[Lotus]

This study found that more ER (estrogen receptors) subtypes are located in the butt as opposed to subcutaneous abdominal adipose tissue. (More research is needed to locate the missing ER subtypes for people wanting a bigger booty).




receptor subtypes alpha and beta in human adipose tissue: influences of adipose cell differentiation and fat depot localization.
Pedersen SB1, Bruun JM, Hube F, Kristensen K, Hauner H, Richelsen B.

Abstract
A novel ER-subtype, the ER-beta has recently been characterized in various tissues, furthermore five isoforms of the ER-beta are known (ER-beta1--ER-beta5). Using immunoblotting and real- time RT-PCR, ER-alpha and beta were studied in human adipose tissue. The expression of ER-alpha mRNA was equal in subcutaneous gluteal adipose tissue, subcutaneous abdominal and intra-abdominal adipose tissue, similar findings were obtained at the protein level. In contrast the amount of ER-beta1 (protein and mRNA) was significantly lower in intra-abdominal adipose tissue as compared with the subcutaneous adipose tissue (five-fold lower in women, P<0.005 and three-fold lower in men, P<0.005) whereas the expression of ER-beta4 and -beta5 mRNA isoforms were significantly higher in gluteal adipose tissue compared to subcutaneous abdominal adipose tissue. No significant gender differences in ER expression was detected in any of the fat depots investigated. During adipocyte differentiation the expression of ER-alpha, -beta4 and -beta5 mRNA declined, whereas, the expression of ER-beta1 mRNA was constant. In conclusion, the existence of ER-beta isoforms in human adipose tissue was demonstrated and the amount of these receptors was dependent upon fat depot localization, with much reduced expression of ER-beta1 in intra-abdominal adipose tissue compared to subcutaneous adipose tissue. These findings may indicate that estrogens could have differentiation and depot specific effects in human adipose tissue.

[Lotus]

A hypothesis to bigger boobs:

COX expression results in higher levels of prostaglandin E2 (PGE2), which in turn increases CYP19 mRNA & protein expression through increases in intracellular cyclic AMP levels.

[Lotus]

If we really want to blow the doors off aromatase we'd turn our attention to EGFR(epiderrmal growth factor), which sits of the outside of cells, and is esstetial part Mammary Gland Development. So, the question is " how come we don't know about it? ", my guess?.....its to F**kin complicated lol. I'll take at stab at it though: note the highlighted areas, I believe EGFR combined and inhibiting histone deacetylation (HDAC) while upregulating PGE2, should make for the strongest aromatase.......say what?, broad strokes of course, I'm still working on the rough edges as to how it translates to NBE. over stimulus concerns are top priority. In other words, if we can find away around the trouble spots, it lessens proliferation.


function of the epidermal growth factor receptor and erbB-2 during mammary gland morphogenesis.
Sebastian J1, Richards RG, Walker MP, Wiesen JF, Werb Z, Derynck R, Hom YK, Cunha GR, DiAugustine RP.
Author information
Abstract
The hormonal stimulation of mammary gland morphogenesis is believed to occur through growth factor receptor signaling pathways. To determine the importance of the epidermal growth factor receptor (EGFR) pathway, we examined extracts of inguinal mammary glands from prepubertal and pubertal mice for tyrosine-phosphorylated EGFR and other erbB receptors. Tyrosine phosphorylation of both EGFR and erbB-2 was detected in normal female BALB/c mice at 5-6 weeks of age, but not during the prepubertal stage, e.g., 24 days of age. Treatment of mice with estradiol or epidermal growth factor also stimulated the formation of mammary EGFR/erbB-2 phosphotyrosine. Waved-2 mice, which have impaired EGFR kinase activity, exhibited less mammary development than did wild-type (wt) mice when both were evaluated at 36 days of age. Because EGFR knockout (KO) mice die shortly after birth, glands from the newborns were implanted under the renal capsules of female nude mice. Under these conditions, extensive ductal growth was observed in mammary glands from wt animals; in contrast, glands from EGFR KO mice failed to grow beyond rudimentary structures. Tissue recombinants revealed that the wt fat pad supported the morphogenesis of EGFR KO epithelium, whereas the EGFR KO fat pad did not. Taken together, these data suggest that EGFR is essential for morphogenesis of the mammary ducts and functions during this period of mammary development as a heterodimer with erbB-2 in the mammary stroma.






http://www.intechopen.com/books/malignan...esotheliom

[Lotus]

Post: #3319 |
RE: Project X
Btw,

Green Tea - stimulates beta-receptors at fat cells to increase release of lipids into the bloodstream. why is this important?, 95-98% fatty acids are bound in the blood stream (similar to how hormones are), we needed something that displaces hormones and fatty acids, looks like green tea is up for the task.

[tanysquirrel]

in keeping with the thread, there are ERa receptors and ERb receptors, is there anywhere that lists which herbs are which? I havnt researched that yet.. perhaps I should

got this so far.. (hopefully its not a copy elsewhere).
http://www.ncbi.nlm.nih.gov/gene/2100/

Estrogen receptor alpha ERa is the growth receptor
Estrogen receptor beta ERb protects against cancer

Breast growth requires supplements that are pro ERa, having a good ratio of ERa to ERa is a proactive step in achieving normal growth vs malignant growth.

Botanical Modulation of Menopausal Symptoms: Mechanisms of Action?
https://www.thieme-connect.com/products/...32-1328187

ah nice! ty.. and here I have been fiddling around all day with ERa and ERb , ER1 and ER2 explorations

[Lotus]

The research doors are open huh?, chances are you'll find more related NBE/HrT in this thread as opposed to other places, I'll be adding my other research threads into this one, it might save you some time. You should look at stat5 protein, interleukin6, histone, carrier proteins, to name a few.

present study we show that caveolin-1 binds directly to ERalpha. This is part of the first part, which is party of the second part, (is that how it goes?) anyways, subcellular localization of COX-2 and caveolin-1 was determined.

J Biol Chem. 2001 Sep 14;276(37):34975-82. Epub 2001 Jun 29.

Colocalization and interaction of cyclooxygenase-2 with caveolin-1 in human fibroblasts.

Abstract
Results from our previous study suggest that cyclooxygenase-2 (COX-2) induced by phorbol 12-myristate 13-acetate (PMA) may be localized to caveolae-like structures (Liou, J.-Y., Shyue, S.-K., Tsai, M.-J., Chung, C.-L., Chu, K.-Y., and Wu, K. K. (2000) J. Biol. Chem. 275, 15314-15320). In this study, we determined subcellular localization of COX-2 and caveolin-1 by confocal microscopy. COX-2 in human foreskin fibroblasts stimulated by PMA (100 nm) or interleukin-1beta (1 ng/ml) for 6 h was localized to plasma membrane in addition to endoplasmic reticulum and nuclear envelope. Caveolin-1 was localized to plasma membrane, and image overlay showed colocalization of COX-2 with caveolin-1. This was confirmed by the presence of COX-2 and caveolin-1 in the detergent-insoluble membrane fraction of cells stimulated by PMA. Immunoprecipitation showed complex formation of COX-2 with caveolin-1 in a time-dependent manner. A larger quantity of COX-2 was complexed with caveolin-1 in PMA-treated than in interleukin-1beta-treated cells. Purified COX-2 complexed with glutathione S-transferase-fused caveolin-1, which was not inhibited by the scaffolding domain peptide. Caveolin-1-bound COX-2 was catalytically active, and its activity was not inhibited by the scaffolding domain peptide. These results suggest that COX-2 induced by PMA and interleukin-1beta is colocalized with caveolin-1 in the segregated caveolae compartment. Because caveolae are rich in signaling molecules, this COX-2 compartment may play an important role in diverse pathophysiological processes.
PMID: 11432874 [PubMed - indexed for MEDLINE]

[Marcy]

This chart is AWESOME! I'm really interested in exploring the rhubarb over the next few weeks. Ours is coming in heavy this spring. See if I can generate some growth action with some rhubarb sauce. Maybe even try some topical application. Thanks Lotus. Very helpful chart!

[tanysquirrel]

at this rate, we will all become certifiable (crazy) or endocrinologists!

I think I would look sexy in a lab coat and glasses (better a lab coat than a straight jacket). all this info make my head swirl.

[tanysquirrel]

if I recall right (think its in my acorn thread) Rhubarb also exhibits ability to kill cancer cells. quite an awesome little rhub

[Lotus]

Going beyond the typical norms of research we'd be looking at exactly how proteins can help protect against cancers and common illness. mTOR signaling and protein kinase is where we should be looking:

The phosphatidylinositol 3 kinase (PI3K) pathway is one of the major pathways modulating cell growth, proliferation, metabolism, survival, and angiogenesis.

Targeting PI3 kinase/AKT/mTOR signaling in cancer.
Review article
Sheppard K, et al. Crit Rev Oncog. 2012.
Show full citation
Abstract
The phosphatidylinositol 3 kinase (PI3K) pathway is one of the major pathways modulating cell growth, proliferation, metabolism, survival, and angiogenesis. Hyperactivation of this pathway is one of the most frequent occurrences in human cancer and is thus an obvious target for treatment of this disease. Currently there are 26 novel compounds targeting the PI3K pathway being assessed in more than 150 cancer-related clinical trials. Although this pathway is involved in many vital biologic functions, data emanating from these clinical trials indicate that these drugs are well tolerated. This review outlines the interaction of the PI3K pathway with other signaling cascades, highlights mechanisms involved in hyperactivation, discusses current therapeutics in cancer-related clinical trials that target this pathway, and, based on preclinical data, discusses possible leads on patient selection and combinational therapy, including targeting multiple components of the associated signaling network.

PMID 22471665 [PubMed - indexed for MEDLINE]