
The anabolic steroid stanozolol stimulates the production of prostaglandin E2 (PGE2) and the matrix metalloproteinases collagenase and stromelysin in human skin fibroblasts but not in rheumatoid synovial fibroblasts. The basis for these differential responses was investigated at the levels of DNA synthesis and steroid receptor binding. Stanozolol inhibited fibroblast growth factor (FGF)-stimulated DNA synthesis in both the skin and synovial fibroblasts, showing that both cell types were capable of responding to the compound. Competitive binding assays indicated that stanozolol bound specifically to both the skin and synovial fibroblasts. Binding of stanozolol to both cell types could be partially displaced by progesterone, indicating that stanozolol binds to the progesterone receptor. Immunocytochemical studies confirmed the presence of progesterone receptors on skin and synovial fibroblasts. However, progesterone failed to elicit any response with respect to collagenase production in either cell type. Nortestosterone, dexamethasone and 17 beta-oestradiol had no effect on binding of stanozolol to either cell type. These results indicate that the inhibition of DNA synthesis by stanozolol is elicited through the progesterone receptor. The effects of stanozolol on collagenase and PGE2 production are mediated by a different receptor, present on skin but not synovial fibroblasts, and as yet unidentified.
I scrapped this off of one of H.FPlex's posts on winstrol as well. For whatever it's worth, it does show the PR antagonist activity with stanozolol.
-X
Ellis AJ, Cawston TE, Mackie EJ.
Rheumatology Research Unit, Addenbrooke's Hospital, Cambridge, UK.
The anabolic steroid stanozolol stimulates the production of prostaglandin E2 (PGE2) and the matrix metalloproteinases collagenase and stromelysin in human skin fibroblasts but not in rheumatoid synovial fibroblasts. The basis for these differential responses was investigated at the levels of DNA synthesis and steroid receptor binding. Stanozolol inhibited fibroblast growth factor (FGF)-stimulated DNA synthesis in both the skin and synovial fibroblasts, showing that both cell types were capable of responding to the compound. Competitive binding assays indicated that stanozolol bound specifically to both the skin and synovial fibroblasts. Binding of stanozolol to both cell types could be partially displaced by progesterone, indicating that stanozolol binds to the progesterone receptor. Immunocytochemical studies confirmed the presence of progesterone receptors on skin and synovial fibroblasts. However, progesterone failed to elicit any response with respect to collagenase production in either cell type. Nortestosterone, dexamethasone and 17 beta-oestradiol had no effect on binding of stanozolol to either cell type. These results indicate that the inhibition of DNA synthesis by stanozolol is elicited through the progesterone receptor. The effects of stanozolol on collagenase and PGE2 production are mediated by a different receptor, present on skin but not synovial fibroblasts, and as yet unidentified.
I scrapped this off of one of H.FPlex's posts on winstrol as well. For whatever it's worth, it does show the PR antagonist activity with stanozolol.
-X
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