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Project X (hrt)

Question:

I was reading Lotus first plan of fenugreek, red clover, SP and PC....My plan will be Fenugreek, red clover and Reishi and maybe PC similar to hers...

Is 2400mg of Fenugreek, 500mg of Reishi, 375mg of red clover enough daily?
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(17-06-2017, 01:39 AM)Matida Wrote:  Question:

I was reading Lotus first plan of fenugreek, red clover, SP and PC....My plan will be Fenugreek, red clover and Reishi and maybe PC similar to hers...

Is 2400mg of Fenugreek, 500mg of Reishi, 375mg of red clover enough daily?

Everyone has different allergies and levels of tolerance.  I always start out at suggested label dose rates.  For instance, if RC is one cap per day, and that is say 1000mg, then that's what I would start with.  There maybe things a person has a different tolerance level or allergy that you may NEVER know.  I still think that is why my body did so well on such a small dosage of herbals.   When everyone else was doing 3000mg of PM, I was building breasts with 1200mg per day.  I also found out, that when using FG, I had to take it at a different time than I did my SP.  Otherwise, I got headaches, and skin rashes.  All I needed to do was to separate the 2 like 3 hours and I could tolerate it much better.

Strange, but true.  You just have to start slow, and listen to your own body.
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I now understand how highly organized molecules function inside the mitochondrial matrix, for instance: ATP (which stands for Adenosine Triphosphate) is the Energy Currency for Cells, but before I get into the science (which blows my mind) I must admit ignorance in my early NBE programs.....yup!, I didn't know any better back then  Rolleyes  but here I am now better prepared/informed and ready take on the science of NBE/hrt. 

Btw, only using 600 mg of fenugreek (with 50% saponins) works just fine:
Fenugreek increases estradiol 
http://www.breastnexus.com/showthread.php?tid=26172

Part of the reason (which I know believe) what makes fenugreek useful for NBE is how it works in stomach acid...the saponins (emulsifiers) in FG is mechanism for boosting estradiol in stomach acid, I'll follow up on that later though. 
 

How ATP Transfers Energy
Energy is usually liberated from the ATP molecule to do work in the cell by a reaction that removes one of the phosphate-oxygen groups, leaving adenosine diphosphate (ADP). When the ATP converts to ADP, the ATP is said to be spent. Then the ADP is usually immediately recycled in the mitochondria where it is recharged and comes out again as ATP. In the words of Trefil (1992, p. 93) “hooking and unhooking that last phosphate [on ATP] is what keeps the whole world operating.”

The enormous amount of activity that occurs inside each of the approximately one hundred trillion human cells is shown by the fact that at any instant each cell contains about one billion ATP molecules. This amount is sufficient for that cell’s needs for only a few minutes and must be rapidly recycled. Given a hundred trillion cells in the average male, about 10 to the 23rd power * or one sextillion ATP molecules normally exist in the body. For each ATP “the terminal phosphate is added and removed 3 times each minute” (Kornberg, 1989, p. 65).




The total human body content of ATP is only about 50 grams, which must be constantly recycled every day. The ultimate source of energy for constructing ATP is food; ATP is simply the carrier and regulation-storage unit of energy. The average daily intake of 2,500 food calories translates into a turnover of a whopping 180 kg (400 lbs) of ATP (Kornberg, 1989, p. 65).

The Structure of ATP
ATP contains the purine base adenine and the sugar ribose which together form the nucleoside adenosine. The basic building blocks used to construct ATP are carbon, hydrogen, nitrogen, oxygen, and phosphorus which are assembled in a complex that contains the number of subatomic parts equivalent to over 500 hydrogen atoms. One phosphate ester bond and two phosphate anhydride bonds hold the three phosphates (PO4) and the ribose together. The construction also contains a b-N glycoside bond holding the ribose and the adenine together.
https://www.trueorigin.org/atp.php

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I  believe I can now offer an explanation why bellies get bigger (for some) when using NBE/hrt. 


Mitochondrial respiration in subcutaneous and visceral adipose tissue from patients with morbid obesity
Kraunsøe R1, Boushel R, Hansen CN, Schjerling P, Qvortrup K, Støckel M, Mikines KJ, Dela F.
Author information

Erratum in
* J Physiol. 2010 Oct 15; 588(Pt 20):4055.
Abstract
Adipose tissue exerts important endocrine and metabolic functions in health and disease. Yet the bioenergetics of this tissue is not characterized in humans and possible regional differences are not elucidated. Using high resolution respirometry, mitochondrial respiration was quantified in human abdominal subcutaneous and intra-abdominal visceral (omentum majus) adipose tissue from biopsies obtained in 20 obese patients undergoing bariatric surgery. Mitochondrial DNA (mtDNA) and genomic DNA (gDNA) were determined by the PCR technique for estimation of mitochondrial density. Adipose tissue samples were permeabilized and respirometric measurements were performed in duplicate at 37 degrees C. Substrates (glutamate (G) + malate (M) + octanoyl carnitine (O) + succinate (S)) were added sequentially to provide electrons to complex I + II. ADP ((D)) for state 3 respiration was added after GM. Uncoupled respiration was measured after addition of FCCP. Visceral fat contained more mitochondria per milligram of tissue than subcutaneous fat, but the cells were smaller. Robust, stable oxygen fluxes were found in both tissues, and coupled state 3 (GMOS(D)) and uncoupled respiration were significantly (P < 0.05) higher in visceral (0.95 +/- 0.05 and 1.15 +/- 0.06 pmol O(2) s(1) mg(1), respectively) compared with subcutaneous (0.76 +/- 0.04 and 0.98 +/- 0.05 pmol O(2) s(1) mg(1), respectively) adipose tissue. Expressed per mtDNA, visceral adipose tissue had significantly (P < 0.05) lower mitochondrial respiration. Substrate control ratios were higher and uncoupling control ratio lower (P < 0.05) in visceral compared with subcutaneous adipose tissue. We conclude that visceral fat is bioenergetically more active and more sensitive to mitochondrial substrate supply than subcutaneous fat. Oxidative phosphorylation has a higher relative activity in visceral compared with subcutaneous adipose tissue.

So you see----visceral fat contains more mitochondrial matrix to make more fat from, and this can be completed as seen in billions of signals within minutes inside the mitochondrial matrix. So either burn the excess (energy) so it doesn't go to fat storage. Or....add a supplement that break down fats. 

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Why does breast growth fail/falter or disappear?....the reason (imo) is that it's lacking a vascular network, and without a current blood supply to new tissue (breast) disappears, and while this is a new explanation, it's not new in terms of science. Recently scientists have created a vascular network using a spinach leaf.....(simple amazing) see here:
https://www.sciencedaily.com/releases/20...152753.htm

And what this tells me is that new breast tissue needs to be of muscle....then a vascular network can be added (to muscle), the technology gets a little complicated but think in terms of when using breast pumps, like when breast tissue is expanded using static pressure it's pumping/pulling fats to expand fat cells, where pumping falters is not having a blood supply to keep the oxygen a float (so to speak), my answer would be to build a muscular structure for breast tissue, I know this works because I've been building muscle from my beginning days of NBE, it's a combination of a grab n' pull method to build strength in all the quadrants of the breast. And this is where ATP will help us build a cellular network (for example) for the energy needed to build new muscle, so go back and re-read up on ATP, pay note to this paragraph: 

" Adenylate kinase " requires an atom of magnesium—and this is one of the reasons why sufficient dietary magnesium is important.


Here's the home run (scratch that, it's the grand slam) to all this: 

Localized expression of aromatase in human vascular tissues.
Harada N1, Sasano H, Murakami H, Ohkuma T, Nagura H, Takagi Y.
Author information


Abstract
The atheroprotective effects of estrogen are well established and the presence of an estrogen receptor in vascular tissues has recently been reported. Therefore, we investigated the localization of the estrogen-producing enzyme aromatase in vascular tissues to assess the possible contribution of endocrine, paracrine, and autocrine modes of action. Aromatase was found in human vascular smooth muscle cells (SMCs) but not in endothelial cells on in situ hybridization. These observations were further supported by quantitative analysis of aromatase mRNA and the activity in 15 human vascular specimens. Only trace levels of expression were detected in the 3 infants examined, whereas 0.0088 to 0.0806 amol/ microg RNA of aromatase mRNA and 12.9 to 122.3 fmol. h-1. mg-1 protein of the activity were detected in 12 of the adult individuals. The switching of tissue-specific exon 1 of the human aromatase gene was also observed in some cases. Aromatase was found to be expressed only in cultured SMCs and not in cultured endothelial cells of human aorta and pulmonary artery and to be regulated through dexamethasone and the signaling pathways of protein kinase A and C. Study results revealed the localized expression of aromatase in vascular SMCs, which indicated a possible direct action of locally produced estrogen in an autocrine or paracrine manner, with possible cross talk between smooth muscle and endothelial cells.
PMID: 10364566
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"Why does breast growth fail/falter or disappear?....the reason (imo) is that it's lacking a vascular network, and without a current blood supply to new tissue (breast) disappears." 

Interesting.  However, I'm not entirely sold.  If this is the case, why do women who work out (especially if they lift) actually see a reduction in breast size?  If your theory holds, they should actually see larger breast size (and not simply a larger pectoral muscle which makes it seem like the breast is larger) because of their exercise which contributes to greater blood supply.  Looking at the anatomy of a breast, it seems like size is dependent on glandular development and fat storage, more than anything.  Maybe I'm totally wrong and you can put me in my proper place, Lotus.   Big Grin
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(22-06-2017, 05:02 AM)eloise614 Wrote:  "Why does breast growth fail/falter or disappear?....the reason (imo) is that it's lacking a vascular network, and without a current blood supply to new tissue (breast) disappears." 

Interesting.  However, I'm not entirely sold.  If this is the case, why do women who work out (especially if they lift) actually see a reduction in breast size?  If your theory holds, they should actually see larger breast size (and not simply a larger pectoral muscle which makes it seem like the breast is larger) because of their exercise which contributes to greater blood supply.  Looking at the anatomy of a breast, it seems like size is dependent on glandular development and fat storage, more than anything.  Maybe I'm totally wrong and you can put me in my proper place, Lotus.   Big Grin

My thought is, 1/2 or more of a real feminine breast is fat....  If you work out to the point of a lower BMI, then instead of D size breasts, your lucky to have an A size breast.  Hence many professional women weight lifters are some of the best clients of plastic surgeons.
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Speaking of ATP...

One supplement that ramps up ATP in a way that you can actually feel (perhaps even too much) is Propionyl-L-Carnitine. Having tried all the variations of carnitine, this one in particular (GPLC), can be a little overwhelming/over stimulating if not put to good use. I keep this one in mind in case I ever enter a rowing competition and don't plan on needing to sleep till the next day!

Propionyl L-carnitine increases cardiac efficiency in hypertrophied rat heart
https://www.ncbi.nlm.nih.gov/pubmed/8605952

ATP production and TCA activity are stimulated by propionyl-L-carnitine in the diabetic rat heart
https://www.ncbi.nlm.nih.gov/pubmed/18298127

Treating symptoms of “male menopause,” low levels of testosterone due to aging. Taking propionyl-L-carnitine by mouth in combination with acetyl-L-carnitine for six months seems to improve sexual performance, depression, and fatigue in older men. Taking this combination seems to work about as well as taking testosterone.
http://www.webmd.com/vitamins-supplements/ingredientmono-803-propionyl-l-carnitine.aspx?activeingredientid=803&activeingredientname=propionyl-l-carnitine

Speaking of Coleus Forskohlii

Some people take a combination of Coleus Forskohlii (naturally increase cyclic adenosine monophosphate (cAMP) levels) and Artichoke Extract (Phosphodiesterase-4 (PDE4) inhibitor), to improve memory and cognitive function.

Note that the standardized Forskolin can make bathroom visits a bit more intense.

Speaking of Fenugreek with 50% saponins

I used to take this (Swanson's version of Testofen) as a common stack among body builders who would include a standardized Stinging Nettle extract as necessary to help avoid resulting gynecomastia. The concern was that it would naturally result in increasing moobs without it or something similar.

Note that some find this supplement can make them a bit too aggressive (and not in a good way).

Just a few observations
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(22-06-2017, 05:02 AM)eloise614 Wrote:  "Why does breast growth fail/falter or disappear?....the reason (imo) is that it's lacking a vascular network, and without a current blood supply to new tissue (breast) disappears."  

Interesting.  However, I'm not entirely sold.  If this is the case, why do women who work out (especially if they lift) actually see a reduction in breast size?  

I doubt in that case breasts are to be the only area seeing a reduction of fat, meaning losing fat comes off all over. 

My point is breasts lose their integrity (cell shape and volume) for a number of reasons, I'm offering a supplemental theory. Maybe sustainable breast growth is a continuation of protein synthesis, which is the basic building blocks of DNA synthesis, here's some background on DNA.
https://www.ncbi.nlm.nih.gov/books/NBK22022/

My thought goes beyond protein synthesis though, meaning where and how is it activated in breasts?, the science is there tbh. One example is using the mTOR signaling pathway, and basically, Blush  mTOR (also known as a kinase) can activate Growth Hormones which stimulates protein synthesis....or more specific....milk proteins.
http://physiologyonline.physiology.org/content/21/5/362

Bile-salt-stimulated lipase in human milk: evidence for its synthesis in the lactating mammary gland.
https://www.ncbi.nlm.nih.gov/pubmed/3595844

Getting back to why breast growth falls short...think about it, if adding fat / building muscle / more collagen deposits / growth hormone and a vascular network can grow bigger boobs...well, why the hell not?...

Ask yourself, when fat is transferred to augment breast size (aka liposuction for breasts) why does only a portion of fat take? (succeed), perhaps if the above concept was advanced prior to fat transfer then the transfer rate of fat could be higher?.....just a theory. Based on evidence that vascular aromatase is in smooth muscle tissue via ER-a (estrogen receptors alpha) we know it'll have a hormone source for continued growth rate ...it's just developing the vascular network. 

Quote: Muscle growth occurs whenever the rate of muscle protein synthesis is greater than the rate of muscle protein breakdown.
http://www.unm.edu/~lkravitz/Article%20f...rowLK.html

.....what if a happy equilibrium (or homeostasis) between muscle protein synthesis vs. muscle protein breakdown can be achieved?.....
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Many thanks Aria and V.O.D, great points-advice and science. 

Carnitine Acyltransferase mediates the transmembrane exchange of fatty acyl-carnitine for carnitine, in other words, it (carnitine) is recycled many times over through the inner mitochondrial membrane...so maybe we don't need as much a dose as one thinks (for that reason). Some larger molecules can't make it through the inner mitochondrial membrane, but carnitine does, meaning through to the mitochondrial matrix....you know lol, where the real magic begins.  Wink

Lipid Catabolism: Fatty Acids & Triacylglycerols
http://www.rpi.edu/dept/bcbp/molbiochem/...m#carnpalm


Carnitine 
http://flipper.diff.org/app/pathways/Carnitine

Mammalian long-chain acyl-CoA synthetases.
Soupene E1Kuypers FA.
Author information

Abstract
Acyl-CoA synthetase enzymes are essential for de novo lipid synthesis, fatty acid catabolism, and remodeling of membranes. Activation of fatty acids requires a two-step reaction catalyzed by these enzymes. In the first step, an acyl-AMP intermediate is formed from ATP. AMP is then exchanged with CoA to produce the activated acyl-CoA. The release of AMP in this reaction defines the superfamily of AMP-forming enzymes. The length of the carbon chain of the fatty acid species defines the substrate specificity for the different acyl-CoA synthetases (ACS). On this basis, five sub-families of ACS have been characterized. The purpose of this review is to report on the large family of mammalian long-chain acyl-CoA synthetases (ACSL), which activate fatty acids with chain lengths of 12 to 20 carbon atoms. Five genes and several isoforms generated by alternative splicing have been identified and limited information is available on their localization. The structure of these membrane proteins has not been solved for the mammalian ACSLs but homology to a bacterial form, whose structure has been determined, points at specific structural features that are important for these enzymes across species. The bacterial form acts as a dimer and has a conserved short motif, called the fatty acid Gate domain, that seems to determine substrate specificity. We will discuss the characterization and identification of the different spliced isoforms, draw attention to the inconsistencies and errors in their annotations, and their cellular localizations. These membrane proteins act on membrane-bound substrates probably as homo- and as heterodimer complexes but have often been expressed as single recombinant isoforms, apparently purified as monomers and tested in Triton X-100 micelles. 
We will argue that such studies have failed to provide an accurate assessment of the activity and of the distinct function of these enzymes in mammalian cells.
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In this study treatment with P+PRL (progesterone + prolactin) initiated a synergistic response of 400 fold higher with the combination. When E (estrogen) was co- administered with (P + PRL) it suppressed the effect of P+ PRL. 

Seen here:
Estradiol Represses Prolactin-Induced Expression of Na+/Taurocholate Cotransporting Polypeptide in Liver Cells through Estrogen Receptor-α and Signal Transducers and Activators of Transcription 5a
http://press.endocrine.org/doi/10.1210/en.2003-0752?url_ver=Z39.88-2003&rfr_id=ori%3Arid%3Acrossref.org&rfr_dat=cr_pub%3Dpubmed&


My takeaway from the study is trying a combo PC (progesterone cream) with a MSM cream...which promotes a PRL pathway known as STAT5. I'd like to point (however) that the mouse mammary glands are very similar in structure and function to human mammary (attached study below). Anyways...the STAT5 family of proteins is pretty incredible...I wrote about it many times....MSM promotes this pathway. 

Prolactin induces SHP-2 association with Stat5, nuclear translocation, and binding to the beta-casein gene promoter in mammary cells.
Chughtai N1, Schimchowitsch S, Lebrun JJ, Ali S.
Author information

Abstract
The Src homology 2 (SH2) domain containing protein-tyrosine phosphatase SHP-2 contributes to prolactin receptor (PRLR) signal transduction to beta-casein gene promoter activation. We report for the first time that SHP-2 physically associates with the signal transducer and activator of transcription-5a (Stat5a), an important mediator of PRLR signaling to milk protein gene activation, in the mouse mammary HC11 and the human breast cancer T47D cells when stimulated with prolactin (PRL) and human growth hormone, respectively. In addition, overexpression studies indicate that the carboxyl-terminal SH2 domain of SHP-2 is required to maintain tyrosine phosphorylation of Stat5 and its interaction with SHP-2. Furthermore, we demonstrate by nuclear co-immunoprecipitation and indirect immunofluorescence studies that PRL stimulation of mammary cells leads to the nuclear translocation of SHP-2 as a complex with Stat5a. This process was found to involve the catalytic activity of the phosphatase. Finally, using the Stat5 GAS (gamma-activated sequence) element of the beta-casein gene promoter in electrophoretic mobility shift assays, we demonstrate that PRL induces the SHP-2-Stat5a complex to bind to DNA. The presence of the phosphatase in the protein-bound DNA complex was verified by using polyclonal antisera to SHP-2. Our studies indicate a tight physical and functional interaction between SHP2 and Stat5 required for regulation and perpetuation of PRL-mediated signaling in mammary cells and suggest a potential role for SHP-2 in the nucleus.



Mammary gland development—It’s not just about estrogen1 

Further evidence for convergence between the effects of P and PRL comes from various readouts of the response by MEC to this combination of hormones. In one approach, we administered all possible combinations of E, P, and PRL to sexually mature OVX mice and measured cellular proliferation 5 d later (Hovey et al., 2001). As expected, E alone increased MEC proliferation, whereas P or PRL alone had no effect. Consistent with their cooperative effect, treatment with P+PRL initiated a synergistic response such that cell division was 400- fold higher following treatment with this combination. Interestingly, when E was co- administered, it suppressed the effect of P+PRL, perhaps further highlighting an ability of P and PRL to function in-dependent of E. At the same time, there was proliferation in the adjacent MG stroma, although it remains unclear whether this response preceded or followed that in the epithelium. The synergistic response to P and PRL was also evident at the intracellular level through increased phosphorylation of the IR substrates 1 and 2 (Lee et al., 2003). Others have implicated additional local consequences that likely mediate the combined effects of P and PRL (Lee and Ormandy, 2012). 
https://www.ncbi.nlm.nih.gov/pmc/article...752091.pdf


The comparative pathology of human and mouse mammary glands.
Cardiff RD1, Wellings SR.
Author information

Department of Pathology and The Center for Comparative Medicine, University of California, Davis 95616, USA. rdcardiff@ucdavis.edu
Abstract
The mouse has emerged as a primary animal model for human breast cancer because the mammary glands of the two species are very similar in structure and function. In this regard the TDLU and LA have similar morphology. The mouse, infected by MMTV, develops "spontaneous" tumors with specific but limited tumor phenotypes. The advent of genetic manipulation has created transgenic mice that develop hyperplasias and tumors morphologically and cytochemically comparable to lesions in humans. Even experienced pathologists have difficulty distinguishing between lesions from the two species, and the morphological similarities support the utility of the mouse model in understanding human breast cancer. In this essay we review our experience with the histopathology of human and mouse mammary disease by comparing the normal gland with hyperplastic, dysplastic and neoplastic lesions of traditional and transgenic origin.
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Hi Lotus, You are a true inspiration. I wonder if You have timeline of Your wonderful breast growing?
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