[Lotus]

You might to skip this part, Caveolin 1 is coactivator of estrogen receptor alpha. (More onion parts). yeah ok lol, who thinks of this stuff right?.

A coactivator is a protein that increases gene expression by binding to an activator (or transcription factor) which contains a DNA binding domain. The coactivator is unable to bind DNA by itself.
http://en.m.wikipedia.org/wiki/Coactivator_(genetics)

Caveolin 1 has been shown to interact with Estrogen receptor alpha, Nitric oxide synthase 2A, Epidermal growth factor receptor, Androgen receptor.


Expression of caveolin-1 in the human mammary adenocarcinoma cell line MCF-7 causes ligand-independent concentration of oestrogen receptor alpha (ERalpha) in the nucleus, and potentiates ligand-independent and ligand-dependent transcription from an oestrogen response element-driven reporter gene. Furthermore, caveolin-1 co-immunoprecipitates with ERalpha [Schlegel, Wang, Katzenellenbogen, Pestell and Lisanti (1999) J. Biol. Chem. 274, 33551-33556]. In the present study we show that caveolin-1 binds directly to ERalpha. This interaction is mediated by residues 82-101 of caveolin-1 (i.e. the caveolin scaffolding domain) and residues 1-282 of ERalpha. The caveolin-binding domain of ERalpha includes the ligand-independent transactivation domain, activation function (AF)-1, but lacks the hormone-binding domain and the ligand-gated transactivation domain, AF-2. In co-transfection studies, caveolin-1 potentiates the transcriptional activation of ERalpha(1-282), a truncation mutant that has intact AF-1 and DNA-binding domains. Since AF-1 activity is regulated largely by phosphorylation we determined that co-expression with caveolin-1 increased the basal phosphorylation of ERalpha(1-282), but blocked the epidermal growth factor-dependent increase in phosphorylation. Indeed, caveolin-1 interacted with and potentiated the transactivation of an ERalpha mutant that cannot be phosphorylated by extracellular signal-regulated kinase (ERK)1/2 [ERalpha(Ser(118)-->Ala)]. Thus caveolin-1 is a novel ERalpha regulator that drives ERK1/2-independent phosphorylation and activation of AF-1.



Ligand-independent activation of oestrogen receptor alpha by caveolin-1
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1222136/

Caveolin
http://wikipedia.org/wiki/Caveolin_1

[Lotus]

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]

[The First Aria]

Quick, I am drowning. Throw me a rope, or a bone. It will go well with my head. (get it, bone head) hahaha, o.k., not funny. So what in Iowa does it all mean??? Eat corn, but not the silk??? WTF???? I feel like I just stepped into advance Calculus 201 and flunked 9th grade math...

[Lotus]

Quick, I am drowning. Throw me a rope, or a bone. It will go well with my head. (get it, bone head) hahaha, o.k., not funny. So what in Iowa does it all mean??? Eat corn, but not the silk??? WTF???? I feel like I just stepped into advance Calculus 201 and flunked 9th grade math...

Ah snap!, ask me something easy huh.

You'd have to go back here first to make any sense at all. There's too many parts to wrap it up in a bow. (Sorry)

The health benefits of phyto's are well documented (especially here). These intracellular pathways are very interesting to say the least. That fact that someone did these kinds of studies blows me away lol. The estrogen receptor bioavailability chart I listed on another thread ties into these two studies. Put them all together and you get the sense of a reality check of sorts on NBE. The takeaway is that this info explains why we have slow, or no growth at all for some. Plus, I would even go as far to say the same holds true for HRT, and that glaring fact was E2 wasn't strong at binding to ER-a (the growth receptor). Which explains why HRT is slow going too, which if I did HRT I'd add these things below, that's just my opinion though. Estradiol (E2) doesn't all get bound to the estrogen receptors. Consider this though, increased levels of phyto's block out the body's own "natural estrogens", I'd say that's something you can ill afford when trying to grow breasts.


I think the obvious choice is to balance herbs that are PRO-ER-a with ER-b (protective receptor). Turmeric, green tea, essential fatty acids, and certain phtyoestrogens. 5 ar inhibitors are still a viable choice, reishi binds to ER's, not sure which one yet. WP is still a good choice. New weapons are things like 17 beta HSD's, type 1 & 4, plus CYP19 is still a viable option considering the andro to estro pathway,(that backdoor pathway is yet to be tapped).

cAMP or "cyclic adenosine monophosphate" is another possible NBE tool. Imo cAMP ties into fatty acids/aromatase or in large part, cAMP delivers FA's to hormones. In other words increasing blood flow to the receptors increase their bioavailability. Forilskin comes to mind, but quite honestly I think fatty acids work quite the same way.

cAMP is a second messenger, used for intracellular signal transduction, such as transferring the effects of hormones like glucagon and adrenaline, which cannot get through the cell membrane. Its purposes include the activation of protein kinases and regulating the effects of adrenaline and glucagon. It is also used to regulate the passage of Ca2+ through ion channels.

cyclic adenosine monophosphate
http://psychology.wikia.com/wiki/Cyclic_...ophosphate

[ellacraig]

Quick, I am drowning. Throw me a rope, or a bone. It will go well with my head. (get it, bone head) hahaha, o.k., not funny. So what in Iowa does it all mean??? Eat corn, but not the silk??? WTF???? I feel like I just stepped into advance Calculus 201 and flunked 9th grade math...

I LIKE CORN...
I FAILED AT MATH TOO...

[Lotus]

How's this?

Eating protein rich foods will impove ER-a (boob growth) binding process.

Any Tuna fans?, (and that's not tuna fins)

[ellacraig]

How's this?

Eating protein rich foods will impove ER-a (boob growth) binding process.

Any Tuna fans?, (and that's not tuna fins)

Love TUNA. But its all supplied in cans with all that toxic lining in the cans that contributes towards BC. Cant win huh... *sobs*

I love tuna on rice, with fried onion and cheese grated over the top and some seasame seeds!

[Lotus]

Ok, foods like these then

Foods High in Branched-Chain Amino Acids

10 Foods High in Branched-Chain Amino Acids
Chicken, fish, eggs and beans contain branched-chain amino acids.

The branched-chain amino acids -- leucine, isoleucine and valine -- are three of the eight essential amino acids you must obtain through your diet. They share a similar branched shape, which sets them apart from other amino acids, but they’re still used to produce proteins in your body. They also fill roles that support your muscles. You can count on getting varying amounts of all three amino acids from protein-containing foods.

Benefits of Branched-Chain Amino Acids
The branched-chain amino acids, or BCAAs, are metabolized in your muscles, where they provide an important source of energy. They also promote protein synthesis in muscles and reduce exercise-induced muscle damage, according to an article in the September 2008 issue of the “Journal of Sports Medicine and Physical Fitness.” In a controlled study where men participated in an eight-week resistance training program, the group that took BCAA supplements gained more lean mass and lost more weight than men who did not take BCAAs, according to a report in the July 2009 issue of the “Journal of International Society of Sports Nutrition.”

Best Sources of BCAAs

The best sources of BCAAs are meat, chicken, fish, dairy products and eggs, reports NYU Langone Medical Center. As a guideline, you can figure on consuming about 1.7 grams of leucine and 1 gram each of isoleucine and valine from a 3-ounce serving of meat, poultry or fish or from 1/2 cup of cottage cheese. A cup of milk contains about half that amount. Whey protein is another good option for boosting your intake of BCAAs.

Plant-Based Choices
Soybeans, baked beans, lima beans, lentils, brown rice, whole wheat, corn and nuts such as almonds and cashews are good sources of branched-chain amino acids, reports the Huntington College of Health Sciences. Of all the plant-based foods, beans have the highest amount of total protein, so they're the best choice for BCAAs. One cup of vegetarian baked beans has about 1 gram of each of the BCAAs. By comparison, 1 cup of cooked brown rice and quinoa have 0.4 gram of leucine, 0.2 gram of isoleucine and 0.3 gram of valine.

Recommended Daily Intake

The recommended dietary allowance for leucine is 42 milligrams for every kilogram, or 2.2 pounds, of body weight. You should get 19 milligrams per kilogram of isoleucine and 24 milligrams per kilogram of valine. Healthy people can get enough BCAAs by consuming their RDA for total protein, which is 46 grams daily for women and 56 grams for men. If you’re sick or injured, you may need to boost your BCAA intake. Therapeutic dosages range from 1 gram to 5 grams daily, reports NYU Langone Medical Center, but talk to your health care provider if you have any concerns about your protein intake.

http://www.livestrong.com/article/286637...ino-acids/

[SarahSchilling]

Well, the poison lining leeches into some foods more than others.

Just don't ever eat canned tomatos!!!

[ellacraig]

Well, the poison lining leeches into some foods more than others.

Just don't ever eat canned tomatos!!!

Would the same apply to baked beans? I love organic baked beans. Is it an acid thing
They are the only canned foods I eat..