[Roserose]

There's two versions, male and female (this is the female one), (sample illustration only- not a suggested program, for illustration only).

Please Check my program (sample)


Follicular Cycle
Ainterol PM - 500mg - 2x daily
Collagen - 2x times a daily
Vit D - 2000iu -1x daily total of 2000iu
Fish oil - 1000mg 3x daily
Coconut oil 1 tbsp daily

Mid Cycle?

Luteal Cycle
Fenugreek -610mg each -3x daily
Fennel - 480mg each - 2x daily
Dong Quai -565mg -2x daily
Dandelion - 525mg -1x daily
L-Tyrosine - 500mg 1x daily

Massages/Noogleberry

Exercise

Diet/Calories Per day

Other:
___________________


Age/weight (optional)
Bust:
Overbust:
Underbust:
Goal:

Hi Lotus may i know,

Why you dont include aromatase in the sample program? Is it because its not that essential in NbE program?

[Roserose]

I have posted new reply twice but it doesnt show up here, kinda weird.

Btw Lotus may i know why you dont include aromatase in the sample program in previous page? Is it because long term use of it have bad side effects as stated above?

[Lotus]

I have posted new reply twice but it doesnt show up here, kinda weird.

Btw Lotus may i know why you dont include aromatase in the sample program in previous page? Is it because long term use of it have bad side effects as stated above?

Hi Dfleurs,

It's a fictional program, I used this an illustration of how a program would appear when we get the new section(s) up and running.

Good catch.

[Lotus]

If I do a critique in that program I'd say it has some functional aromatase with coconut oil, vit D,

Amino acids in my opinion are pro-aromatase...... Cox inhibitors too

[Roserose]

Ah i see.

So about the not taking androgen in long term kind of freak me out a bit. But its actually quite essential in NBE program right?

[Lotus]

Ah i see.

So about the not taking androgen in long term kind of freak me out a bit. But its actually quite essential in NBE program right?

That has more to do if androgens are deprived for long periods. An example would be like depleting androgens, which is impossible. An extreme example would be in castration, you'd think that would elimante androgens, but it doesn't......adrenal androgens still would exist, but.....the androgen production is minor, and technically DHT would still exist too, but overlooked.

Androgen health in women is necessary, DHT is one big obstacle too. Ovaries are the largest producer of androgens, out of that is DHEA(s) is the king. But the androstenedione pathway (of DHEA) is easier for the aromatase enzyme to E2.

[Roserose]

Hmmmm so is reishi still good to take? i guess taking everything in moderation is always better but NBE is such a long journey thus everything will be kind of long term type

[-Clelia-]

well done Lotus, these findings about ER receptor, are very interesting! I need to study a bit, compare some studies, then I will come back here. Differences in physiology can explain different results with the same compound (ex. Genistein), also our receptors exist in "strong or weak version", then more ore less signal response to molecules. Moreover, there is 35% of population that has not the enzimatic process which converts and activate genisteine and daidzeine (they both need to cut off the glycone, to be active), this occurs in the gut. Phytoestrogen also act in opposite way, before and after menopause. I will report links later, because im using a mobile now. We need to make things clear, from the whole information. See you!

[Lotus]

What i do not understand up there underlined is:
why addiction of DHT didn't decrease gland morphology in adult mammary gland?
why affected just the midpuberty, retarding development?
maybe in the adult mammary gland, DHT in extra amount, is it converted in 3-diol? so it can neutralize is own androgenic effect? I don't know...maybe it's that back-door effect, but result is not estrogenic, otherwise mammary gland should have developed..

I could understand just flutamide action... in midpuberty should work less because of less presence of AR receptor. When AR receptors increase in post-puberty, the antagonism of them promote growing.

If we low DHT, we should mimic a bit flutamide action. And also, more testosterone will be converted in estradiol, as mentioned in your sign

Hi Clelia,

Hope you had a good weekend,

Sorry I jumped ahead a few spots, getting back to your question. 3b-diol does explain the back door response. I'm just wondering if there's a re-absorption response before being excreted?, (e.g. re-activate DHT, one more time) as seen with estrogen metabolites. I dunno?,

But in males it does seem that 3-diol has estrogen action (ER-b) in epithelia of efferent ductules and the epididymis. I'm going to post about 4-5 posts regarding this process (male ER-b) that I posted a few months ago if that's ok. If rather focus on mammary DHT's fine too, either way, there's much to solve with your help.

So what if there was way to influence an estrogen action in the Leydig cells since they already include estrogen receptors. Well, a pathway needs to be established. Here is one possible source, or could be a possible action.

Sperm, a source of estrogen
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1518866/
Environ Health Perspect. Oct 1995; 103(Suppl 7): 59–62.
PMCID: PMC1518866
Research Article
Sperm, a source of estrogen.

Other info: it's being researched already.

Estrogen signaling in testicular cells.

Aromatase transforms irreversibly androgens into estrogens and is present in the endoplasmic reticulum of various tissues including the mammalian testis. In rat all testicular cells except peritubular cells express aromatase. Indeed in adult rat germ cells (pachytene spermatocytes and round spermatids) we have demonstrated the presence of a functional aromatase (transcript, protein and biological activity) and the estrogen output is equivalent to that of Leydig cells. In addition in the adult rat, transcripts of aromatase vary according to the germ cell type and to the stages of seminiferous epithelium. By contrast with the androgen receptors mainly localized in somatic cells, estrogen receptors (ERs) are described in most of the testicular cells including germ cells. Moreover, besides the presence of high affinity ERα and/or ERβ, a rapid membrane effect has been recently reported and we demonstrated that GPR30 (a transmembrane intracellular estrogen receptor) is expressed in adult rat pachytene spermatocytes. Therefore estrogens through both GPR30 and ERα are able to activate the rapid EGFR/ERK/c-jun signaling cascade, which in turn triggers an apoptotic mitochondrial pathway involving an increase in Bax expression and a concomitant reduction of cyclin A1 and B1 gene levels. In another study in round spermatids of adult rat we have shown that the rapid membrane effect of estradiol is also efficient in controlling apoptosis and maturation / differentiation of these haploid germ cells. In man the presence of a biologically active aromatase and of estrogen receptors has been reported in Leydig cells, but also in immature germ cells and ejaculated spermatozoa. Thus the role of estrogen (intracrine, autocrine and / or paracrine) in spermatogenesis (proliferation, apoptosis, survival and maturation) and more generally, in male reproduction is now evidenced taking into account the simultaneous presence of a biologically active aromatase and the widespread distribution of estrogen receptors especially in haploid germ cells.

oK then I just have to ask...
Would men's sperm be a significant source of aromatase?

I think so, the study concluded that Leydig cells, germ cells, and seminiferous tubules all showed positive stains for aromatase. But it has to do more with the head (tip) of sperm.

I take that back, it's the tail that has the most aromatase and the head of the epididymis displays estrogen receptors where estrogen synthesis occurs.

Summary diagram of potential estrogen action in epithelia of efferent ductules and the epididymis. At least 4 potential pathways are considered. 1) testosterone (T) can enter the cell or be converted to E2 by aromatase (Arom) found in luminal sperm [54]. Testosterone binds AR and translocates into the nucleus, where it binds to AREs, on the promoter regions of genes with or without EREs. 2) E2 will either enter the cell, as did testosterone or bind the membrane ESR (mESR1). It remains controversial whether E2 binds GPR30 in the membrane [144] or collaborates with mESR1 to mediate epidermal growth factor receptor (EGFR) activation (nonclassical) of kinases and phosphorylation [180]. It is well known that E2 binds ESR1 and translocates into the nucleus for classical mediation of transcription through EREs and recruitment of numerous cofactor proteins (C1–3). It is unknown how AR and ESR1 compete for these cofactors, or what happens when the steroid balance is altered in a cell expressing both receptors. 3) The ESR1 can also be activated through phosphorylation and mediate transcription through the ERE. 4) It is well documented in other tissues that mESR1 binds E2, resulting in very rapid cell signaling [84, 175, 178]. This rapid steroid activity through the membrane receptor involves caveolin-1, G proteins, and the phosphorylation/dephosphorylation cascades, which mediate transcription either through the ESR1/ERE or other transcription factors (TF).
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071263/


I think we made an important step in solving the Estrogen action in Genetic Males and NBE.

Or a 67 yard field goal.

[Lotus]

Clelia,
The part of the re-absorption might come from Aldo-keto reductases (AKRs), what do you think?.
Example:

Type 3 3alpha-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2, aka-AKR acts solely as a reductase to convert 5alpha-dihydrotestosterone (DHT), a potent ligand for the AR

_____________________________________________

It's like deconstructing a model (call it a airplane model) that someone else built, only you're working in reverse to deconstruct right. Same applies here, you see a study that states 5 alpha reductase is reduced in the liver, now maybe this study was for cancer research or something similar. Let's take one of these studies,

Role of human type 3 3alpha-hydroxysteroid dehydrogenase (AKR1C2) in androgen metabolism of prostate cancer cells.

Aldo-keto reductases (AKRs) is another superfamily class of enzymes like the Cytochrome P450 enzyme super family, which are present in most tissues of the body, and play important roles in hormone synthesis and breakdown (including estrogen and testosterone synthesis and metabolism), cholesterol synthesis, and vitamin D metabolism. Cytochrome P450 enzymes also function to metabolize potentially toxic compounds, including drugs and products of endogenous metabolism such as bilirubin, principally in the liver.

AKRs are involved in the development and progression of many cancers, as well as chemotherapeutic drug resistance. AKR1B1 and AKR1B10 are overexpressed in tumors, such as liver, breast, and lung cancer. Several AKRs (AKR1A1, AKR1B10, and AKR1C1-3) are involved in tobacco-carcinogenesis, but they also catalyze the detoxication of nicotine derived nitrosamino ketones. In addition, AKR1C1-3 enzymes play a key role in the regulation of proliferative signaling in hormone dependent cancers.

So what they did in this study was to cut off the androgen synthesis to the receptors using another steroid , Four human aldo-keto reductases (AKRs) that belong to the AKR1C subfamily function in vitro as 3-keto-, 17-keto- and 20-ketosteroid reductases or as 3alpha-, 17beta- and 20alpha- hydroxysteroid oxidases to varying degrees. By acting as ketosteroid reductases or hydroxysteroid oxidases these AKRs can either convert potent sex hormones (androgens, estrogens and progestins) into their inactive metabolites or they can form potent hormones by catalyzing the reverse reaction. In this manner they may regulate occupancy and trans-activation of steroid hormone receptors.

In English, I want to find the link to activate AKR1c in the liver to shut off the androgen receptors therefore DHT never gets activated, simple right?.

Regulates access of 5alpha-DHT to the androgen receptor.

Abstract
Pairs of hydroxysteroid dehydrogenases (HSDs) govern ligand access to steroid receptors in target tissues and act as molecular switches. By acting as reductases or oxidases, HSDs convert potent ligands into their cognate inactive metabolites or vice versa. This pre-receptor regulation of steroid hormone action may have profound effects on hormonal response. We have identified the HSDs responsible for regulating ligand access to the androgen receptor (AR) in human prostate. Type 3 3alpha-hydroxysteroid dehydrogenase (aldo-keto reductase 1C2, aka-AKR acts solely as a reductase to convert 5alpha-dihydrotestosterone (DHT), a potent ligand for the AR (K(d)=10(-11)M for the AR), to the inactive androgen 3alpha-androstanediol (K(d)=10(-6)M for the AR); while RoDH like 3alpha-HSD (a short-chain dehydrogenase/reductase (SDR)) acts solely as an oxidase to convert 3alpha-androstanediol back to 5alpha-DHT. Our studies suggest that aldo-keto reductase (AKRs) and SDRs function as reductases and oxidases, respectively, to control ligand access to nuclear receptors.
http://www.ncbi.nlm.nih.gov/pubmed/17223255

Notice how Aldo-keto reductases (AKRs) position themselves between DHT and 3-diols, this is where the estrogenic action takes place. These actions of AKR1C's takes place in androgen metabolism of the prostate.

Aldo-keto reductases (AKRs) is another superfamily class of enzymes like the Cytochrome P450 enzyme super family.






Estrogen receptor β and 17β-hydroxysteroid dehydrogenase type 6, a growth regulatory pathway that is lost in prostate cancer

Estrogen receptor β (ERβ) is activated in the prostate by 5α-andros- tane-3β,17β-diol (3β-Adiol) where it exerts antiproliferative activity. The proliferative action of the androgen receptor is activated by 5α- dihydrotestosterone (DHT). Thus, prostate growth is governed by the balance between androgen receptor and ERβ activation. 3β- Adiol is a high-affinity ligand and agonist of ERβ and is derived from DHT by 3-keto reductase/3β-hydroxysteroid dehydrogenase en- zymes. Here, we demonstrate that, when it is expressed in living cells containing an estrogen response element-luciferase reporter, 17β-hydroxysteroid dehydrogenase type 6 (17βHSD6) converts the androgen DHT to the estrogen 3β-Adiol, and this leads to activation of the ERβ reporter. This conversion of DHT occurs at concentrations that are in the physiological range of this hormone in the prostate. Immunohistochemical analysis revealed that 17βHSD6 is expressed in ERβ-positive epithelial cells of the human prostate and that, in prostate cancers of Gleason grade higher than 3, both ERβ and 17βHSD6 are undetectable. Both proteins were present in benign prostatic hyperplasia samples. These observations reveal that for- mation of 3β-Adiol via 17βHSD6 from DHT is an important growth regulatory pathway that is lost in prostate cancer.

http://www.ncbi.nlm.nih.gov/pmc/articles...117772.pdf